Identification and functional characterization of amphioxus Miple, ancestral type of vertebrate midkine/pleiotrophin homologues
Midkine (MK) and pleiotrophin (PTN) are the only two members of heparin-binding growth factor family. MK/PTN homologues found from Drosophila to humans are shown to have antibacterial activities and their antibacterial domains are conserved during evolution. However, little is known about MK/PTN hom...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Gao, Zhan [verfasserIn] |
|---|
| Format: |
E-Artikel |
|---|---|
| Sprache: |
Englisch |
| Erschienen: |
2018transfer abstract |
|---|
| Schlagwörter: |
|---|
| Umfang: |
13 |
|---|
| Übergeordnetes Werk: |
Enthalten in: GABAergic mRNA expression is differentially expressed across the prelimbic and orbitofrontal cortices of rats sensitized to methamphetamine: Relevance to psychosis - Wearne, Travis A. ELSEVIER, 2016transfer abstract, ontogeny, phylogeny, aging : the official journal of the International Society of Developmental and Comparative Immunology, Amsterdam [u.a.] |
|---|---|
| Übergeordnetes Werk: |
volume:89 ; year:2018 ; pages:31-43 ; extent:13 |
| Links: |
|---|
| DOI / URN: |
10.1016/j.dci.2018.08.005 |
|---|
| Katalog-ID: |
ELV043941354 |
|---|
| LEADER | 01000caa a22002652 4500 | ||
|---|---|---|---|
| 001 | ELV043941354 | ||
| 003 | DE-627 | ||
| 005 | 20230626004403.0 | ||
| 007 | cr uuu---uuuuu | ||
| 008 | 181113s2018 xx |||||o 00| ||eng c | ||
| 024 | 7 | |a 10.1016/j.dci.2018.08.005 |2 doi | |
| 028 | 5 | 2 | |a /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000001061.pica |
| 035 | |a (DE-627)ELV043941354 | ||
| 035 | |a (ELSEVIER)S0145-305X(18)30350-1 | ||
| 040 | |a DE-627 |b ger |c DE-627 |e rakwb | ||
| 041 | |a eng | ||
| 082 | 0 | 4 | |a 610 |q VZ |
| 082 | 0 | 4 | |a 610 |q VZ |
| 084 | |a 44.88 |2 bkl | ||
| 100 | 1 | |a Gao, Zhan |e verfasserin |4 aut | |
| 245 | 1 | 0 | |a Identification and functional characterization of amphioxus Miple, ancestral type of vertebrate midkine/pleiotrophin homologues |
| 264 | 1 | |c 2018transfer abstract | |
| 300 | |a 13 | ||
| 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 Midkine (MK) and pleiotrophin (PTN) are the only two members of heparin-binding growth factor family. MK/PTN homologues found from Drosophila to humans are shown to have antibacterial activities and their antibacterial domains are conserved during evolution. However, little is known about MK/PTN homologue in the basal chordate amphioxus, and overall, information regarding MK/PTN homologues is rather limited in invertebrates. In this study, we identified a single MK/PTN homologue in Branchiostoma japonicum, termed BjMiple, which has a novel domain structure of PTN-PTNr1-PTNr2, and represents the ancestral form of vertebrate MK/PTN family proteins. BjMiple was expressed mainly in the ovary in a tissue-dependent fashion, and its expression was remarkably up-regulated following challenge with bacteria or their signature molecules LPS and LTA, suggesting its involvement in antibacterial responses. Functional assays revealed that BjMiple had strong antimicrobial activity, capable of killing a panel of Gram-negative and Gram-positive bacteria via a membranolytic mechanism, including interaction with bacterial membrane via LPS and LTA, membrane depolarization and high intracellular levels of ROS. Importantly, strong antibacterial activity was localized in PTN42-61 and PTNr142-66. Additionally, BjMiple and its derived peptides PTN42-61 and PTNr142-66 were not cytotoxic to human RBCs and mammalian cells. Taken together, our study suggests that amphioxus Miple is the ancestral type of vertebrate MK/PTN family homologues, and can play important roles as innate peptide antibiotics, which renders it a promising template for the design of novel peptide antibiotics against multi-drug resistant bacteria. | ||
| 520 | |a Midkine (MK) and pleiotrophin (PTN) are the only two members of heparin-binding growth factor family. MK/PTN homologues found from Drosophila to humans are shown to have antibacterial activities and their antibacterial domains are conserved during evolution. However, little is known about MK/PTN homologue in the basal chordate amphioxus, and overall, information regarding MK/PTN homologues is rather limited in invertebrates. In this study, we identified a single MK/PTN homologue in Branchiostoma japonicum, termed BjMiple, which has a novel domain structure of PTN-PTNr1-PTNr2, and represents the ancestral form of vertebrate MK/PTN family proteins. BjMiple was expressed mainly in the ovary in a tissue-dependent fashion, and its expression was remarkably up-regulated following challenge with bacteria or their signature molecules LPS and LTA, suggesting its involvement in antibacterial responses. Functional assays revealed that BjMiple had strong antimicrobial activity, capable of killing a panel of Gram-negative and Gram-positive bacteria via a membranolytic mechanism, including interaction with bacterial membrane via LPS and LTA, membrane depolarization and high intracellular levels of ROS. Importantly, strong antibacterial activity was localized in PTN42-61 and PTNr142-66. Additionally, BjMiple and its derived peptides PTN42-61 and PTNr142-66 were not cytotoxic to human RBCs and mammalian cells. Taken together, our study suggests that amphioxus Miple is the ancestral type of vertebrate MK/PTN family homologues, and can play important roles as innate peptide antibiotics, which renders it a promising template for the design of novel peptide antibiotics against multi-drug resistant bacteria. | ||
| 650 | 7 | |a Amphioxus |2 Elsevier | |
| 650 | 7 | |a Heparin-binding growth factor |2 Elsevier | |
| 650 | 7 | |a Pleiotrophin |2 Elsevier | |
| 650 | 7 | |a Branchiostoma |2 Elsevier | |
| 650 | 7 | |a Midkine |2 Elsevier | |
| 700 | 1 | |a Qu, Baozhen |4 oth | |
| 700 | 1 | |a Yao, Lan |4 oth | |
| 700 | 1 | |a Ma, Zengyu |4 oth | |
| 700 | 1 | |a Cui, Pengfei |4 oth | |
| 700 | 1 | |a Zhang, Shicui |4 oth | |
| 773 | 0 | 8 | |i Enthalten in |n Elsevier Science |a Wearne, Travis A. ELSEVIER |t GABAergic mRNA expression is differentially expressed across the prelimbic and orbitofrontal cortices of rats sensitized to methamphetamine: Relevance to psychosis |d 2016transfer abstract |d ontogeny, phylogeny, aging : the official journal of the International Society of Developmental and Comparative Immunology |g Amsterdam [u.a.] |w (DE-627)ELV019920881 |
| 773 | 1 | 8 | |g volume:89 |g year:2018 |g pages:31-43 |g extent:13 |
| 856 | 4 | 0 | |u https://doi.org/10.1016/j.dci.2018.08.005 |3 Volltext |
| 912 | |a GBV_USEFLAG_U | ||
| 912 | |a GBV_ELV | ||
| 912 | |a SYSFLAG_U | ||
| 912 | |a SSG-OLC-PHA | ||
| 912 | |a GBV_ILN_60 | ||
| 936 | b | k | |a 44.88 |j Urologie |j Nephrologie |q VZ |
| 951 | |a AR | ||
| 952 | |d 89 |j 2018 |h 31-43 |g 13 | ||
| author_variant |
z g zg |
|---|---|
| matchkey_str |
gaozhanqubaozhenyaolanmazengyucuipengfei:2018----:dniiainnfntoacaatrztooapixsilacsrlyefetbae |
