Human L-Dopa decarboxylase interaction with annexin V and expression during apoptosis
l-Dopa Decarboxylase (DDC) is a pyridoxal requiring enzyme that catalyzes the decarboxylation of L-3,4-dihydroxyphenylalanine (l-Dopa) to Dopamine (DA). The function of DDC in physiological and pathological biochemical pathways remains poorly understood, while the function and regulation of human DD...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Chalatsa, Ioanna [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2020transfer abstract |
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| Schlagwörter: |
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| Umfang: |
9 |
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| Übergeordnetes Werk: |
Enthalten in: Energy-saving improvement of heat integration for separating dilute azeotropic components in extractive distillation - Duan, Cong ELSEVIER, 2022, an international journal of biochemistry and molecular biology, Paris [u.a.] |
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| Übergeordnetes Werk: |
volume:177 ; year:2020 ; pages:78-86 ; extent:9 |
| Links: |
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| DOI / URN: |
10.1016/j.biochi.2020.08.010 |
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| 520 | |a l-Dopa Decarboxylase (DDC) is a pyridoxal requiring enzyme that catalyzes the decarboxylation of L-3,4-dihydroxyphenylalanine (l-Dopa) to Dopamine (DA). The function of DDC in physiological and pathological biochemical pathways remains poorly understood, while the function and regulation of human DDC isoforms is almost completely elusive. We have shown that Annexin V, a fundamental apoptosis marker, is an inhibitor of l-Dopa decarboxylase activity. Here we show the interaction of both the full-length DDC and the truncated isoform alternative DDC (Alt-DDC) with Annexin V in human tissue and cell lines. Interestingly, DDC isoform expression is enhanced or remains unaffected following staurosporine (STS) treatment, despite increased levels of cytotoxicity and apoptosis. The findings presented here provide novel insights concerning the involvement of DDC in programmed cell death. | ||
| 520 | |a l-Dopa Decarboxylase (DDC) is a pyridoxal requiring enzyme that catalyzes the decarboxylation of L-3,4-dihydroxyphenylalanine (l-Dopa) to Dopamine (DA). The function of DDC in physiological and pathological biochemical pathways remains poorly understood, while the function and regulation of human DDC isoforms is almost completely elusive. We have shown that Annexin V, a fundamental apoptosis marker, is an inhibitor of l-Dopa decarboxylase activity. Here we show the interaction of both the full-length DDC and the truncated isoform alternative DDC (Alt-DDC) with Annexin V in human tissue and cell lines. Interestingly, DDC isoform expression is enhanced or remains unaffected following staurosporine (STS) treatment, despite increased levels of cytotoxicity and apoptosis. The findings presented here provide novel insights concerning the involvement of DDC in programmed cell death. | ||
| 650 | 7 | |a Staurosporine |2 Elsevier | |
| 650 | 7 | |a Cytotoxicity |2 Elsevier | |
| 650 | 7 | |a Annexin V |2 Elsevier | |
| 650 | 7 | |a Alternative l-Dopa decarboxylase (alt-DDC) |2 Elsevier | |
| 650 | 7 | |a L-dopa decarboxylase |2 Elsevier | |
| 650 | 7 | |a Apoptosis |2 Elsevier | |
| 700 | 1 | |a Arvanitis, Nikolaos |4 oth | |
| 700 | 1 | |a Arvanitis, Dimitrios |4 oth | |
| 700 | 1 | |a Tsakou, Anastasia C. |4 oth | |
| 700 | 1 | |a Kalantzis, Evangelos D. |4 oth | |
| 700 | 1 | |a Vassiliou, Alice G. |4 oth | |
| 700 | 1 | |a Sideris, Diamantis C. |4 oth | |
| 700 | 1 | |a Frakolaki, Efseveia |4 oth | |
| 700 | 1 | |a Vassilaki, Niki |4 oth | |
| 700 | 1 | |a Vassilacopoulou, Dido |4 oth | |
