A thioredoxin domain-containing protein 12 from black rockfish Sebastes schlegelii: Responses to immune challenges and protection from apoptosis against oxidative stress
Thioredoxin (TXN) superfamily proteins are identified by the presence of a thioredoxin active site with a conserved CXXC active motif. TXN members are involved in a wide range of biochemical and biological functions including redox regulation, refolding of disulfide containing proteins, and regulati...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Thulasitha, William Shanthakumar [verfasserIn] |
|---|
| Format: |
E-Artikel |
|---|---|
| Sprache: |
Englisch |
| Erschienen: |
2016transfer abstract |
|---|
| Umfang: |
9 |
|---|
| Übergeordnetes Werk: |
Enthalten in: Monitoring land surface albedo and vegetation dynamics using high spatial and temporal resolution synthetic time series from Landsat and the MODIS BRDF/NBAR/albedo product - Wang, Zhuosen ELSEVIER, 2017, CBP : an international journal, London [u.a.] |
|---|---|
| Übergeordnetes Werk: |
volume:185 ; year:2016 ; pages:29-37 ; extent:9 |
| Links: |
|---|
| DOI / URN: |
10.1016/j.cbpc.2016.02.005 |
|---|
| Katalog-ID: |
ELV019121008 |
|---|
| LEADER | 01000caa a22002652 4500 | ||
|---|---|---|---|
| 001 | ELV019121008 | ||
| 003 | DE-627 | ||
| 005 | 20230625125343.0 | ||
| 007 | cr uuu---uuuuu | ||
| 008 | 180603s2016 xx |||||o 00| ||eng c | ||
| 024 | 7 | |a 10.1016/j.cbpc.2016.02.005 |2 doi | |
| 028 | 5 | 2 | |a GBVA2016005000001.pica |
| 035 | |a (DE-627)ELV019121008 | ||
| 035 | |a (ELSEVIER)S1532-0456(16)30021-7 | ||
| 040 | |a DE-627 |b ger |c DE-627 |e rakwb | ||
| 041 | |a eng | ||
| 082 | 0 | |a 610 | |
| 082 | 0 | 4 | |a 610 |q DE-600 |
| 082 | 0 | 4 | |a 550 |q VZ |
| 084 | |a KARTEN |q DE-1a |2 fid | ||
| 084 | |a 38.03 |2 bkl | ||
| 084 | |a 74.48 |2 bkl | ||
| 084 | |a 74.41 |2 bkl | ||
| 100 | 1 | |a Thulasitha, William Shanthakumar |e verfasserin |4 aut | |
| 245 | 1 | 0 | |a A thioredoxin domain-containing protein 12 from black rockfish Sebastes schlegelii: Responses to immune challenges and protection from apoptosis against oxidative stress |
| 264 | 1 | |c 2016transfer abstract | |
| 300 | |a 9 | ||
| 336 | |a nicht spezifiziert |b zzz |2 rdacontent | ||
| 337 | |a nicht spezifiziert |b z |2 rdamedia | ||
| 338 | |a nicht spezifiziert |b zu |2 rdacarrier | ||
| 520 | |a Thioredoxin (TXN) superfamily proteins are identified by the presence of a thioredoxin active site with a conserved CXXC active motif. TXN members are involved in a wide range of biochemical and biological functions including redox regulation, refolding of disulfide containing proteins, and regulation of transcription factors. In the present study, a thioredoxin domain-containing protein 12 was identified and characterized from black rockfish, Sebastes schlegelii (RfTXNDC12). The full length of RfTXNDC12 consists of a 522-bp coding region encoding a 173-amino acid protein. It has a 29-amino acid signal peptide and a single TXN active site with a consensus atypical WCGAC active motif. Multiple sequence alignment revealed that the active site is conserved among vertebrates. RfTXNDC12 shares highest identity with its Epinephelus coioides homolog. Transcriptional analysis revealed its ubiquitous expression in a wide range of tissues with the highest expression in the ovary. Immune challenges conducted with Streptococcus iniae and poly I:C caused upregulation of RfTXNDC12 transcript levels in gills and peripheral blood cells (PBCs), while lipopolysaccharide injection caused downregulation of RfTXNDC12 in gills and upregulation in PBCs. Similar to TXN, RfTXNDC12 exhibited insulin disulfide reducing activity. Interestingly, the recombinant protein showed significant protection of LNCaP cells against apoptosis induced by H2O2-mediated oxidative stress in a concentration dependent manner. Collectively, the present data indicate that RfTXNDC12 is a TXN superfamily member, which could function as a potential antioxidant enzyme and be involved in a defense mechanism against immune challenges. | ||
| 520 | |a Thioredoxin (TXN) superfamily proteins are identified by the presence of a thioredoxin active site with a conserved CXXC active motif. TXN members are involved in a wide range of biochemical and biological functions including redox regulation, refolding of disulfide containing proteins, and regulation of transcription factors. In the present study, a thioredoxin domain-containing protein 12 was identified and characterized from black rockfish, Sebastes schlegelii (RfTXNDC12). The full length of RfTXNDC12 consists of a 522-bp coding region encoding a 173-amino acid protein. It has a 29-amino acid signal peptide and a single TXN active site with a consensus atypical WCGAC active motif. Multiple sequence alignment revealed that the active site is conserved among vertebrates. RfTXNDC12 shares highest identity with its Epinephelus coioides homolog. Transcriptional analysis revealed its ubiquitous expression in a wide range of tissues with the highest expression in the ovary. Immune challenges conducted with Streptococcus iniae and poly I:C caused upregulation of RfTXNDC12 transcript levels in gills and peripheral blood cells (PBCs), while lipopolysaccharide injection caused downregulation of RfTXNDC12 in gills and upregulation in PBCs. Similar to TXN, RfTXNDC12 exhibited insulin disulfide reducing activity. Interestingly, the recombinant protein showed significant protection of LNCaP cells against apoptosis induced by H2O2-mediated oxidative stress in a concentration dependent manner. Collectively, the present data indicate that RfTXNDC12 is a TXN superfamily member, which could function as a potential antioxidant enzyme and be involved in a defense mechanism against immune challenges. | ||
| 700 | 1 | |a Umasuthan, Navaneethaiyer |4 oth | |
| 700 | 1 | |a Jayasooriya, R.G.P.T. |4 oth | |
| 700 | 1 | |a Noh, Jae Koo |4 oth | |
| 700 | 1 | |a Park, Hae-Chul |4 oth | |
| 700 | 1 | |a Lee, Jehee |4 oth | |
| 773 | 0 | 8 | |i Enthalten in |n Pergamon Press |a Wang, Zhuosen ELSEVIER |t Monitoring land surface albedo and vegetation dynamics using high spatial and temporal resolution synthetic time series from Landsat and the MODIS BRDF/NBAR/albedo product |d 2017 |d CBP : an international journal |g London [u.a.] |w (DE-627)ELV007784783 |
| 773 | 1 | 8 | |g volume:185 |g year:2016 |g pages:29-37 |g extent:9 |
| 856 | 4 | 0 | |u https://doi.org/10.1016/j.cbpc.2016.02.005 |3 Volltext |
| 912 | |a GBV_USEFLAG_U | ||
| 912 | |a GBV_ELV | ||
| 912 | |a SYSFLAG_U | ||
| 912 | |a FID-KARTEN | ||
| 912 | |a SSG-OPC-GGO | ||
| 912 | |a SSG-OPC-AST | ||
| 912 | |a SSG-OPC-GEO | ||
| 936 | b | k | |a 38.03 |j Methoden und Techniken der Geowissenschaften |q VZ |
| 936 | b | k | |a 74.48 |j Geoinformationssysteme |q VZ |
| 936 | b | k | |a 74.41 |j Luftaufnahmen |j Photogrammetrie |q VZ |
| 951 | |a AR | ||
| 952 | |d 185 |j 2016 |h 29-37 |g 9 | ||
| 953 | |2 045F |a 610 | ||
| author_variant |
w s t ws wst |
|---|---|
| matchkey_str |
thulasithawilliamshanthakumarumasuthanna:2016----:tirdxnoanotiigrti1fobakokiheatsclgliepnetimncalneadrtc |
| hierarchy_sort_str |
2016transfer abstract |
| bklnumber |
38.03 74.48 74.41 |
| publishDate |
2016 |
| allfields |