| hierarchy_sort_str |
2018transfer abstract |
| bklnumber |
44.88 |
| publishDate |
2018 |
| allfields |
10.1016/j.dci.2018.08.005 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000001061.pica (DE-627)ELV043941354 (ELSEVIER)S0145-305X(18)30350-1 DE-627 ger DE-627 rakwb eng 610 VZ 610 VZ 44.88 bkl Gao, Zhan verfasserin aut Identification and functional characterization of amphioxus Miple, ancestral type of vertebrate midkine/pleiotrophin homologues 2018transfer abstract 13 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Midkine (MK) and pleiotrophin (PTN) are the only two members of heparin-binding growth factor family. MK/PTN homologues found from Drosophila to humans are shown to have antibacterial activities and their antibacterial domains are conserved during evolution. However, little is known about MK/PTN homologue in the basal chordate amphioxus, and overall, information regarding MK/PTN homologues is rather limited in invertebrates. In this study, we identified a single MK/PTN homologue in Branchiostoma japonicum, termed BjMiple, which has a novel domain structure of PTN-PTNr1-PTNr2, and represents the ancestral form of vertebrate MK/PTN family proteins. BjMiple was expressed mainly in the ovary in a tissue-dependent fashion, and its expression was remarkably up-regulated following challenge with bacteria or their signature molecules LPS and LTA, suggesting its involvement in antibacterial responses. Functional assays revealed that BjMiple had strong antimicrobial activity, capable of killing a panel of Gram-negative and Gram-positive bacteria via a membranolytic mechanism, including interaction with bacterial membrane via LPS and LTA, membrane depolarization and high intracellular levels of ROS. Importantly, strong antibacterial activity was localized in PTN42-61 and PTNr142-66. Additionally, BjMiple and its derived peptides PTN42-61 and PTNr142-66 were not cytotoxic to human RBCs and mammalian cells. Taken together, our study suggests that amphioxus Miple is the ancestral type of vertebrate MK/PTN family homologues, and can play important roles as innate peptide antibiotics, which renders it a promising template for the design of novel peptide antibiotics against multi-drug resistant bacteria. Midkine (MK) and pleiotrophin (PTN) are the only two members of heparin-binding growth factor family. MK/PTN homologues found from Drosophila to humans are shown to have antibacterial activities and their antibacterial domains are conserved during evolution. However, little is known about MK/PTN homologue in the basal chordate amphioxus, and overall, information regarding MK/PTN homologues is rather limited in invertebrates. In this study, we identified a single MK/PTN homologue in Branchiostoma japonicum, termed BjMiple, which has a novel domain structure of PTN-PTNr1-PTNr2, and represents the ancestral form of vertebrate MK/PTN family proteins. BjMiple was expressed mainly in the ovary in a tissue-dependent fashion, and its expression was remarkably up-regulated following challenge with bacteria or their signature molecules LPS and LTA, suggesting its involvement in antibacterial responses. Functional assays revealed that BjMiple had strong antimicrobial activity, capable of killing a panel of Gram-negative and Gram-positive bacteria via a membranolytic mechanism, including interaction with bacterial membrane via LPS and LTA, membrane depolarization and high intracellular levels of ROS. Importantly, strong antibacterial activity was localized in PTN42-61 and PTNr142-66. Additionally, BjMiple and its derived peptides PTN42-61 and PTNr142-66 were not cytotoxic to human RBCs and mammalian cells. Taken together, our study suggests that amphioxus Miple is the ancestral type of vertebrate MK/PTN family homologues, and can play important roles as innate peptide antibiotics, which renders it a promising template for the design of novel peptide antibiotics against multi-drug resistant bacteria. Amphioxus Elsevier Heparin-binding growth factor Elsevier Pleiotrophin Elsevier Branchiostoma Elsevier Midkine Elsevier Qu, Baozhen oth Yao, Lan oth Ma, Zengyu oth Cui, Pengfei oth Zhang, Shicui oth Enthalten in Elsevier Science Wearne, Travis A. ELSEVIER GABAergic mRNA expression is differentially expressed across the prelimbic and orbitofrontal cortices of rats sensitized to methamphetamine: Relevance to psychosis 2016transfer abstract ontogeny, phylogeny, aging : the official journal of the International Society of Developmental and Comparative Immunology Amsterdam [u.a.] (DE-627)ELV019920881 volume:89 year:2018 pages:31-43 extent:13 https://doi.org/10.1016/j.dci.2018.08.005 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA GBV_ILN_60 44.88 Urologie Nephrologie VZ AR 89 2018 31-43 13 |
| spelling |
10.1016/j.dci.2018.08.005 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000001061.pica (DE-627)ELV043941354 (ELSEVIER)S0145-305X(18)30350-1 DE-627 ger DE-627 rakwb eng 610 VZ 610 VZ 44.88 bkl Gao, Zhan verfasserin aut Identification and functional characterization of amphioxus Miple, ancestral type of vertebrate midkine/pleiotrophin homologues 2018transfer abstract 13 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Midkine (MK) and pleiotrophin (PTN) are the only two members of heparin-binding growth factor family. MK/PTN homologues found from Drosophila to humans are shown to have antibacterial activities and their antibacterial domains are conserved during evolution. However, little is known about MK/PTN homologue in the basal chordate amphioxus, and overall, information regarding MK/PTN homologues is rather limited in invertebrates. In this study, we identified a single MK/PTN homologue in Branchiostoma japonicum, termed BjMiple, which has a novel domain structure of PTN-PTNr1-PTNr2, and represents the ancestral form of vertebrate MK/PTN family proteins. BjMiple was expressed mainly in the ovary in a tissue-dependent fashion, and its expression was remarkably up-regulated following challenge with bacteria or their signature molecules LPS and LTA, suggesting its involvement in antibacterial responses. Functional assays revealed that BjMiple had strong antimicrobial activity, capable of killing a panel of Gram-negative and Gram-positive bacteria via a membranolytic mechanism, including interaction with bacterial membrane via LPS and LTA, membrane depolarization and high intracellular levels of ROS. Importantly, strong antibacterial activity was localized in PTN42-61 and PTNr142-66. Additionally, BjMiple and its derived peptides PTN42-61 and PTNr142-66 were not cytotoxic to human RBCs and mammalian cells. Taken together, our study suggests that amphioxus Miple is the ancestral type of vertebrate MK/PTN family homologues, and can play important roles as innate peptide antibiotics, which renders it a promising template for the design of novel peptide antibiotics against multi-drug resistant bacteria. Midkine (MK) and pleiotrophin (PTN) are the only two members of heparin-binding