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10.1016/j.biochi.2020.08.010 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000001218.pica (DE-627)ELV05157425X (ELSEVIER)S0300-9084(20)30194-2 DE-627 ger DE-627 rakwb eng 600 VZ 50.70 bkl Chalatsa, Ioanna verfasserin aut Human L-Dopa decarboxylase interaction with annexin V and expression during apoptosis 2020transfer abstract 9 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier l-Dopa Decarboxylase (DDC) is a pyridoxal requiring enzyme that catalyzes the decarboxylation of L-3,4-dihydroxyphenylalanine (l-Dopa) to Dopamine (DA). The function of DDC in physiological and pathological biochemical pathways remains poorly understood, while the function and regulation of human DDC isoforms is almost completely elusive. We have shown that Annexin V, a fundamental apoptosis marker, is an inhibitor of l-Dopa decarboxylase activity. Here we show the interaction of both the full-length DDC and the truncated isoform alternative DDC (Alt-DDC) with Annexin V in human tissue and cell lines. Interestingly, DDC isoform expression is enhanced or remains unaffected following staurosporine (STS) treatment, despite increased levels of cytotoxicity and apoptosis. The findings presented here provide novel insights concerning the involvement of DDC in programmed cell death. l-Dopa Decarboxylase (DDC) is a pyridoxal requiring enzyme that catalyzes the decarboxylation of L-3,4-dihydroxyphenylalanine (l-Dopa) to Dopamine (DA). The function of DDC in physiological and pathological biochemical pathways remains poorly understood, while the function and regulation of human DDC isoforms is almost completely elusive. We have shown that Annexin V, a fundamental apoptosis marker, is an inhibitor of l-Dopa decarboxylase activity. Here we show the interaction of both the full-length DDC and the truncated isoform alternative DDC (Alt-DDC) with Annexin V in human tissue and cell lines. Interestingly, DDC isoform expression is enhanced or remains unaffected following staurosporine (STS) treatment, despite increased levels of cytotoxicity and apoptosis. The findings presented here provide novel insights concerning the involvement of DDC in programmed cell death. Staurosporine Elsevier Cytotoxicity Elsevier Annexin V Elsevier Alternative l-Dopa decarboxylase (alt-DDC) Elsevier L-dopa decarboxylase Elsevier Apoptosis Elsevier Arvanitis, Nikolaos oth Arvanitis, Dimitrios oth Tsakou, Anastasia C. oth Kalantzis, Evangelos D. oth Vassiliou, Alice G. oth Sideris, Diamantis C. oth Frakolaki, Efseveia oth Vassilaki, Niki oth Vassilacopoulou, Dido oth Enthalten in Elsevier Duan, Cong ELSEVIER Energy-saving improvement of heat integration for separating dilute azeotropic components in extractive distillation 2022 an international journal of biochemistry and molecular biology Paris [u.a.] (DE-627)ELV008857954 volume:177 year:2020 pages:78-86 extent:9 https://doi.org/10.1016/j.biochi.2020.08.010 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U 50.70 Energie: Allgemeines VZ AR 177 2020 78-86 9 |
| spelling |
10.1016/j.biochi.2020.08.010 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000001218.pica (DE-627)ELV05157425X (ELSEVIER)S0300-9084(20)30194-2 DE-627 ger DE-627 rakwb eng 600 VZ 50.70 bkl Chalatsa, Ioanna verfasserin aut Human L-Dopa decarboxylase interaction with annexin V and expression during apoptosis 2020transfer abstract 9 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier l-Dopa Decarboxylase (DDC) is a pyridoxal requiring enzyme that catalyzes the decarboxylation of L-3,4-dihydroxyphenylalanine (l-Dopa) to Dopamine (DA). The function of DDC in physiological and pathological biochemical pathways remains poorly understood, while the function and regulation of human DDC isoforms is almost completely elusive. We have shown that Annexin V, a fundamental apoptosis marker, is an inhibitor of l-Dopa decarboxylase activity. Here we show the interaction