10.1016/j.cbpc.2016.02.005 doi GBVA2016005000001.pica (DE-627)ELV019121008 (ELSEVIER)S1532-0456(16)30021-7 DE-627 ger DE-627 rakwb eng 610 610 DE-600 550 VZ KARTEN DE-1a fid 38.03 bkl 74.48 bkl 74.41 bkl Thulasitha, William Shanthakumar verfasserin aut A thioredoxin domain-containing protein 12 from black rockfish Sebastes schlegelii: Responses to immune challenges and protection from apoptosis against oxidative stress 2016transfer abstract 9 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Thioredoxin (TXN) superfamily proteins are identified by the presence of a thioredoxin active site with a conserved CXXC active motif. TXN members are involved in a wide range of biochemical and biological functions including redox regulation, refolding of disulfide containing proteins, and regulation of transcription factors. In the present study, a thioredoxin domain-containing protein 12 was identified and characterized from black rockfish, Sebastes schlegelii (RfTXNDC12). The full length of RfTXNDC12 consists of a 522-bp coding region encoding a 173-amino acid protein. It has a 29-amino acid signal peptide and a single TXN active site with a consensus atypical WCGAC active motif. Multiple sequence alignment revealed that the active site is conserved among vertebrates. RfTXNDC12 shares highest identity with its Epinephelus coioides homolog. Transcriptional analysis revealed its ubiquitous expression in a wide range of tissues with the highest expression in the ovary. Immune challenges conducted with Streptococcus iniae and poly I:C caused upregulation of RfTXNDC12 transcript levels in gills and peripheral blood cells (PBCs), while lipopolysaccharide injection caused downregulation of RfTXNDC12 in gills and upregulation in PBCs. Similar to TXN, RfTXNDC12 exhibited insulin disulfide reducing activity. Interestingly, the recombinant protein showed significant protection of LNCaP cells against apoptosis induced by H2O2-mediated oxidative stress in a concentration dependent manner. Collectively, the present data indicate that RfTXNDC12 is a TXN superfamily member, which could function as a potential antioxidant enzyme and be involved in a defense mechanism against immune challenges. Thioredoxin (TXN) superfamily proteins are identified by the presence of a thioredoxin active site with a conserved CXXC active motif. TXN members are involved in a wide range of biochemical and biological functions including redox regulation, refolding of disulfide containing proteins, and regulation of transcription factors. In the present study, a thioredoxin domain-containing protein 12 was identified and characterized from black rockfish, Sebastes schlegelii (RfTXNDC12). The full length of RfTXNDC12 consists of a 522-bp coding region encoding a 173-amino acid protein. It has a 29-amino acid signal peptide and a single TXN active site with a consensus atypical WCGAC active motif. Multiple sequence alignment revealed that the active site is conserved among vertebrates. RfTXNDC12 shares highest identity with its Epinephelus coioides homolog. Transcriptional analysis revealed its ubiquitous expression in a wide range of tissues with the highest expression in the ovary. Immune challenges conducted with Streptococcus iniae and poly I:C caused upregulation of RfTXNDC12 transcript levels in gills and peripheral blood cells (PBCs), while lipopolysaccharide injection caused downregulation of RfTXNDC12 in gills and upregulation in PBCs. Similar to TXN, RfTXNDC12 exhibited insulin disulfide reducing activity. Interestingly, the recombinant protein showed significant protection of LNCaP cells against apoptosis induced by H2O2-mediated oxidative stress in a concentration dependent manner. Collectively, the present data indicate that RfTXNDC12 is a TXN superfamily member, which could function as a potential antioxidant enzyme and be involved in a defense mechanism against immune challenges. Umasuthan, Navaneethaiyer oth Jayasooriya, R.G.P.T. oth Noh, Jae Koo oth Park, Hae-Chul oth Lee, Jehee oth Enthalten in Pergamon Press Wang, Zhuosen ELSEVIER Monitoring land surface albedo and vegetation dynamics using high spatial and temporal resolution synthetic time series from Landsat and the MODIS BRDF/NBAR/albedo product 2017 CBP : an international journal London [u.a.] (DE-627)ELV007784783 volume:185 year:2016 pages:29-37 extent:9 https://doi.org/10.1016/j.cbpc.2016.02.005 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U FID-KARTEN SSG-OPC-GGO SSG-OPC-AST SSG-OPC-GEO 38.03 Methoden und Techniken der Geowissenschaften VZ 74.48 Geoinformationssysteme VZ 74.41 Luftaufnahmen Photogrammetrie VZ AR 185 2016 29-37 9 045F 610 |
| spelling |
10.1016/j.cbpc.2016.02.005 doi GBVA2016005000001.pica (DE-627)ELV019121008 (ELSEVIER)S1532-0456(16)30021-7 DE-627 ger DE-627 rakwb eng 610 610 DE-600 550 VZ KARTEN DE-1a fid 38.03 bkl 74.48 bkl 74.41 bkl Thulasitha, William Shanthakumar verfasserin aut A thioredoxin domain-containing protein 12 from black rockfish Sebastes schlegelii: Responses to immune challenges and protection from apoptosis against oxidative stress 2016transfer abstract 9 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Thioredoxin (TXN) superfamily proteins are identified by the presence of a thioredoxin active site with a conserved CXXC active motif. TXN members are involved in a wide range of biochemical and biological functions including redox regulation, refolding of disulfide containing proteins, and regulation of transcription factors. In the present study, a thioredoxin domain-containing protein 12 was identified and characterized from black rockfish, Sebastes schlegelii (RfTXNDC12). The full length of RfTXNDC12 consists of a 522-bp coding region encoding a 173-amino acid protein. It has a 29-amino acid signal peptide and a single TXN active site with a consensus atypical WCGAC active motif. Multiple sequence alignment revealed that the active site is conserved among vertebrates. RfTXNDC12 shares highest identity with its Epinephelus coioides homolog. Transcriptional analysis revealed its ubiquitous expression in a wide range of tissues with the highest expression in the ovary. Immune challenges conducted with Streptococcus iniae and poly I:C caused upregulation of RfTXNDC12 transcript levels in gills and peripheral blood cells (PBCs), while lipopolysaccharide injection caused downregulation of RfTXNDC12 in gills and upregulation in PBCs. Similar to TXN, RfTXNDC12 exhibited insulin disulfide reducing activity. Interestingly, the recombinant protein showed significant protection of LNCaP cells against apoptosis induced by H2O2-mediated oxidative stress in a concentration dependent manner. Collectively, the present data indicate that RfTXNDC12 is a TXN superfamily member, which could function as a potential antioxidant enzyme and be involved in a defense mechanism against immune challenges. Thioredoxin (TXN) superfamily proteins are identified by the presence of a thioredoxin active site with a conserved CXXC active motif. TXN members are involved in a wide range of biochemical and biological functions including redox regulation, refolding of disulfide containing proteins, and regulation of transcription factors. In the present study, a thioredoxin domain-containing protein 12 was identified and characterized from black rockfish, Sebastes schlegelii (RfTXNDC12). The full length of RfTXNDC12 consists of