growth factor family. MK/PTN homologues found from Drosophila to humans are shown to have antibacterial activities and their antibacterial domains are conserved during evolution. However, little is known about MK/PTN homologue in the basal chordate amphioxus, and overall, information regarding MK/PTN homologues is rather limited in invertebrates. In this study, we identified a single MK/PTN homologue in Branchiostoma japonicum, termed BjMiple, which has a novel domain structure of PTN-PTNr1-PTNr2, and represents the ancestral form of vertebrate MK/PTN family proteins. BjMiple was expressed mainly in the ovary in a tissue-dependent fashion, and its expression was remarkably up-regulated following challenge with bacteria or their signature molecules LPS and LTA, suggesting its involvement in antibacterial responses. Functional assays revealed that BjMiple had strong antimicrobial activity, capable of killing a panel of Gram-negative and Gram-positive bacteria via a membranolytic mechanism, including interaction with bacterial membrane via LPS and LTA, membrane depolarization and high intracellular levels of ROS. Importantly, strong antibacterial activity was localized in PTN42-61 and PTNr142-66. Additionally, BjMiple and its derived peptides PTN42-61 and PTNr142-66 were not cytotoxic to human RBCs and mammalian cells. Taken together, our study suggests that amphioxus Miple is the ancestral type of vertebrate MK/PTN family homologues, and can play important roles as innate peptide antibiotics, which renders it a promising template for the design of novel peptide antibiotics against multi-drug resistant bacteria. Amphioxus Elsevier Heparin-binding growth factor Elsevier Pleiotrophin Elsevier Branchiostoma Elsevier Midkine Elsevier Qu, Baozhen oth Yao, Lan oth Ma, Zengyu oth Cui, Pengfei oth Zhang, Shicui oth Enthalten in Elsevier Science Wearne, Travis A. ELSEVIER GABAergic mRNA expression is differentially expressed across the prelimbic and orbitofrontal cortices of rats sensitized to methamphetamine: Relevance to psychosis 2016transfer abstract ontogeny, phylogeny, aging : the official journal of the International Society of Developmental and Comparative Immunology Amsterdam [u.a.] (DE-627)ELV019920881 volume:89 year:2018 pages:31-43 extent:13 https://doi.org/10.1016/j.dci.2018.08.005 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA GBV_ILN_60 44.88 Urologie Nephrologie VZ AR 89 2018 31-43 13 |
| allfields_unstemmed |
10.1016/j.dci.2018.08.005 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000001061.pica (DE-627)ELV043941354 (ELSEVIER)S0145-305X(18)30350-1 DE-627 ger DE-627 rakwb eng 610 VZ 610 VZ 44.88 bkl Gao, Zhan verfasserin aut Identification and functional characterization of amphioxus Miple, ancestral type of vertebrate midkine/pleiotrophin homologues 2018transfer abstract 13 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Midkine (MK) and pleiotrophin (PTN) are the only two members of heparin-binding growth factor family. MK/PTN homologues found from Drosophila to humans are shown to have antibacterial activities and their antibacterial domains are conserved during evolution. However, little is known about MK/PTN homologue in the basal chordate amphioxus, and overall, information regarding MK/PTN homologues is rather limited in invertebrates. In this study, we identified a single MK/PTN homologue in Branchiostoma japonicum, termed BjMiple, which has a novel domain structure of PTN-PTNr1-PTNr2, and represents the ancestral form of vertebrate MK/PTN family proteins. BjMiple was expressed mainly in the ovary in a tissue-dependent fashion, and its expression was remarkably up-regulated following challenge with bacteria or their signature molecules LPS and LTA, suggesting its involvement in antibacterial responses. Functional assays revealed that BjMiple had strong antimicrobial activity, capable of killing a panel of Gram-negative and Gram-positive bacteria via a membranolytic mechanism, including interaction with bacterial membrane via LPS and LTA, membrane depolarization and high intracellular levels of ROS. Importantly, strong antibacterial activity was localized in PTN42-61 and PTNr142-66. Additionally, BjMiple and its derived peptides PTN42-61 and PTNr142-66 were not cytotoxic to human RBCs and mammalian cells. Taken together, our study suggests that amphioxus Miple is the ancestral type of vertebrate MK/PTN family homologues, and can play important roles as innate peptide antibiotics, which renders it a promising template for the design of novel peptide antibiotics against multi-drug resistant bacteria. Midkine (MK) and pleiotrophin (PTN) are the only two members of heparin-binding growth factor family. MK/PTN homologues found from Drosophila to humans are shown to have antibacterial activities and their antibacterial domains are conserved during evolution. However, little is known about MK/PTN homologue in the basal chordate amphioxus, and overall, information regarding MK/PTN homologues is rather limited in invertebrates. In this study, we identified a single MK/PTN homologue in Branchiostoma japonicum, termed BjMiple, which has a novel domain structure of PTN-PTNr1-PTNr2, and represents the ancestral form of vertebrate MK/PTN family proteins. BjMiple was expressed mainly in the ovary in a tissue-dependent fashion, and its expression was remarkably up-regulated following challenge with bacteria or their signature molecules LPS and LTA, suggesting its involvement in antibacterial responses. Functional assays revealed that BjMiple had strong antimicrobial activity, capable of killing a panel of Gram-negative and Gram-positive bacteria via a membranolytic mechanism, including interaction with bacterial membrane via LPS and LTA, membrane depolarization and high intracellular levels of ROS. Importantly, strong antibacterial activity was localized in PTN42-61 and PTNr142-66. Additionally, BjMiple and its derived peptides PTN42-61 and PTNr142-66 were not cytotoxic to human RBCs and mammalian cells. Taken together, our study suggests that amphioxus Miple is the ancestral type of vertebrate MK/PTN family homologues, and can play important roles as innate peptide antibiotics, which renders it a promising template for the design of novel peptide antibiotics against multi-drug resistant bacteria. Amphioxus Elsevier Heparin-binding growth factor Elsevier Pleiotrophin Elsevier Branchiostoma Elsevier Midkine Elsevier Qu, Baozhen oth Yao, Lan oth Ma, Zengyu oth Cui, Pengfei oth Zhang, Shicui oth Enthalten in Elsevier Science Wearne, Travis A. ELSEVIER GABAergic mRNA expression is differentially expressed across the prelimbic and orbitofrontal cortices of rats sensitized to methamphetamine: Relevance to psychosis 2016transfer abstract ontogeny, phylogeny, aging : the official journal of the International Society of Developmental and Comparative Immunology Amsterdam [u.a.] (DE-627)ELV019920881 volume:89 year:2018 pages:31-43 extent:13 https://doi.org/10.1016/j.dci.2018.08.005 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA GBV_ILN_60 44.88 Urologie Nephrologie VZ AR 89 2018 31-43 13 |