of both the full-length DDC and the truncated isoform alternative DDC (Alt-DDC) with Annexin V in human tissue and cell lines. Interestingly, DDC isoform expression is enhanced or remains unaffected following staurosporine (STS) treatment, despite increased levels of cytotoxicity and apoptosis. The findings presented here provide novel insights concerning the involvement of DDC in programmed cell death. l-Dopa Decarboxylase (DDC) is a pyridoxal requiring enzyme that catalyzes the decarboxylation of L-3,4-dihydroxyphenylalanine (l-Dopa) to Dopamine (DA). The function of DDC in physiological and pathological biochemical pathways remains poorly understood, while the function and regulation of human DDC isoforms is almost completely elusive. We have shown that Annexin V, a fundamental apoptosis marker, is an inhibitor of l-Dopa decarboxylase activity. Here we show the interaction of both the full-length DDC and the truncated isoform alternative DDC (Alt-DDC) with Annexin V in human tissue and cell lines. Interestingly, DDC isoform expression is enhanced or remains unaffected following staurosporine (STS) treatment, despite increased levels of cytotoxicity and apoptosis. The findings presented here provide novel insights concerning the involvement of DDC in programmed cell death. Staurosporine Elsevier Cytotoxicity Elsevier Annexin V Elsevier Alternative l-Dopa decarboxylase (alt-DDC) Elsevier L-dopa decarboxylase Elsevier Apoptosis Elsevier Arvanitis, Nikolaos oth Arvanitis, Dimitrios oth Tsakou, Anastasia C. oth Kalantzis, Evangelos D. oth Vassiliou, Alice G. oth Sideris, Diamantis C. oth Frakolaki, Efseveia oth Vassilaki, Niki oth Vassilacopoulou, Dido oth Enthalten in Elsevier Duan, Cong ELSEVIER Energy-saving improvement of heat integration for separating dilute azeotropic components in extractive distillation 2022 an international journal of biochemistry and molecular biology Paris [u.a.] (DE-627)ELV008857954 volume:177 year:2020 pages:78-86 extent:9 https://doi.org/10.1016/j.biochi.2020.08.010 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U 50.70 Energie: Allgemeines VZ AR 177 2020 78-86 9 |
| allfields_unstemmed |
10.1016/j.biochi.2020.08.010 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000001218.pica (DE-627)ELV05157425X (ELSEVIER)S0300-9084(20)30194-2 DE-627 ger DE-627 rakwb eng 600 VZ 50.70 bkl Chalatsa, Ioanna verfasserin aut Human L-Dopa decarboxylase interaction with annexin V and expression during apoptosis 2020transfer abstract 9 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier l-Dopa Decarboxylase (DDC) is a pyridoxal requiring enzyme that catalyzes the decarboxylation of L-3,4-dihydroxyphenylalanine (l-Dopa) to Dopamine (DA). The function of DDC in physiological and pathological biochemical pathways remains poorly understood, while the function and regulation of human DDC isoforms is almost completely elusive. We have shown that Annexin V, a fundamental apoptosis marker, is an inhibitor of l-Dopa decarboxylase activity. Here we show the interaction of both the full-length DDC and the truncated isoform alternative DDC (Alt-DDC) with Annexin V in human tissue and cell lines. Interestingly, DDC isoform expression is enhanced or remains unaffected following staurosporine (STS) treatment, despite increased levels of cytotoxicity and apoptosis. The findings presented here provide novel insights concerning the involvement of DDC in programmed cell death. l-Dopa Decarboxylase (DDC) is a pyridoxal requiring enzyme that catalyzes the decarboxylation of L-3,4-dihydroxyphenylalanine (l-Dopa) to Dopamine (DA). The function of DDC in physiological and pathological biochemical pathways remains poorly understood, while the function and regulation of human DDC isoforms is almost completely elusive. We have shown that Annexin V, a fundamental apoptosis marker, is an inhibitor of l-Dopa