Human L-Dopa decarboxylase interaction with annexin V and expression during apoptosis.
Biochimie
; 177: 78-86, 2020 Oct.
Article
in En
| MEDLINE
| ID: mdl-32835737
ABSTRACT
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.
Key words
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Aromatic-L-Amino-Acid Decarboxylases
/
Annexin A5
/
Enzyme Inhibitors
Limits:
Animals
/
Female
/
Humans
/
Pregnancy
Language:
En
Journal:
Biochimie
Year:
2020
Document type:
Article