| allfieldsGer |
10.1016/j.dci.2018.08.005 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000001061.pica (DE-627)ELV043941354 (ELSEVIER)S0145-305X(18)30350-1 DE-627 ger DE-627 rakwb eng 610 VZ 610 VZ 44.88 bkl Gao, Zhan verfasserin aut Identification and functional characterization of amphioxus Miple, ancestral type of vertebrate midkine/pleiotrophin homologues 2018transfer abstract 13 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Midkine (MK) and pleiotrophin (PTN) are the only two members of heparin-binding growth factor family. MK/PTN homologues found from Drosophila to humans are shown to have antibacterial activities and their antibacterial domains are conserved during evolution. However, little is known about MK/PTN homologue in the basal chordate amphioxus, and overall, information regarding MK/PTN homologues is rather limited in invertebrates. In this study, we identified a single MK/PTN homologue in Branchiostoma japonicum, termed BjMiple, which has a novel domain structure of PTN-PTNr1-PTNr2, and represents the ancestral form of vertebrate MK/PTN family proteins. BjMiple was expressed mainly in the ovary in a tissue-dependent fashion, and its expression was remarkably up-regulated following challenge with bacteria or their signature molecules LPS and LTA, suggesting its involvement in antibacterial responses. Functional assays revealed that BjMiple had strong antimicrobial activity, capable of killing a panel of Gram-negative and Gram-positive bacteria via a membranolytic mechanism, including interaction with bacterial membrane via LPS and LTA, membrane depolarization and high intracellular levels of ROS. Importantly, strong antibacterial activity was localized in PTN42-61 and PTNr142-66. Additionally, BjMiple and its derived peptides PTN42-61 and PTNr142-66 were not cytotoxic to human RBCs and mammalian cells. Taken together, our study suggests that amphioxus Miple is the ancestral type of vertebrate MK/PTN family homologues, and can play important roles as innate peptide antibiotics, which renders it a promising template for the design of novel peptide antibiotics against multi-drug resistant bacteria. Midkine (MK) and pleiotrophin (PTN) are the only two members of heparin-binding growth factor family. MK/PTN homologues found from Drosophila to humans are shown to have antibacterial activities and their antibacterial domains are conserved during evolution. However, little is known about MK/PTN homologue in the basal chordate amphioxus, and overall, information regarding MK/PTN homologues is rather limited in invertebrates. In this study, we identified a single MK/PTN homologue in Branchiostoma japonicum, termed BjMiple, which has a novel domain structure of PTN-PTNr1-PTNr2, and represents the ancestral form of vertebrate MK/PTN family proteins. BjMiple was expressed mainly in the ovary in a tissue-dependent fashion, and its expression was remarkably up-regulated following challenge with bacteria or their signature molecules LPS and LTA, suggesting its involvement in antibacterial responses. Functional assays revealed that BjMiple had strong antimicrobial activity, capable of killing a panel of Gram-negative and Gram-positive bacteria via a membranolytic mechanism, including interaction with bacterial membrane via LPS and LTA, membrane depolarization and high intracellular levels of ROS. Importantly, strong antibacterial activity was localized in PTN42-61 and PTNr142-66. Additionally, BjMiple and its derived peptides PTN42-61 and PTNr142-66 were not cytotoxic to human RBCs and mammalian cells. Taken together, our study suggests that amphioxus Miple is the ancestral type of vertebrate MK/PTN family homologues, and can play important roles as innate peptide antibiotics, which renders it a promising template for the design of novel peptide antibiotics against multi-drug resistant bacteria. Amphioxus Elsevier Heparin-binding growth factor Elsevier Pleiotrophin Elsevier Branchiostoma Elsevier Midkine Elsevier Qu, Baozhen oth Yao, Lan oth Ma, Zengyu oth Cui, Pengfei oth Zhang, Shicui oth Enthalten in Elsevier Science Wearne, Travis A. ELSEVIER GABAergic mRNA expression is differentially expressed across the prelimbic and orbitofrontal cortices of rats sensitized to methamphetamine: Relevance to psychosis 2016transfer abstract ontogeny, phylogeny, aging : the official journal of the International Society of Developmental and Comparative Immunology Amsterdam [u.a.] (DE-627)ELV019920881 volume:89 year:2018 pages:31-43 extent:13 https://doi.org/10.1016/j.dci.2018.08.005 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA GBV_ILN_60 44.88 Urologie Nephrologie VZ AR 89 2018 31-43 13 |
| allfieldsSound |
10.1016/j.dci.2018.08.005 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000001061.pica (DE-627)ELV043941354 (ELSEVIER)S0145-305X(18)30350-1 DE-627 ger DE-627 rakwb eng 610 VZ 610 VZ 44.88 bkl Gao, Zhan verfasserin aut Identification and functional characterization of amphioxus Miple, ancestral type of vertebrate midkine/pleiotrophin homologues 2018transfer abstract 13 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Midkine (MK) and pleiotrophin (PTN) are the only two members of heparin-binding growth factor family. MK/PTN homologues found from Drosophila to humans are shown to have antibacterial activities and their antibacterial domains are conserved during evolution. However, little is known about MK/PTN homologue in the basal chordate amphioxus, and overall, information regarding MK/PTN homologues is rather limited in invertebrates. In this study, we identified a single MK/PTN homologue in Branchiostoma japonicum, termed BjMiple, which has a novel domain structure of PTN-PTNr1-PTNr2, and represents the ancestral form of vertebrate MK/PTN family proteins. BjMiple was expressed mainly in the ovary in a tissue-dependent fashion, and its expression was remarkably up-regulated following challenge with bacteria or their signature molecules LPS and LTA, suggesting its involvement in antibacterial responses. Functional assays revealed that BjMiple had strong antimicrobial activity, capable of killing a panel of Gram-negative and Gram-positive bacteria via a membranolytic mechanism, including interaction with bacterial membrane via LPS and LTA, membrane depolarization and high intracellular levels of ROS. Importantly, strong antibacterial activity was localized in PTN42-61 and PTNr142-66. Additionally, BjMiple and its derived peptides PTN42-61 and PTNr142-66 were not cytotoxic to human RBCs and mammalian cells. Taken together, our study suggests that amphioxus Miple is the ancestral type of vertebrate MK/PTN family homologues, and can play important roles as innate peptide antibiotics, which renders it a promising template for the design of novel peptide antibiotics against multi-drug resistant bacteria. Midkine (MK) and pleiotrophin (PTN) are the only two members