decarboxylase activity. Here we show the interaction of both the full-length DDC and the truncated isoform alternative DDC (Alt-DDC) with Annexin V in human tissue and cell lines. Interestingly, DDC isoform expression is enhanced or remains unaffected following staurosporine (STS) treatment, despite increased levels of cytotoxicity and apoptosis. The findings presented here provide novel insights concerning the involvement of DDC in programmed cell death. Staurosporine Elsevier Cytotoxicity Elsevier Annexin V Elsevier Alternative l-Dopa decarboxylase (alt-DDC) Elsevier L-dopa decarboxylase Elsevier Apoptosis Elsevier Arvanitis, Nikolaos oth Arvanitis, Dimitrios oth Tsakou, Anastasia C. oth Kalantzis, Evangelos D. oth Vassiliou, Alice G. oth Sideris, Diamantis C. oth Frakolaki, Efseveia oth Vassilaki, Niki oth Vassilacopoulou, Dido oth Enthalten in Elsevier Duan, Cong ELSEVIER Energy-saving improvement of heat integration for separating dilute azeotropic components in extractive distillation 2022 an international journal of biochemistry and molecular biology Paris [u.a.] (DE-627)ELV008857954 volume:177 year:2020 pages:78-86 extent:9 https://doi.org/10.1016/j.biochi.2020.08.010 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U 50.70 Energie: Allgemeines VZ AR 177 2020 78-86 9 |
| allfieldsGer |
10.1016/j.biochi.2020.08.010 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000001218.pica (DE-627)ELV05157425X (ELSEVIER)S0300-9084(20)30194-2 DE-627 ger DE-627 rakwb eng 600 VZ 50.70 bkl Chalatsa, Ioanna verfasserin aut Human L-Dopa decarboxylase interaction with annexin V and expression during apoptosis 2020transfer abstract 9 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier l-Dopa Decarboxylase (DDC) is a pyridoxal requiring enzyme that catalyzes the decarboxylation of L-3,4-dihydroxyphenylalanine (l-Dopa) to Dopamine (DA). The function of DDC in physiological and pathological biochemical pathways remains poorly understood, while the function and regulation of human DDC isoforms is almost completely elusive. We have shown that Annexin V, a fundamental apoptosis marker, is an inhibitor of l-Dopa decarboxylase activity. Here we show the interaction of both the full-length DDC and the truncated isoform alternative DDC (Alt-DDC) with Annexin V in human tissue and cell lines. Interestingly, DDC isoform expression is enhanced or remains unaffected following staurosporine (STS) treatment, despite increased levels of cytotoxicity and apoptosis. The findings presented here provide novel insights concerning the involvement of DDC in programmed cell death. l-Dopa Decarboxylase (DDC) is a pyridoxal requiring enzyme that catalyzes the decarboxylation of L-3,4-dihydroxyphenylalanine (l-Dopa) to Dopamine (DA). The function of DDC in physiological and pathological biochemical pathways remains poorly understood, while the function and regulation of human DDC isoforms is almost completely elusive. We have shown that Annexin V, a fundamental apoptosis marker, is an inhibitor of l-Dopa decarboxylase activity. Here we show the interaction of both the full-length DDC and the truncated isoform alternative DDC (Alt-DDC) with Annexin V in human tissue and cell lines. Interestingly, DDC isoform expression is enhanced or remains unaffected following staurosporine (STS) treatment, despite increased levels of cytotoxicity and apoptosis. The findings presented here provide novel insights concerning the involvement of DDC in programmed cell death. Staurosporine Elsevier Cytotoxicity Elsevier Annexin V Elsevier Alternative l-Dopa decarboxylase (alt-DDC) Elsevier L-dopa decarboxylase Elsevier Apoptosis Elsevier Arvanitis, Nikolaos oth Arvanitis, Dimitrios oth Tsakou, Anastasia C. oth Kalantzis, Evangelos D. oth Vassiliou, Alice G. oth Sideris, Diamantis C. oth Frakolaki, Efseveia oth Vassilaki, Niki oth Vassilacopoulou, Dido oth Enthalten in Elsevier Duan, Cong ELSEVIER Energy-saving improvement of heat integration for separating dilute azeotropic components in extractive distillation 2022 an international journal of biochemistry and molecular biology Paris [u.a.] (DE-627)ELV008857954 volume:177 year:2020 pages:78-86 extent:9 https://doi.org/10.1016/j.biochi.2020.08.010 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U 50.70 Energie: Allgemeines VZ AR 177 2020 78-86 9 |