a 522-bp coding region encoding a 173-amino acid protein. It has a 29-amino acid signal peptide and a single TXN active site with a consensus atypical WCGAC active motif. Multiple sequence alignment revealed that the active site is conserved among vertebrates. RfTXNDC12 shares highest identity with its Epinephelus coioides homolog. Transcriptional analysis revealed its ubiquitous expression in a wide range of tissues with the highest expression in the ovary. Immune challenges conducted with Streptococcus iniae and poly I:C caused upregulation of RfTXNDC12 transcript levels in gills and peripheral blood cells (PBCs), while lipopolysaccharide injection caused downregulation of RfTXNDC12 in gills and upregulation in PBCs. Similar to TXN, RfTXNDC12 exhibited insulin disulfide reducing activity. Interestingly, the recombinant protein showed significant protection of LNCaP cells against apoptosis induced by H2O2-mediated oxidative stress in a concentration dependent manner. Collectively, the present data indicate that RfTXNDC12 is a TXN superfamily member, which could function as a potential antioxidant enzyme and be involved in a defense mechanism against immune challenges. Umasuthan, Navaneethaiyer oth Jayasooriya, R.G.P.T. oth Noh, Jae Koo oth Park, Hae-Chul oth Lee, Jehee oth Enthalten in Pergamon Press Wang, Zhuosen ELSEVIER Monitoring land surface albedo and vegetation dynamics using high spatial and temporal resolution synthetic time series from Landsat and the MODIS BRDF/NBAR/albedo product 2017 CBP : an international journal London [u.a.] (DE-627)ELV007784783 volume:185 year:2016 pages:29-37 extent:9 https://doi.org/10.1016/j.cbpc.2016.02.005 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U FID-KARTEN SSG-OPC-GGO SSG-OPC-AST SSG-OPC-GEO 38.03 Methoden und Techniken der Geowissenschaften VZ 74.48 Geoinformationssysteme VZ 74.41 Luftaufnahmen Photogrammetrie VZ AR 185 2016 29-37 9 045F 610 |
| allfields_unstemmed |
10.1016/j.cbpc.2016.02.005 doi GBVA2016005000001.pica (DE-627)ELV019121008 (ELSEVIER)S1532-0456(16)30021-7 DE-627 ger DE-627 rakwb eng 610 610 DE-600 550 VZ KARTEN DE-1a fid 38.03 bkl 74.48 bkl 74.41 bkl Thulasitha, William Shanthakumar verfasserin aut A thioredoxin domain-containing protein 12 from black rockfish Sebastes schlegelii: Responses to immune challenges and protection from apoptosis against oxidative stress 2016transfer abstract 9 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Thioredoxin (TXN) superfamily proteins are identified by the presence of a thioredoxin active site with a conserved CXXC active motif. TXN members are involved in a wide range of biochemical and biological functions including redox regulation, refolding of disulfide containing proteins, and regulation of transcription factors. In the present study, a thioredoxin domain-containing protein 12 was identified and characterized from black rockfish, Sebastes schlegelii (RfTXNDC12). The full length of RfTXNDC12 consists of a 522-bp coding region encoding a 173-amino acid protein. It has a 29-amino acid signal peptide and a single TXN active site with a consensus atypical WCGAC active motif. Multiple sequence alignment revealed that the active site is conserved among vertebrates. RfTXNDC12 shares highest identity with its Epinephelus coioides homolog. Transcriptional analysis revealed its ubiquitous expression in a wide range of tissues with the highest expression in the ovary. Immune challenges conducted with Streptococcus iniae and poly I:C caused upregulation of RfTXNDC12 transcript levels in gills and peripheral blood cells (PBCs), while lipopolysaccharide injection caused downregulation of RfTXNDC12 in gills and upregulation in PBCs. Similar to TXN, RfTXNDC12 exhibited insulin disulfide reducing activity. Interestingly, the recombinant protein showed significant protection of LNCaP cells against apoptosis induced by H2O2-mediated oxidative stress in a concentration dependent manner. Collectively, the present data indicate that RfTXNDC12 is a TXN superfamily member, which could function as a potential antioxidant enzyme and be involved in a defense mechanism against immune challenges. Thioredoxin (TXN) superfamily proteins are identified by the presence of a thioredoxin active site with a conserved CXXC active motif. TXN members are involved in a wide range of biochemical and biological functions including redox regulation, refolding of disulfide containing proteins, and regulation of transcription factors. In the present study, a thioredoxin domain-containing protein 12 was identified and characterized from black rockfish, Sebastes schlegelii (RfTXNDC12). The full length of RfTXNDC12 consists of a 522-bp coding region encoding a 173-amino acid protein. It has a 29-amino acid signal peptide and a single TXN active site with a consensus atypical WCGAC active motif. Multiple sequence alignment revealed that the active site is conserved among vertebrates. RfTXNDC12 shares highest identity with its Epinephelus coioides homolog. Transcriptional analysis revealed its ubiquitous expression in a wide range of tissues with the highest expression in the ovary. Immune challenges conducted with Streptococcus iniae and poly I:C caused upregulation of RfTXNDC12 transcript levels in gills and peripheral blood cells (PBCs), while lipopolysaccharide injection caused downregulation of RfTXNDC12 in gills and upregulation in PBCs. Similar to TXN, RfTXNDC12 exhibited insulin disulfide reducing activity. Interestingly, the recombinant protein showed significant protection of LNCaP cells against apoptosis induced by H2O2-mediated oxidative stress in a concentration dependent manner. Collectively, the present data indicate that RfTXNDC12 is a TXN superfamily member, which could function as a potential antioxidant enzyme and be involved in a defense mechanism against immune challenges. Umasuthan, Navaneethaiyer oth Jayasooriya, R.G.P.T. oth Noh, Jae Koo oth Park, Hae-Chul oth Lee, Jehee oth Enthalten in Pergamon Press Wang, Zhuosen ELSEVIER Monitoring land surface albedo and vegetation dynamics using high spatial and temporal resolution synthetic time series from Landsat and the MODIS BRDF/NBAR/albedo product 2017 CBP : an international journal London [u.a.] (DE-627)ELV007784783 volume:185 year:2016 pages:29-37 extent:9 https://doi.org/10.1016/j.cbpc.2016.02.005 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U FID-KARTEN SSG-OPC-GGO SSG-OPC-AST SSG-OPC-GEO 38.03 Methoden und Techniken der Geowissenschaften VZ 74.48 Geoinformationssysteme VZ 74.41 Luftaufnahmen Photogrammetrie VZ AR 185 2016 29-37 9 045F 610 |
| allfieldsGer |