of heparin-binding growth factor family. MK/PTN homologues found from Drosophila to humans are shown to have antibacterial activities and their antibacterial domains are conserved during evolution. However, little is known about MK/PTN homologue in the basal chordate amphioxus, and overall, information regarding MK/PTN homologues is rather limited in invertebrates. In this study, we identified a single MK/PTN homologue in Branchiostoma japonicum, termed BjMiple, which has a novel domain structure of PTN-PTNr1-PTNr2, and represents the ancestral form of vertebrate MK/PTN family proteins. BjMiple was expressed mainly in the ovary in a tissue-dependent fashion, and its expression was remarkably up-regulated following challenge with bacteria or their signature molecules LPS and LTA, suggesting its involvement in antibacterial responses. Functional assays revealed that BjMiple had strong antimicrobial activity, capable of killing a panel of Gram-negative and Gram-positive bacteria via a membranolytic mechanism, including interaction with bacterial membrane via LPS and LTA, membrane depolarization and high intracellular levels of ROS. Importantly, strong antibacterial activity was localized in PTN42-61 and PTNr142-66. Additionally, BjMiple and its derived peptides PTN42-61 and PTNr142-66 were not cytotoxic to human RBCs and mammalian cells. Taken together, our study suggests that amphioxus Miple is the ancestral type of vertebrate MK/PTN family homologues, and can play important roles as innate peptide antibiotics, which renders it a promising template for the design of novel peptide antibiotics against multi-drug resistant bacteria. Amphioxus Elsevier Heparin-binding growth factor Elsevier Pleiotrophin Elsevier Branchiostoma Elsevier Midkine Elsevier Qu, Baozhen oth Yao, Lan oth Ma, Zengyu oth Cui, Pengfei oth Zhang, Shicui oth Enthalten in Elsevier Science Wearne, Travis A. ELSEVIER GABAergic mRNA expression is differentially expressed across the prelimbic and orbitofrontal cortices of rats sensitized to methamphetamine: Relevance to psychosis 2016transfer abstract ontogeny, phylogeny, aging : the official journal of the International Society of Developmental and Comparative Immunology Amsterdam [u.a.] (DE-627)ELV019920881 volume:89 year:2018 pages:31-43 extent:13 https://doi.org/10.1016/j.dci.2018.08.005 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA GBV_ILN_60 44.88 Urologie Nephrologie VZ AR 89 2018 31-43 13 |
| language |
English |
| source |
Enthalten in GABAergic mRNA expression is differentially expressed across the prelimbic and orbitofrontal cortices of rats sensitized to methamphetamine: Relevance to psychosis Amsterdam [u.a.] volume:89 year:2018 pages:31-43 extent:13 |
| sourceStr |
Enthalten in GABAergic mRNA expression is differentially expressed across the prelimbic and orbitofrontal cortices of rats sensitized to methamphetamine: Relevance to psychosis Amsterdam [u.a.] volume:89 year:2018 pages:31-43 extent:13 |
| format_phy_str_mv |
Article |
| bklname |
Urologie Nephrologie |
| institution |
findex.gbv.de |
| topic_facet |
Amphioxus Heparin-binding growth factor Pleiotrophin Branchiostoma Midkine |
| dewey-raw |
610 |
| isfreeaccess_bool |
false |
| container_title |
GABAergic mRNA expression is differentially expressed across the prelimbic and orbitofrontal cortices of rats sensitized to methamphetamine: Relevance to psychosis |
| authorswithroles_txt_mv |
Gao, Zhan @@aut@@ Qu, Baozhen @@oth@@ Yao, Lan @@oth@@ Ma, Zengyu @@oth@@ Cui, Pengfei @@oth@@ Zhang, Shicui @@oth@@ |
| publishDateDaySort_date |
2018-01-01T00:00:00Z |
| hierarchy_top_id |
ELV019920881 |
| dewey-sort |
3610 |
| id |
ELV043941354 |
| 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">ELV043941354</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20230626004403.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">181113s2018 xx |||||o 00| ||eng c</controlfield><datafield tag="024" ind1="7" ind2=" "><subfield code="a">10.1016/j.dci.2018.08.005</subfield><subfield code="2">doi</subfield></datafield><datafield tag="028" ind1="5" ind2="2"><subfield code="a">/cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000001061.pica</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)ELV043941354</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(ELSEVIER)S0145-305X(18)30350-1</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="4"><subfield code="a">610</subfield><subfield code="q">VZ</subfield></datafield><datafield tag="082" ind1="0" ind2="4"><subfield code="a">610</subfield><subfield code="q">VZ</subfield></datafield><datafield tag="084" ind1=" " ind2=" "><subfield code="a">44.88</subfield><subfield code="2">bkl</subfield></datafield><datafield tag="100" ind1="1" ind2=" "><subfield code="a">Gao, Zhan</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Identification and functional characterization of amphioxus Miple, ancestral type of vertebrate midkine/pleiotrophin homologues</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">2018transfer abstract</subfield></datafield><datafield tag="300" ind1=" " ind2=" "><subfield code="a">13</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">Midkine (MK) and pleiotrophin (PTN) are the only two members of heparin-binding growth factor family. MK/PTN homologues found from Drosophila to humans are shown to have antibacterial activities and their antibacterial domains are conserved during evolution. However, little is known about MK/PTN homologue in the basal chordate amphioxus, and overall, information regarding MK/PTN homologues is rather limited in invertebrates. In this study, we identified a single MK/PTN homologue in Branchiostoma japonicum, termed BjMiple, which has a novel domain structure of PTN-PTNr1-PTNr2, and represents the ancestral form of vertebrate MK/PTN family proteins. BjMiple was expressed mainly in the ovary in a tissue-dependent fashion, and its expression was remarkably up-regulated following challenge with bacteria or their signature molecules LPS and LTA, suggesting its involvement in antibacterial responses. Functional assays revealed that BjMiple had strong antimicrobial activity, capable of killing a panel of Gram-negative and Gram-positive bacteria via a membranolytic mechanism, including interaction with bacterial membrane via LPS and LTA, membrane depolarization and high intracellular levels of ROS. Importantly, strong antibacterial activity was localized in PTN42-61 and PTNr142-66. Additionally, BjMiple and its derived peptides PTN42-61 and PTNr142-66 were not cytotoxic to human RBCs and mammalian cells. Taken together, our study suggests that amphioxus Miple is the ancestral type of vertebrate MK/PTN family homologues, and can play important roles as innate peptide antibiotics, which renders it a promising template for the design of novel peptide antibiotics against multi-drug resistant bacteria.