| allfieldsSound |
10.1016/j.biochi.2020.08.010 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000001218.pica (DE-627)ELV05157425X (ELSEVIER)S0300-9084(20)30194-2 DE-627 ger DE-627 rakwb eng 600 VZ 50.70 bkl Chalatsa, Ioanna verfasserin aut Human L-Dopa decarboxylase interaction with annexin V and expression during apoptosis 2020transfer abstract 9 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier l-Dopa Decarboxylase (DDC) is a pyridoxal requiring enzyme that catalyzes the decarboxylation of L-3,4-dihydroxyphenylalanine (l-Dopa) to Dopamine (DA). The function of DDC in physiological and pathological biochemical pathways remains poorly understood, while the function and regulation of human DDC isoforms is almost completely elusive. We have shown that Annexin V, a fundamental apoptosis marker, is an inhibitor of l-Dopa decarboxylase activity. Here we show the interaction of both the full-length DDC and the truncated isoform alternative DDC (Alt-DDC) with Annexin V in human tissue and cell lines. Interestingly, DDC isoform expression is enhanced or remains unaffected following staurosporine (STS) treatment, despite increased levels of cytotoxicity and apoptosis. The findings presented here provide novel insights concerning the involvement of DDC in programmed cell death. l-Dopa Decarboxylase (DDC) is a pyridoxal requiring enzyme that catalyzes the decarboxylation of L-3,4-dihydroxyphenylalanine (l-Dopa) to Dopamine (DA). The function of DDC in physiological and pathological biochemical pathways remains poorly understood, while the function and regulation of human DDC isoforms is almost completely elusive. We have shown that Annexin V, a fundamental apoptosis marker, is an inhibitor of l-Dopa decarboxylase activity. Here we show the interaction of both the full-length DDC and the truncated isoform alternative DDC (Alt-DDC) with Annexin V in human tissue and cell lines. Interestingly, DDC isoform expression is enhanced or remains unaffected following staurosporine (STS) treatment, despite increased levels of cytotoxicity and apoptosis. The findings presented here provide novel insights concerning the involvement of DDC in programmed cell death. Staurosporine Elsevier Cytotoxicity Elsevier Annexin V Elsevier Alternative l-Dopa decarboxylase (alt-DDC) Elsevier L-dopa decarboxylase Elsevier Apoptosis Elsevier Arvanitis, Nikolaos oth Arvanitis, Dimitrios oth Tsakou, Anastasia C. oth Kalantzis, Evangelos D. oth Vassiliou, Alice G. oth Sideris, Diamantis C. oth Frakolaki, Efseveia oth Vassilaki, Niki oth Vassilacopoulou, Dido oth Enthalten in Elsevier Duan, Cong ELSEVIER Energy-saving improvement of heat integration for separating dilute azeotropic components in extractive distillation 2022 an international journal of biochemistry and molecular biology Paris [u.a.] (DE-627)ELV008857954 volume:177 year:2020 pages:78-86 extent:9 https://doi.org/10.1016/j.biochi.2020.08.010 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U 50.70 Energie: Allgemeines VZ AR 177 2020 78-86 9 |
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Enthalten in Energy-saving improvement of heat integration for separating dilute azeotropic components in extractive distillation Paris [u.a.] volume:177 year:2020 pages:78-86 extent:9 |
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Enthalten in Energy-saving improvement of heat integration for separating dilute azeotropic components in extractive distillation Paris [u.a.] volume:177 year:2020 pages:78-86 extent:9 |