10.1016/j.cbpc.2016.02.005 doi GBVA2016005000001.pica (DE-627)ELV019121008 (ELSEVIER)S1532-0456(16)30021-7 DE-627 ger DE-627 rakwb eng 610 610 DE-600 550 VZ KARTEN DE-1a fid 38.03 bkl 74.48 bkl 74.41 bkl Thulasitha, William Shanthakumar verfasserin aut A thioredoxin domain-containing protein 12 from black rockfish Sebastes schlegelii: Responses to immune challenges and protection from apoptosis against oxidative stress 2016transfer abstract 9 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Thioredoxin (TXN) superfamily proteins are identified by the presence of a thioredoxin active site with a conserved CXXC active motif. TXN members are involved in a wide range of biochemical and biological functions including redox regulation, refolding of disulfide containing proteins, and regulation of transcription factors. In the present study, a thioredoxin domain-containing protein 12 was identified and characterized from black rockfish, Sebastes schlegelii (RfTXNDC12). The full length of RfTXNDC12 consists of a 522-bp coding region encoding a 173-amino acid protein. It has a 29-amino acid signal peptide and a single TXN active site with a consensus atypical WCGAC active motif. Multiple sequence alignment revealed that the active site is conserved among vertebrates. RfTXNDC12 shares highest identity with its Epinephelus coioides homolog. Transcriptional analysis revealed its ubiquitous expression in a wide range of tissues with the highest expression in the ovary. Immune challenges conducted with Streptococcus iniae and poly I:C caused upregulation of RfTXNDC12 transcript levels in gills and peripheral blood cells (PBCs), while lipopolysaccharide injection caused downregulation of RfTXNDC12 in gills and upregulation in PBCs. Similar to TXN, RfTXNDC12 exhibited insulin disulfide reducing activity. Interestingly, the recombinant protein showed significant protection of LNCaP cells against apoptosis induced by H2O2-mediated oxidative stress in a concentration dependent manner. Collectively, the present data indicate that RfTXNDC12 is a TXN superfamily member, which could function as a potential antioxidant enzyme and be involved in a defense mechanism against immune challenges. Thioredoxin (TXN) superfamily proteins are identified by the presence of a thioredoxin active site with a conserved CXXC active motif. TXN members are involved in a wide range of biochemical and biological functions including redox regulation, refolding of disulfide containing proteins, and regulation of transcription factors. In the present study, a thioredoxin domain-containing protein 12 was identified and characterized from black rockfish, Sebastes schlegelii (RfTXNDC12). The full length of RfTXNDC12 consists of a 522-bp coding region encoding a 173-amino acid protein. It has a 29-amino acid signal peptide and a single TXN active site with a consensus atypical WCGAC active motif. Multiple sequence alignment revealed that the active site is conserved among vertebrates. RfTXNDC12 shares highest identity with its Epinephelus coioides homolog. Transcriptional analysis revealed its ubiquitous expression in a wide range of tissues with the highest expression in the ovary. Immune challenges conducted with Streptococcus iniae and poly I:C caused upregulation of RfTXNDC12 transcript levels in gills and peripheral blood cells (PBCs), while lipopolysaccharide injection caused downregulation of RfTXNDC12 in gills and upregulation in PBCs. Similar to TXN, RfTXNDC12 exhibited insulin disulfide reducing activity. Interestingly, the recombinant protein showed significant protection of LNCaP cells against apoptosis induced by H2O2-mediated oxidative stress in a concentration dependent manner. Collectively, the present data indicate that RfTXNDC12 is a TXN superfamily member, which could function as a potential antioxidant enzyme and be involved in a defense mechanism against immune challenges. Umasuthan, Navaneethaiyer oth Jayasooriya, R.G.P.T. oth Noh, Jae Koo oth Park, Hae-Chul oth Lee, Jehee oth Enthalten in Pergamon Press Wang, Zhuosen ELSEVIER Monitoring land surface albedo and vegetation dynamics using high spatial and temporal resolution synthetic time series from Landsat and the MODIS BRDF/NBAR/albedo product 2017 CBP : an international journal London [u.a.] (DE-627)ELV007784783 volume:185 year:2016 pages:29-37 extent:9 https://doi.org/10.1016/j.cbpc.2016.02.005 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U FID-KARTEN SSG-OPC-GGO SSG-OPC-AST SSG-OPC-GEO 38.03 Methoden und Techniken der Geowissenschaften VZ 74.48 Geoinformationssysteme VZ 74.41 Luftaufnahmen Photogrammetrie VZ AR 185 2016 29-37 9 045F 610 |
| allfieldsSound |
10.1016/j.cbpc.2016.02.005 doi GBVA2016005000001.pica (DE-627)ELV019121008 (ELSEVIER)S1532-0456(16)30021-7 DE-627 ger DE-627 rakwb eng 610 610 DE-600 550 VZ KARTEN DE-1a fid 38.03 bkl 74.48 bkl 74.41 bkl Thulasitha, William Shanthakumar verfasserin aut A thioredoxin domain-containing protein 12 from black rockfish Sebastes schlegelii: Responses to immune challenges and protection from apoptosis against oxidative stress 2016transfer abstract 9 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Thioredoxin (TXN) superfamily proteins are identified by the presence of a thioredoxin active site with a conserved CXXC active motif. TXN members are involved in a wide range of biochemical and biological functions including redox regulation, refolding of disulfide containing proteins, and regulation of transcription factors. In the present study, a thioredoxin domain-containing protein 12 was identified and characterized from black rockfish, Sebastes schlegelii (RfTXNDC12). The full length of RfTXNDC12 consists of a 522-bp coding region encoding a 173-amino acid protein. It has a 29-amino acid signal peptide and a single TXN active site with a consensus atypical WCGAC active motif. Multiple sequence alignment revealed that the active site is conserved among vertebrates. RfTXNDC12 shares highest identity with its Epinephelus coioides homolog. Transcriptional analysis revealed its ubiquitous expression in a wide range of tissues with the highest expression in the ovary. Immune challenges conducted with Streptococcus iniae and poly I:C caused upregulation of RfTXNDC12 transcript levels in gills and peripheral blood cells (PBCs), while lipopolysaccharide injection caused downregulation of RfTXNDC12 in gills and upregulation in PBCs. Similar to TXN, RfTXNDC12 exhibited insulin disulfide reducing activity. Interestingly, the recombinant protein showed significant protection of LNCaP cells against apoptosis induced by H2O2-mediated oxidative stress in a concentration dependent manner. Collectively, the present data indicate that RfTXNDC12 is a TXN superfamily member, which could function as a potential antioxidant enzyme and be involved in a defense mechanism against immune challenges. Thioredoxin (TXN) superfamily proteins are identified by the presence of a thioredoxin active site with a conserved CXXC active motif. TXN members are involved in a wide range of biochemical and biological functions including redox regulation, refolding of disulfide containing proteins, and regulation of transcription factors. In the present study, a thioredoxin domain-containing protein 12 was identified and characterized from black rockfish, Sebastes schlegelii (RfTXNDC12). The full length of RfTXNDC12 consists of a 522-bp coding region encoding a 173-amino acid protein. It has a 29-amino acid signal peptide and a single TXN active site with a consensus atypical WCGAC active motif. Multiple sequence alignment revealed that the active site is conserved among vertebrates. RfTXNDC12 shares highest identity with its Epinephelus coioides homolog. Transcriptional analysis revealed its ubiquitous expression in a wide range of tissues with the highest expression in the ovary. Immune challenges conducted with Streptococcus iniae and poly I:C caused upregulation of RfTXNDC12 transcript levels in gills and peripheral blood cells (PBCs), while