</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Midkine (MK) and pleiotrophin (PTN) are the only two members of heparin-binding growth factor family. MK/PTN homologues found from Drosophila to humans are shown to have antibacterial activities and their antibacterial domains are conserved during evolution. However, little is known about MK/PTN homologue in the basal chordate amphioxus, and overall, information regarding MK/PTN homologues is rather limited in invertebrates. In this study, we identified a single MK/PTN homologue in Branchiostoma japonicum, termed BjMiple, which has a novel domain structure of PTN-PTNr1-PTNr2, and represents the ancestral form of vertebrate MK/PTN family proteins. BjMiple was expressed mainly in the ovary in a tissue-dependent fashion, and its expression was remarkably up-regulated following challenge with bacteria or their signature molecules LPS and LTA, suggesting its involvement in antibacterial responses. Functional assays revealed that BjMiple had strong antimicrobial activity, capable of killing a panel of Gram-negative and Gram-positive bacteria via a membranolytic mechanism, including interaction with bacterial membrane via LPS and LTA, membrane depolarization and high intracellular levels of ROS. Importantly, strong antibacterial activity was localized in PTN42-61 and PTNr142-66. Additionally, BjMiple and its derived peptides PTN42-61 and PTNr142-66 were not cytotoxic to human RBCs and mammalian cells. Taken together, our study suggests that amphioxus Miple is the ancestral type of vertebrate MK/PTN family homologues, and can play important roles as innate peptide antibiotics, which renders it a promising template for the design of novel peptide antibiotics against multi-drug resistant bacteria.</subfield></datafield><datafield tag="650" ind1=" " ind2="7"><subfield code="a">Amphioxus</subfield><subfield code="2">Elsevier</subfield></datafield><datafield tag="650" ind1=" " ind2="7"><subfield code="a">Heparin-binding growth factor</subfield><subfield code="2">Elsevier</subfield></datafield><datafield tag="650" ind1=" " ind2="7"><subfield code="a">Pleiotrophin</subfield><subfield code="2">Elsevier</subfield></datafield><datafield tag="650" ind1=" " ind2="7"><subfield code="a">Branchiostoma</subfield><subfield code="2">Elsevier</subfield></datafield><datafield tag="650" ind1=" " ind2="7"><subfield code="a">Midkine</subfield><subfield code="2">Elsevier</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Qu, Baozhen</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Yao, Lan</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Ma, Zengyu</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Cui, Pengfei</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Zhang, Shicui</subfield><subfield code="4">oth</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">Enthalten in</subfield><subfield code="n">Elsevier Science</subfield><subfield code="a">Wearne, Travis A. ELSEVIER</subfield><subfield code="t">GABAergic mRNA expression is differentially expressed across the prelimbic and orbitofrontal cortices of rats sensitized to methamphetamine: Relevance to psychosis</subfield><subfield code="d">2016transfer abstract</subfield><subfield code="d">ontogeny, phylogeny, aging : the official journal of the International Society of Developmental and Comparative Immunology</subfield><subfield code="g">Amsterdam [u.a.]</subfield><subfield code="w">(DE-627)ELV019920881</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:89</subfield><subfield code="g">year:2018</subfield><subfield code="g">pages:31-43</subfield><subfield code="g">extent:13</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">https://doi.org/10.1016/j.dci.2018.08.005</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">SSG-OLC-PHA</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_60</subfield></datafield><datafield tag="936" ind1="b" ind2="k"><subfield code="a">44.88</subfield><subfield code="j">Urologie</subfield><subfield code="j">Nephrologie</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">89</subfield><subfield code="j">2018</subfield><subfield code="h">31-43</subfield><subfield code="g">13</subfield></datafield></record></collection>
|
| author |
Gao, Zhan |
| spellingShingle |
Gao, Zhan ddc 610 bkl 44.88 Elsevier Amphioxus Elsevier Heparin-binding growth factor Elsevier Pleiotrophin Elsevier Branchiostoma Elsevier Midkine Identification and functional characterization of amphioxus Miple, ancestral type of vertebrate midkine/pleiotrophin homologues |
| authorStr |
Gao, Zhan |
| ppnlink_with_tag_str_mv |
@@773@@(DE-627)ELV019920881 |
| format |
electronic Article |
| dewey-ones |
610 - Medicine & health |
| delete_txt_mv |
keep |
| author_role |
aut |
| collection |
elsevier |
| remote_str |
true |
| illustrated |
Not Illustrated |
| topic_title |
610 VZ 44.88 bkl Identification and functional characterization of amphioxus Miple, ancestral type of vertebrate midkine/pleiotrophin homologues Amphioxus Elsevier Heparin-binding growth factor Elsevier Pleiotrophin Elsevier Branchiostoma Elsevier Midkine Elsevier |
| topic |
ddc 610 bkl 44.88 Elsevier Amphioxus Elsevier Heparin-binding growth factor Elsevier Pleiotrophin Elsevier Branchiostoma Elsevier Midkine |
| topic_unstemmed |
ddc 610 bkl 44.88 Elsevier Amphioxus Elsevier Heparin-binding growth factor Elsevier Pleiotrophin Elsevier Branchiostoma Elsevier Midkine |
| topic_browse |
ddc 610 bkl 44.88 Elsevier Amphioxus Elsevier Heparin-binding growth factor Elsevier Pleiotrophin Elsevier Branchiostoma Elsevier Midkine |
| format_facet |
Elektronische Aufsätze Aufsätze Elektronische Ressource |
| format_main_str_mv |
Text Zeitschrift/Artikel |
| carriertype_str_mv |
zu |
| author2_variant |
b q bq l y ly z m zm p c pc s z sz |
| hierarchy_parent_title |
GABAergic mRNA expression is differentially expressed across the prelimbic and orbitofrontal cortices of rats sensitized to methamphetamine: Relevance to psychosis |
| hierarchy_parent_id |
ELV019920881 |
| dewey-tens |
610 - Medicine & health |
| hierarchy_top_title |
GABAergic mRNA expression is differentially expressed across the prelimbic and orbitofrontal cortices of rats sensitized to methamphetamine: Relevance to psychosis |
| isfreeaccess_txt |
false |
| familylinks_str_mv |
(DE-627)ELV019920881 |
| title |
Identification and functional characterization of amphioxus Miple, ancestral type of vertebrate midkine/pleiotrophin homologues |
| ctrlnum |
(DE-627)ELV043941354 (ELSEVIER)S0145-305X(18)30350-1 |
| title_full |
Identification and functional characterization of amphioxus Miple, ancestral type of vertebrate midkine/pleiotrophin homologues |
| author_sort |
Gao, Zhan |
| journal |
GABAergic mRNA expression is differentially expressed across the prelimbic and orbitofrontal cortices of rats sensitized to methamphetamine: Relevance to psychosis |
| journalStr |
GABAergic mRNA expression is differentially expressed across the prelimbic and orbitofrontal cortices of rats sensitized to methamphetamine: Relevance to psychosis |
| lang_code |
eng |
| isOA_bool |
false |
| dewey-hundreds |