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Staurosporine Cytotoxicity Annexin V Alternative l-Dopa decarboxylase (alt-DDC) L-dopa decarboxylase Apoptosis |
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Energy-saving improvement of heat integration for separating dilute azeotropic components in extractive distillation |
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Chalatsa, Ioanna @@aut@@ Arvanitis, Nikolaos @@oth@@ Arvanitis, Dimitrios @@oth@@ Tsakou, Anastasia C. @@oth@@ Kalantzis, Evangelos D. @@oth@@ Vassiliou, Alice G. @@oth@@ Sideris, Diamantis C. @@oth@@ Frakolaki, Efseveia @@oth@@ Vassilaki, Niki @@oth@@ Vassilacopoulou, Dido @@oth@@ |
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human l-dopa decarboxylase interaction with annexin v and expression during apoptosis |
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Human L-Dopa decarboxylase interaction with annexin V and expression during apoptosis |
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l-Dopa Decarboxylase (DDC) is a pyridoxal requiring enzyme that catalyzes the decarboxylation of L-3,4-dihydroxyphenylalanine (l-Dopa) to Dopamine (DA). The function of DDC in physiological and pathological biochemical pathways remains poorly understood, while the function and regulation of human DDC isoforms is almost completely elusive. We have shown that Annexin V, a fundamental apoptosis marker, is an inhibitor of l-Dopa decarboxylase activity. Here we show the interaction of both the full-length DDC and the truncated isoform alternative DDC (Alt-DDC) with Annexin V in human tissue and cell lines. Interestingly, DDC isoform expression is enhanced or remains unaffected following staurosporine (STS) treatment, despite increased levels of cytotoxicity and apoptosis. The findings presented here provide novel insights concerning the involvement of DDC in programmed cell death. |
| abstractGer |
l-Dopa Decarboxylase (DDC) is a pyridoxal requiring enzyme that catalyzes the decarboxylation of L-3,4-dihydroxyphenylalanine (l-Dopa) to Dopamine (DA). The function of DDC in physiological and pathological biochemical pathways remains poorly understood, while the function and regulation of human DDC isoforms is almost completely elusive. We have shown that Annexin V, a fundamental apoptosis marker, is an inhibitor of l-Dopa decarboxylase activity. Here we show the interaction of both the full-length DDC and the truncated isoform alternative DDC (Alt-DDC) with Annexin V in human tissue and cell lines. Interestingly, DDC isoform expression is enhanced or remains unaffected following staurosporine (STS) treatment, despite increased levels of cytotoxicity and apoptosis. The findings presented here provide novel insights concerning the involvement of DDC in programmed cell death. |
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l-Dopa Decarboxylase (DDC) is a pyridoxal requiring enzyme that catalyzes the decarboxylation of L-3,4-dihydroxyphenylalanine (l-Dopa) to Dopamine (DA). The function of DDC in physiological and pathological biochemical pathways remains poorly understood, while the function and regulation of human DDC isoforms is almost completely elusive. We have shown that Annexin V, a fundamental apoptosis marker, is an inhibitor of l-Dopa decarboxylase activity. Here we show the interaction of both the full-length DDC and the truncated isoform alternative DDC (Alt-DDC) with Annexin V in human tissue and cell lines. Interestingly, DDC isoform expression is enhanced or remains unaffected following staurosporine (STS) treatment, despite increased levels of cytotoxicity and apoptosis. The findings presented here provide novel insights concerning the involvement of DDC in programmed cell death. |
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