lipopolysaccharide injection caused downregulation of RfTXNDC12 in gills and upregulation in PBCs. Similar to TXN, RfTXNDC12 exhibited insulin disulfide reducing activity. Interestingly, the recombinant protein showed significant protection of LNCaP cells against apoptosis induced by H2O2-mediated oxidative stress in a concentration dependent manner. Collectively, the present data indicate that RfTXNDC12 is a TXN superfamily member, which could function as a potential antioxidant enzyme and be involved in a defense mechanism against immune challenges. Umasuthan, Navaneethaiyer oth Jayasooriya, R.G.P.T. oth Noh, Jae Koo oth Park, Hae-Chul oth Lee, Jehee oth Enthalten in Pergamon Press Wang, Zhuosen ELSEVIER Monitoring land surface albedo and vegetation dynamics using high spatial and temporal resolution synthetic time series from Landsat and the MODIS BRDF/NBAR/albedo product 2017 CBP : an international journal London [u.a.] (DE-627)ELV007784783 volume:185 year:2016 pages:29-37 extent:9 https://doi.org/10.1016/j.cbpc.2016.02.005 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U FID-KARTEN SSG-OPC-GGO SSG-OPC-AST SSG-OPC-GEO 38.03 Methoden und Techniken der Geowissenschaften VZ 74.48 Geoinformationssysteme VZ 74.41 Luftaufnahmen Photogrammetrie VZ AR 185 2016 29-37 9 045F 610 |
| language |
English |
| source |
Enthalten in Monitoring land surface albedo and vegetation dynamics using high spatial and temporal resolution synthetic time series from Landsat and the MODIS BRDF/NBAR/albedo product London [u.a.] volume:185 year:2016 pages:29-37 extent:9 |
| sourceStr |
Enthalten in Monitoring land surface albedo and vegetation dynamics using high spatial and temporal resolution synthetic time series from Landsat and the MODIS BRDF/NBAR/albedo product London [u.a.] volume:185 year:2016 pages:29-37 extent:9 |
| format_phy_str_mv |
Article |
| bklname |
Methoden und Techniken der Geowissenschaften Geoinformationssysteme Luftaufnahmen Photogrammetrie |
| institution |
findex.gbv.de |
| dewey-raw |
610 |
| isfreeaccess_bool |
false |
| container_title |
Monitoring land surface albedo and vegetation dynamics using high spatial and temporal resolution synthetic time series from Landsat and the MODIS BRDF/NBAR/albedo product |
| authorswithroles_txt_mv |
Thulasitha, William Shanthakumar @@aut@@ Umasuthan, Navaneethaiyer @@oth@@ Jayasooriya, R.G.P.T. @@oth@@ Noh, Jae Koo @@oth@@ Park, Hae-Chul @@oth@@ Lee, Jehee @@oth@@ |
| publishDateDaySort_date |
2016-01-01T00:00:00Z |
| hierarchy_top_id |
ELV007784783 |
| dewey-sort |
3610 |
| id |
ELV019121008 |
| language_de |
englisch |
| fullrecord |
<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a22002652 4500</leader><controlfield tag="001">ELV019121008</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20230625125343.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">180603s2016 xx |||||o 00| ||eng c</controlfield><datafield tag="024" ind1="7" ind2=" "><subfield code="a">10.1016/j.cbpc.2016.02.005</subfield><subfield code="2">doi</subfield></datafield><datafield tag="028" ind1="5" ind2="2"><subfield code="a">GBVA2016005000001.pica</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)ELV019121008</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(ELSEVIER)S1532-0456(16)30021-7</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="041" ind1=" " ind2=" "><subfield code="a">eng</subfield></datafield><datafield tag="082" ind1="0" ind2=" "><subfield code="a">610</subfield></datafield><datafield tag="082" ind1="0" ind2="4"><subfield code="a">610</subfield><subfield code="q">DE-600</subfield></datafield><datafield tag="082" ind1="0" ind2="4"><subfield code="a">550</subfield><subfield code="q">VZ</subfield></datafield><datafield tag="084" ind1=" " ind2=" "><subfield code="a">KARTEN</subfield><subfield code="q">DE-1a</subfield><subfield code="2">fid</subfield></datafield><datafield tag="084" ind1=" " ind2=" "><subfield code="a">38.03</subfield><subfield code="2">bkl</subfield></datafield><datafield tag="084" ind1=" " ind2=" "><subfield code="a">74.48</subfield><subfield code="2">bkl</subfield></datafield><datafield tag="084" ind1=" " ind2=" "><subfield code="a">74.41</subfield><subfield code="2">bkl</subfield></datafield><datafield tag="100" ind1="1" ind2=" "><subfield code="a">Thulasitha, William Shanthakumar</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">A thioredoxin domain-containing protein 12 from black rockfish Sebastes schlegelii: Responses to immune challenges and protection from apoptosis against oxidative stress</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">2016transfer abstract</subfield></datafield><datafield tag="300" ind1=" " ind2=" "><subfield code="a">9</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zzz</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">z</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zu</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Thioredoxin (TXN) superfamily proteins are identified by the presence of a thioredoxin active site with a conserved CXXC active motif. TXN members are involved in a wide range of biochemical and biological functions including redox regulation, refolding of disulfide containing proteins, and regulation of transcription factors. In the present study, a thioredoxin domain-containing protein 12 was identified and characterized from black rockfish, Sebastes schlegelii (RfTXNDC12). The full length of RfTXNDC12 consists of a 522-bp coding region encoding a 173-amino acid protein. It has a 29-amino acid signal peptide and a single TXN active site with a consensus atypical WCGAC active motif. Multiple sequence alignment revealed that the active site is conserved among vertebrates. RfTXNDC12 shares highest identity with its Epinephelus coioides homolog. Transcriptional analysis revealed its ubiquitous expression in a wide range of tissues with the highest expression in the ovary. Immune challenges conducted with Streptococcus iniae and poly I:C caused upregulation of RfTXNDC12 transcript levels in gills and peripheral blood cells (PBCs), while lipopolysaccharide injection caused downregulation of RfTXNDC12 in gills and upregulation in PBCs. Similar to TXN, RfTXNDC12 exhibited insulin disulfide reducing activity. Interestingly, the recombinant protein showed significant protection of LNCaP cells against apoptosis induced by H2O2-mediated oxidative stress in a concentration dependent manner. Collectively, the present data indicate that RfTXNDC12 is a TXN superfamily member, which could function as a potential antioxidant enzyme and be involved in a defense mechanism against immune challenges.