600 - Technology |
| recordtype |
marc |
| publishDateSort |
2018 |
| contenttype_str_mv |
zzz |
| container_start_page |
31 |
| author_browse |
Gao, Zhan |
| container_volume |
89 |
| physical |
13 |
| class |
610 VZ 44.88 bkl |
| format_se |
Elektronische Aufsätze |
| author-letter |
Gao, Zhan |
| doi_str_mv |
10.1016/j.dci.2018.08.005 |
| dewey-full |
610 |
| title_sort |
identification and functional characterization of amphioxus miple, ancestral type of vertebrate midkine/pleiotrophin homologues |
| title_auth |
Identification and functional characterization of amphioxus Miple, ancestral type of vertebrate midkine/pleiotrophin homologues |
| abstract |
Midkine (MK) and pleiotrophin (PTN) are the only two members of heparin-binding growth factor family. MK/PTN homologues found from Drosophila to humans are shown to have antibacterial activities and their antibacterial domains are conserved during evolution. However, little is known about MK/PTN homologue in the basal chordate amphioxus, and overall, information regarding MK/PTN homologues is rather limited in invertebrates. In this study, we identified a single MK/PTN homologue in Branchiostoma japonicum, termed BjMiple, which has a novel domain structure of PTN-PTNr1-PTNr2, and represents the ancestral form of vertebrate MK/PTN family proteins. BjMiple was expressed mainly in the ovary in a tissue-dependent fashion, and its expression was remarkably up-regulated following challenge with bacteria or their signature molecules LPS and LTA, suggesting its involvement in antibacterial responses. Functional assays revealed that BjMiple had strong antimicrobial activity, capable of killing a panel of Gram-negative and Gram-positive bacteria via a membranolytic mechanism, including interaction with bacterial membrane via LPS and LTA, membrane depolarization and high intracellular levels of ROS. Importantly, strong antibacterial activity was localized in PTN42-61 and PTNr142-66. Additionally, BjMiple and its derived peptides PTN42-61 and PTNr142-66 were not cytotoxic to human RBCs and mammalian cells. Taken together, our study suggests that amphioxus Miple is the ancestral type of vertebrate MK/PTN family homologues, and can play important roles as innate peptide antibiotics, which renders it a promising template for the design of novel peptide antibiotics against multi-drug resistant bacteria. |
| abstractGer |
Midkine (MK) and pleiotrophin (PTN) are the only two members of heparin-binding growth factor family. MK/PTN homologues found from Drosophila to humans are shown to have antibacterial activities and their antibacterial domains are conserved during evolution. However, little is known about MK/PTN homologue in the basal chordate amphioxus, and overall, information regarding MK/PTN homologues is rather limited in invertebrates. In this study, we identified a single MK/PTN homologue in Branchiostoma japonicum, termed BjMiple, which has a novel domain structure of PTN-PTNr1-PTNr2, and represents the ancestral form of vertebrate MK/PTN family proteins. BjMiple was expressed mainly in the ovary in a tissue-dependent fashion, and its expression was remarkably up-regulated following challenge with bacteria or their signature molecules LPS and LTA, suggesting its involvement in antibacterial responses. Functional assays revealed that BjMiple had strong antimicrobial activity, capable of killing a panel of Gram-negative and Gram-positive bacteria via a membranolytic mechanism, including interaction with bacterial membrane via LPS and LTA, membrane depolarization and high intracellular levels of ROS. Importantly, strong antibacterial activity was localized in PTN42-61 and PTNr142-66. Additionally, BjMiple and its derived peptides PTN42-61 and PTNr142-66 were not cytotoxic to human RBCs and mammalian cells. Taken together, our study suggests that amphioxus Miple is the ancestral type of vertebrate MK/PTN family homologues, and can play important roles as innate peptide antibiotics, which renders it a promising template for the design of novel peptide antibiotics against multi-drug resistant bacteria. |
| abstract_unstemmed |
Midkine (MK) and pleiotrophin (PTN) are the only two members of heparin-binding growth factor family. MK/PTN homologues found from Drosophila to humans are shown to have antibacterial activities and their antibacterial domains are conserved during evolution. However, little is known about MK/PTN homologue in the basal chordate amphioxus, and overall, information regarding MK/PTN homologues is rather limited in invertebrates. In this study, we identified a single MK/PTN homologue in Branchiostoma japonicum, termed BjMiple, which has a novel domain structure of PTN-PTNr1-PTNr2, and represents the ancestral form of vertebrate MK/PTN family proteins. BjMiple was expressed mainly in the ovary in a tissue-dependent fashion, and its expression was remarkably up-regulated following challenge with bacteria or their signature molecules LPS and LTA, suggesting its involvement in antibacterial responses. Functional assays revealed that BjMiple had strong antimicrobial activity, capable of killing a panel of Gram-negative and Gram-positive bacteria via a membranolytic mechanism, including interaction with bacterial membrane via LPS and LTA, membrane depolarization and high intracellular levels of ROS. Importantly, strong antibacterial activity was localized in PTN42-61 and PTNr142-66. Additionally, BjMiple and its derived peptides PTN42-61 and PTNr142-66 were not cytotoxic to human RBCs and mammalian cells. Taken together, our study suggests that amphioxus Miple is the ancestral type of vertebrate MK/PTN family homologues, and can play important roles as innate peptide antibiotics, which renders it a promising template for the design of novel peptide antibiotics against multi-drug resistant bacteria. |
| collection_details |
GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA GBV_ILN_60 |
| title_short |
Identification and functional characterization of amphioxus Miple, ancestral type of vertebrate midkine/pleiotrophin homologues |
| url |
https://doi.org/10.1016/j.dci.2018.08.005 |
| remote_bool |
true |
| author2 |
Qu, Baozhen Yao, Lan Ma, Zengyu Cui, Pengfei Zhang, Shicui |
| author2Str |
Qu, Baozhen Yao, Lan Ma, Zengyu Cui, Pengfei Zhang, Shicui |
| ppnlink |
ELV019920881 |
| mediatype_str_mv |
z |
| isOA_txt |
false |
| hochschulschrift_bool |
false |
| author2_role |
oth oth oth oth oth |
| doi_str |
10.1016/j.dci.2018.08.005 |
| up_date |
2024-07-06T20:09:54.756Z |
| _version_ |
1803861722143916032 |