</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Thioredoxin (TXN) superfamily proteins are identified by the presence of a thioredoxin active site with a conserved CXXC active motif. TXN members are involved in a wide range of biochemical and biological functions including redox regulation, refolding of disulfide containing proteins, and regulation of transcription factors. In the present study, a thioredoxin domain-containing protein 12 was identified and characterized from black rockfish, Sebastes schlegelii (RfTXNDC12). The full length of RfTXNDC12 consists of a 522-bp coding region encoding a 173-amino acid protein. It has a 29-amino acid signal peptide and a single TXN active site with a consensus atypical WCGAC active motif. Multiple sequence alignment revealed that the active site is conserved among vertebrates. RfTXNDC12 shares highest identity with its Epinephelus coioides homolog. Transcriptional analysis revealed its ubiquitous expression in a wide range of tissues with the highest expression in the ovary. Immune challenges conducted with Streptococcus iniae and poly I:C caused upregulation of RfTXNDC12 transcript levels in gills and peripheral blood cells (PBCs), while lipopolysaccharide injection caused downregulation of RfTXNDC12 in gills and upregulation in PBCs. Similar to TXN, RfTXNDC12 exhibited insulin disulfide reducing activity. Interestingly, the recombinant protein showed significant protection of LNCaP cells against apoptosis induced by H2O2-mediated oxidative stress in a concentration dependent manner. Collectively, the present data indicate that RfTXNDC12 is a TXN superfamily member, which could function as a potential antioxidant enzyme and be involved in a defense mechanism against immune challenges.</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Umasuthan, Navaneethaiyer</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Jayasooriya, R.G.P.T.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Noh, Jae Koo</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Park, Hae-Chul</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Lee, Jehee</subfield><subfield code="4">oth</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">Enthalten in</subfield><subfield code="n">Pergamon Press</subfield><subfield code="a">Wang, Zhuosen ELSEVIER</subfield><subfield code="t">Monitoring land surface albedo and vegetation dynamics using high spatial and temporal resolution synthetic time series from Landsat and the MODIS BRDF/NBAR/albedo product</subfield><subfield code="d">2017</subfield><subfield code="d">CBP : an international journal</subfield><subfield code="g">London [u.a.]</subfield><subfield code="w">(DE-627)ELV007784783</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:185</subfield><subfield code="g">year:2016</subfield><subfield code="g">pages:29-37</subfield><subfield code="g">extent:9</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">https://doi.org/10.1016/j.cbpc.2016.02.005</subfield><subfield code="3">Volltext</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_U</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ELV</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SYSFLAG_U</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">FID-KARTEN</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OPC-GGO</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OPC-AST</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OPC-GEO</subfield></datafield><datafield tag="936" ind1="b" ind2="k"><subfield code="a">38.03</subfield><subfield code="j">Methoden und Techniken der Geowissenschaften</subfield><subfield code="q">VZ</subfield></datafield><datafield tag="936" ind1="b" ind2="k"><subfield code="a">74.48</subfield><subfield code="j">Geoinformationssysteme</subfield><subfield code="q">VZ</subfield></datafield><datafield tag="936" ind1="b" ind2="k"><subfield code="a">74.41</subfield><subfield code="j">Luftaufnahmen</subfield><subfield code="j">Photogrammetrie</subfield><subfield code="q">VZ</subfield></datafield><datafield tag="951" ind1=" " ind2=" "><subfield code="a">AR</subfield></datafield><datafield tag="952" ind1=" " ind2=" "><subfield code="d">185</subfield><subfield code="j">2016</subfield><subfield code="h">29-37</subfield><subfield code="g">9</subfield></datafield><datafield tag="953" ind1=" " ind2=" "><subfield code="2">045F</subfield><subfield code="a">610</subfield></datafield></record></collection>
|
| author |
Thulasitha, William Shanthakumar |
| spellingShingle |
Thulasitha, William Shanthakumar ddc 610 ddc 550 fid KARTEN bkl 38.03 bkl 74.48 bkl 74.41 A thioredoxin domain-containing protein 12 from black rockfish Sebastes schlegelii: Responses to immune challenges and protection from apoptosis against oxidative stress |
| authorStr |
Thulasitha, William Shanthakumar |
| ppnlink_with_tag_str_mv |
@@773@@(DE-627)ELV007784783 |
| format |
electronic Article |
| dewey-ones |
610 - Medicine & health 550 - Earth sciences |
| delete_txt_mv |
keep |
| author_role |
aut |
| collection |
elsevier |
| remote_str |
true |
| illustrated |
Not Illustrated |
| topic_title |
610 610 DE-600 550 VZ KARTEN DE-1a fid 38.03 bkl 74.48 bkl 74.41 bkl A thioredoxin domain-containing protein 12 from black rockfish Sebastes schlegelii: Responses to immune challenges and protection from apoptosis against oxidative stress |
| topic |
ddc 610 ddc 550 fid KARTEN bkl 38.03 bkl 74.48 bkl 74.41 |
| topic_unstemmed |
ddc 610 ddc 550 fid KARTEN bkl 38.03 bkl 74.48 bkl 74.41 |
| topic_browse |
ddc 610 ddc 550 fid KARTEN bkl 38.03 bkl 74.48 bkl 74.41 |
| format_facet |
Elektronische Aufsätze Aufsätze Elektronische Ressource |
| format_main_str_mv |
Text Zeitschrift/Artikel |
| carriertype_str_mv |
zu |
| author2_variant |
n u nu r j rj j k n jk jkn h c p hcp j l jl |
| hierarchy_parent_title |
Monitoring land surface albedo and vegetation dynamics using high spatial and temporal resolution synthetic time series from Landsat and the MODIS BRDF/NBAR/albedo product |
| hierarchy_parent_id |
ELV007784783 |
| dewey-tens |
610 - Medicine & health 550 - Earth sciences & geology |
| hierarchy_top_title |
Monitoring land surface albedo and vegetation dynamics using high spatial and temporal resolution synthetic time series from Landsat and the MODIS BRDF/NBAR/albedo product |
| isfreeaccess_txt |
false |
| familylinks_str_mv |
(DE-627)ELV007784783 |
| title |
A thioredoxin domain-containing protein 12 from black rockfish Sebastes schlegelii: Responses to immune challenges and protection from apoptosis against oxidative stress |
| ctrlnum |
(DE-627)ELV019121008 (ELSEVIER)S1532-0456(16)30021-7 |
| title_full |
A thioredoxin domain-containing protein 12 from black rockfish Sebastes schlegelii: Responses to immune challenges and protection from apoptosis against oxidative stress |
| author_sort |
Thulasitha, William Shanthakumar |
| journal |
Monitoring land surface albedo and vegetation dynamics using high spatial and temporal resolution synthetic time series from Landsat and the MODIS BRDF/NBAR/albedo product |
| journalStr |
Monitoring land surface albedo and vegetation dynamics using high spatial and temporal resolution synthetic time series from Landsat and the MODIS BRDF/NBAR/albedo product |
| lang_code |
eng |
| isOA_bool |
false |
| dewey-hundreds |
600 - Technology 500 - Science |
| recordtype |
marc |
| publishDateSort |
2016 |
| contenttype_str_mv |
zzz |
| container_start_page |
29 |
| author_browse |
Thulasitha, William Shanthakumar |
| container_volume |
185 |
| physical |
9 |
| class |
610 610 DE-600 550 VZ KARTEN DE-1a fid 38.03 bkl 74.48 bkl 74.41 bkl |
| format_se |
Elektronische Aufsätze |
| author-letter |
Thulasitha, William Shanthakumar |
| doi_str_mv |
10.1016/j.cbpc.2016.02.005 |
| dewey-full |
610 550 |
| title_sort |
a thioredoxin domain-containing protein 12 from black rockfish sebastes schlegelii: responses to immune challenges and protection from apoptosis against oxidative stress |
| title_auth |
A thioredoxin domain-containing protein 12 from black rockfish Sebastes schlegelii: Responses to immune challenges and protection from apoptosis against oxidative stress |
| abstract |
Thioredoxin (TXN) superfamily proteins are identified by the presence of a thioredoxin active site with a conserved CXXC active motif. TXN members are involved in a wide range of biochemical and biological functions including redox regulation, refolding of disulfide containing proteins, and regulation of transcription factors. In the present study, a thioredoxin domain-containing protein 12 was identified and characterized from black rockfish, Sebastes schlegelii (RfTXNDC12). The full length of RfTXNDC12 consists of a 522-bp coding region encoding a 173-amino acid protein. It has a 29-amino acid signal peptide and a single TXN active site with a consensus atypical WCGAC active motif. Multiple sequence alignment revealed that the active site is conserved among vertebrates. RfTXNDC12 shares highest identity with its Epinephelus coioides homolog. Transcriptional analysis revealed its ubiquitous expression in a wide range of tissues with the highest expression in the ovary. Immune challenges conducted with Streptococcus iniae and poly I:C caused upregulation of RfTXNDC12 transcript levels in gills and peripheral blood cells (PBCs), while lipopolysaccharide injection caused downregulation of RfTXNDC12 in gills and upregulation in PBCs. Similar to TXN, RfTXNDC12 exhibited insulin disulfide reducing activity. Interestingly, the recombinant protein showed significant protection of LNCaP cells against apoptosis induced by H2O2-mediated oxidative stress in a concentration dependent manner. Collectively, the present data indicate that RfTXNDC12 is a TXN superfamily member, which could function as a potential antioxidant enzyme and be involved in a defense mechanism against immune challenges. |
| abstractGer |
Thioredoxin (TXN) superfamily proteins are identified by the presence of a thioredoxin active site with a conserved CXXC active motif. TXN members are involved in a wide range of biochemical and biological functions including redox regulation, refolding of disulfide containing proteins, and regulation of transcription factors. In the present study, a thioredoxin domain-containing protein 12 was identified and characterized from black rockfish, Sebastes schlegelii (RfTXNDC12). The full length of RfTXNDC12 consists of a 522-bp coding region encoding a 173-amino acid protein. It has a 29-amino acid signal peptide and a single TXN active site with a consensus atypical WCGAC active motif. Multiple sequence alignment revealed that the active site is conserved among vertebrates. RfTXNDC12 shares highest identity with its Epinephelus coioides homolog. Transcriptional analysis revealed its ubiquitous expression in a wide range of tissues with the highest expression in the ovary. Immune challenges conducted with Streptococcus iniae and poly I:C caused upregulation of RfTXNDC12 transcript levels in gills and peripheral blood cells (PBCs), while lipopolysaccharide injection caused downregulation of RfTXNDC12 in gills and upregulation in PBCs. Similar to TXN, RfTXNDC12 exhibited insulin disulfide reducing activity. Interestingly, the recombinant protein showed significant protection of LNCaP cells against apoptosis induced by H2O2-mediated oxidative stress in a concentration dependent manner. Collectively, the present data indicate that RfTXNDC12 is a TXN superfamily member, which could function as a potential antioxidant enzyme and be involved in a defense mechanism against immune challenges. |
| abstract_unstemmed |
Thioredoxin (TXN) superfamily proteins are identified by the presence of a thioredoxin active site with a conserved CXXC active motif. TXN members are involved in a wide range of biochemical and biological functions including redox regulation, refolding of disulfide containing proteins, and regulation of transcription factors. In the present study, a thioredoxin domain-containing protein 12 was identified and characterized from black rockfish, Sebastes schlegelii (RfTXNDC12). The full length of RfTXNDC12 consists of a 522-bp coding region encoding a 173-amino acid protein. It has a 29-amino acid signal peptide and a single TXN active site with a consensus atypical WCGAC active motif. Multiple sequence alignment revealed that the active site is conserved among vertebrates. RfTXNDC12 shares highest identity with its Epinephelus coioides homolog. Transcriptional analysis revealed its ubiquitous expression in a wide range of tissues with the highest expression in the ovary. Immune challenges conducted with Streptococcus iniae and poly I:C caused upregulation of RfTXNDC12 transcript levels in gills and peripheral blood cells (PBCs), while lipopolysaccharide injection caused downregulation of RfTXNDC12 in gills and upregulation in PBCs. Similar to TXN, RfTXNDC12 exhibited insulin disulfide reducing activity. Interestingly, the recombinant protein showed significant protection of LNCaP cells against apoptosis induced by H2O2-mediated oxidative stress in a concentration dependent manner. Collectively, the present data indicate that RfTXNDC12 is a TXN superfamily member, which could function as a potential antioxidant enzyme and be involved in a defense mechanism against immune challenges. |
| collection_details |
GBV_USEFLAG_U GBV_ELV SYSFLAG_U FID-KARTEN SSG-OPC-GGO SSG-OPC-AST SSG-OPC-GEO |
| title_short |
A thioredoxin domain-containing protein 12 from black rockfish Sebastes schlegelii: Responses to immune challenges and protection from apoptosis against oxidative stress |
| url |
https://doi.org/10.1016/j.cbpc.2016.02.005 |
| remote_bool |
true |
| author2 |
Umasuthan, Navaneethaiyer Jayasooriya, R.G.P.T. Noh, Jae Koo Park, Hae-Chul Lee, Jehee |
| author2Str |
Umasuthan, Navaneethaiyer Jayasooriya, R.G.P.T. Noh, Jae Koo Park, Hae-Chul Lee, Jehee |
| ppnlink |
ELV007784783 |
| mediatype_str_mv |
z |
| isOA_txt |
false |
| hochschulschrift_bool |
false |
| author2_role |
oth oth oth oth oth |
| doi_str |
10.1016/j.cbpc.2016.02.005 |
| up_date |
2024-07-06T20:37:15.104Z |
| _version_ |
1803863442174509056 |
| fullrecord_marcxml |
<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a22002652 4500</leader><controlfield tag="001">ELV019121008</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20230625125343.