| 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">ELV043941354</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20230626004403.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">181113s2018 xx |||||o 00| ||eng c</controlfield><datafield tag="024" ind1="7" ind2=" "><subfield code="a">10.1016/j.dci.2018.08.005</subfield><subfield code="2">doi</subfield></datafield><datafield tag="028" ind1="5" ind2="2"><subfield code="a">/cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000001061.pica</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)ELV043941354</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(ELSEVIER)S0145-305X(18)30350-1</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="4"><subfield code="a">610</subfield><subfield code="q">VZ</subfield></datafield><datafield tag="082" ind1="0" ind2="4"><subfield code="a">610</subfield><subfield code="q">VZ</subfield></datafield><datafield tag="084" ind1=" " ind2=" "><subfield code="a">44.88</subfield><subfield code="2">bkl</subfield></datafield><datafield tag="100" ind1="1" ind2=" "><subfield code="a">Gao, Zhan</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Identification and functional characterization of amphioxus Miple, ancestral type of vertebrate midkine/pleiotrophin homologues</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">2018transfer abstract</subfield></datafield><datafield tag="300" ind1=" " ind2=" "><subfield code="a">13</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">Midkine (MK) and pleiotrophin (PTN) are the only two members of heparin-binding growth factor family. MK/PTN homologues found from Drosophila to humans are shown to have antibacterial activities and their antibacterial domains are conserved during evolution. However, little is known about MK/PTN homologue in the basal chordate amphioxus, and overall, information regarding MK/PTN homologues is rather limited in invertebrates. In this study, we identified a single MK/PTN homologue in Branchiostoma japonicum, termed BjMiple, which has a novel domain structure of PTN-PTNr1-PTNr2, and represents the ancestral form of vertebrate MK/PTN family proteins. BjMiple was expressed mainly in the ovary in a tissue-dependent fashion, and its expression was remarkably up-regulated following challenge with bacteria or their signature molecules LPS and LTA, suggesting its involvement in antibacterial responses. Functional assays revealed that BjMiple had strong antimicrobial activity, capable of killing a panel of Gram-negative and Gram-positive bacteria via a membranolytic mechanism, including interaction with bacterial membrane via LPS and LTA, membrane depolarization and high intracellular levels of ROS. Importantly, strong antibacterial activity was localized in PTN42-61 and PTNr142-66. Additionally, BjMiple and its derived peptides PTN42-61 and PTNr142-66 were not cytotoxic to human RBCs and mammalian cells. Taken together, our study suggests that amphioxus Miple is the ancestral type of vertebrate MK/PTN family homologues, and can play important roles as innate peptide antibiotics, which renders it a promising template for the design of novel peptide antibiotics against multi-drug resistant bacteria.</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Midkine (MK) and pleiotrophin (PTN) are the only two members of heparin-binding growth factor family. MK/PTN homologues found from Drosophila to humans are shown to have antibacterial activities and their antibacterial domains are conserved during evolution. However, little is known about MK/PTN homologue in the basal chordate amphioxus, and overall, information regarding MK/PTN homologues is rather limited in invertebrates. In this study, we identified a single MK/PTN homologue in Branchiostoma japonicum, termed BjMiple, which has a novel domain structure of PTN-PTNr1-PTNr2, and represents the ancestral form of vertebrate MK/PTN family proteins. BjMiple was expressed mainly in the ovary in a tissue-dependent fashion, and its expression was remarkably up-regulated following challenge with bacteria or their signature molecules LPS and LTA, suggesting its involvement in antibacterial responses. Functional assays revealed that BjMiple had strong antimicrobial activity, capable of killing a panel of Gram-negative and Gram-positive bacteria via a membranolytic mechanism, including interaction with bacterial membrane via LPS and LTA, membrane depolarization and high intracellular levels of ROS. Importantly, strong antibacterial activity was localized in PTN42-61 and PTNr142-66. Additionally, BjMiple and its derived peptides PTN42-61 and PTNr142-66 were not cytotoxic to human RBCs and mammalian cells. Taken together, our study suggests that amphioxus Miple is the ancestral type of vertebrate MK/PTN family homologues, and can play important roles as innate peptide antibiotics, which renders it a promising template for the design of novel peptide antibiotics against multi-drug resistant bacteria.</subfield></datafield><datafield tag="650" ind1=" " ind2="7"><subfield code="a">Amphioxus</subfield><subfield code="2">Elsevier</subfield></datafield><datafield tag="650" ind1=" " ind2="7"><subfield code="a">Heparin-binding growth factor</subfield><subfield code="2">Elsevier</subfield></datafield><datafield tag="650" ind1=" " ind2="7"><subfield code="a">Pleiotrophin</subfield><subfield code="2">Elsevier</subfield></datafield><datafield tag="650" ind1=" " ind2="7"><subfield code="a">Branchiostoma</subfield><subfield code="2">Elsevier</subfield></datafield><datafield tag="650" ind1=" " ind2="7"><subfield code="a">Midkine</subfield><subfield code="2">Elsevier</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Qu, Baozhen</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Yao, Lan</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Ma, Zengyu</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Cui, Pengfei</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Zhang, Shicui</subfield><subfield code="4">oth</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">Enthalten in</subfield><subfield code="n">Elsevier Science</subfield><subfield code="a">Wearne, Travis A. ELSEVIER</subfield><subfield code="t">GABAergic mRNA expression is differentially expressed across the prelimbic and orbitofrontal cortices of rats sensitized to methamphetamine: Relevance to psychosis</subfield><subfield code="d">2016transfer abstract</subfield><subfield code="d">ontogeny, phylogeny, aging : the official journal of the International Society of Developmental and Comparative Immunology</subfield><subfield code="g">Amsterdam [u.a.]</subfield><subfield code="w">(DE-627)ELV019920881</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:89</subfield><subfield code="g">year:2018</subfield><subfield code="g">pages:31-43</subfield><subfield code="g">extent:13</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">https://doi.org/10.1016/j.dci.2018.08.005</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">SSG-OLC-PHA</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_60</subfield></datafield><datafield tag="936" ind1="b" ind2="k"><subfield code="a">44.88</subfield><subfield code="j">Urologie</subfield><subfield code="j">Nephrologie</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">89</subfield><subfield code="j">2018</subfield><subfield code="h">31-43</subfield><subfield code="g">13</subfield></datafield></record></collection>
|
| score |
7.399928 |