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">180603s2016 xx |||||o 00| ||eng c</controlfield><datafield tag="024" ind1="7" ind2=" "><subfield code="a">10.1016/j.cbpc.2016.02.005</subfield><subfield code="2">doi</subfield></datafield><datafield tag="028" ind1="5" ind2="2"><subfield code="a">GBVA2016005000001.pica</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)ELV019121008</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(ELSEVIER)S1532-0456(16)30021-7</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="041" ind1=" " ind2=" "><subfield code="a">eng</subfield></datafield><datafield tag="082" ind1="0" ind2=" "><subfield code="a">610</subfield></datafield><datafield tag="082" ind1="0" ind2="4"><subfield code="a">610</subfield><subfield code="q">DE-600</subfield></datafield><datafield tag="082" ind1="0" ind2="4"><subfield code="a">550</subfield><subfield code="q">VZ</subfield></datafield><datafield tag="084" ind1=" " ind2=" "><subfield code="a">KARTEN</subfield><subfield code="q">DE-1a</subfield><subfield code="2">fid</subfield></datafield><datafield tag="084" ind1=" " ind2=" "><subfield code="a">38.03</subfield><subfield code="2">bkl</subfield></datafield><datafield tag="084" ind1=" " ind2=" "><subfield code="a">74.48</subfield><subfield code="2">bkl</subfield></datafield><datafield tag="084" ind1=" " ind2=" "><subfield code="a">74.41</subfield><subfield code="2">bkl</subfield></datafield><datafield tag="100" ind1="1" ind2=" "><subfield code="a">Thulasitha, William Shanthakumar</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">A thioredoxin domain-containing protein 12 from black rockfish Sebastes schlegelii: Responses to immune challenges and protection from apoptosis against oxidative stress</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">2016transfer abstract</subfield></datafield><datafield tag="300" ind1=" " ind2=" "><subfield code="a">9</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zzz</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">z</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zu</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Thioredoxin (TXN) superfamily proteins are identified by the presence of a thioredoxin active site with a conserved CXXC active motif. TXN members are involved in a wide range of biochemical and biological functions including redox regulation, refolding of disulfide containing proteins, and regulation of transcription factors. In the present study, a thioredoxin domain-containing protein 12 was identified and characterized from black rockfish, Sebastes schlegelii (RfTXNDC12). The full length of RfTXNDC12 consists of a 522-bp coding region encoding a 173-amino acid protein. It has a 29-amino acid signal peptide and a single TXN active site with a consensus atypical WCGAC active motif. Multiple sequence alignment revealed that the active site is conserved among vertebrates. RfTXNDC12 shares highest identity with its Epinephelus coioides homolog. Transcriptional analysis revealed its ubiquitous expression in a wide range of tissues with the highest expression in the ovary. Immune challenges conducted with Streptococcus iniae and poly I:C caused upregulation of RfTXNDC12 transcript levels in gills and peripheral blood cells (PBCs), while lipopolysaccharide injection caused downregulation of RfTXNDC12 in gills and upregulation in PBCs. Similar to TXN, RfTXNDC12 exhibited insulin disulfide reducing activity. Interestingly, the recombinant protein showed significant protection of LNCaP cells against apoptosis induced by H2O2-mediated oxidative stress in a concentration dependent manner. Collectively, the present data indicate that RfTXNDC12 is a TXN superfamily member, which could function as a potential antioxidant enzyme and be involved in a defense mechanism against immune challenges.</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Thioredoxin (TXN) superfamily proteins are identified by the presence of a thioredoxin active site with a conserved CXXC active motif. TXN members are involved in a wide range of biochemical and biological functions including redox regulation, refolding of disulfide containing proteins, and regulation of transcription factors. In the present study, a thioredoxin domain-containing protein 12 was identified and characterized from black rockfish, Sebastes schlegelii (RfTXNDC12). The full length of RfTXNDC12 consists of a 522-bp coding region encoding a 173-amino acid protein. It has a 29-amino acid signal peptide and a single TXN active site with a consensus atypical WCGAC active motif. Multiple sequence alignment revealed that the active site is conserved among vertebrates. RfTXNDC12 shares highest identity with its Epinephelus coioides homolog. Transcriptional analysis revealed its ubiquitous expression in a wide range of tissues with the highest expression in the ovary. Immune challenges conducted with Streptococcus iniae and poly I:C caused upregulation of RfTXNDC12 transcript levels in gills and peripheral blood cells (PBCs), while lipopolysaccharide injection caused downregulation of RfTXNDC12 in gills and upregulation in PBCs. Similar to TXN, RfTXNDC12 exhibited insulin disulfide reducing activity. Interestingly, the recombinant protein showed significant protection of LNCaP cells against apoptosis induced by H2O2-mediated oxidative stress in a concentration dependent manner. Collectively, the present data indicate that RfTXNDC12 is a TXN superfamily member, which could function as a potential antioxidant enzyme and be involved in a defense mechanism against immune challenges.</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Umasuthan, Navaneethaiyer</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Jayasooriya, R.G.P.T.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Noh, Jae Koo</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Park, Hae-Chul</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Lee, Jehee</subfield><subfield code="4">oth</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">Enthalten in</subfield><subfield code="n">Pergamon Press</subfield><subfield code="a">Wang, Zhuosen ELSEVIER</subfield><subfield code="t">Monitoring land surface albedo and vegetation dynamics using high spatial and temporal resolution synthetic time series from Landsat and the MODIS BRDF/NBAR/albedo product</subfield><subfield code="d">2017</subfield><subfield code="d">CBP : an international journal</subfield><subfield code="g">London [u.a.]</subfield><subfield code="w">(DE-627)ELV007784783</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:185</subfield><subfield code="g">year:2016</subfield><subfield code="g">pages:29-37</subfield><subfield code="g">extent:9</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">https://doi.org/10.1016/j.cbpc.2016.02.005</subfield><subfield code="3">Volltext</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_U</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ELV</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SYSFLAG_U</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">FID-KARTEN</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OPC-GGO</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OPC-AST</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OPC-GEO</subfield></datafield><datafield tag="936" ind1="b" ind2="k"><subfield code="a">38.03</subfield><subfield code="j">Methoden und Techniken der Geowissenschaften</subfield><subfield code="q">VZ</subfield></datafield><datafield tag="936" ind1="b" ind2="k"><subfield code="a">74.48</subfield><subfield code="j">Geoinformationssysteme</subfield><subfield code="q">VZ</subfield></datafield><datafield tag="936" ind1="b" ind2="k"><subfield code="a">74.41</subfield><subfield code="j">Luftaufnahmen</subfield><subfield code="j">Photogrammetrie</subfield><subfield code="q">VZ</subfield></datafield><datafield tag="951" ind1=" " ind2=" "><subfield code="a">AR</subfield></datafield><datafield tag="952" ind1=" " ind2=" "><subfield code="d">185</subfield><subfield code="j">2016</subfield><subfield code="h">29-37</subfield><subfield code="g">9</subfield></datafield><datafield tag="953" ind1=" " ind2=" "><subfield code="2">045F</subfield><subfield code="a">610</subfield></datafield></record></collection>
|
| score |
7.400255 |