|
rdf:type |
|
|
lifeskim:mentions |
umls-concept:C0001655,
umls-concept:C0014432,
umls-concept:C0021467,
umls-concept:C0021469,
umls-concept:C0055633,
umls-concept:C0063848,
umls-concept:C0072068,
umls-concept:C0301714,
umls-concept:C0332120,
umls-concept:C0596311,
umls-concept:C1330957,
umls-concept:C1551336,
umls-concept:C1709450,
umls-concept:C1709694
|
|
pubmed:issue |
2
|
|
pubmed:dateCreated |
1987-3-3
|
|
pubmed:abstractText |
Bovine parathyroid chromogranin A inhibits the cleavage of Z-Ala-Lys-Arg-AMC by either trypsin or IRCM-serine protease 1 (IRCM-SP1), a putative novel processing enzyme originally isolated from porcine pituitary anterior and neurointermediate lobes. On larger substrates, chromogranin A is a reversible competitive inhibitor of the cleavage at pairs of basic amino acids by IRCM-SP1. The substrates tested included pituitary ACTH and adrenal medulla pro-enkephalin-derived peptides such as the 8.6 kDa synenkephalin-containing precursor and peptide B. Chromogranin A is itself selectively processed by IRCM-SP1, and ACTH was shown to compete for such cleavage. These data suggest that chromogranins as a class of acidic proteins could participate in the tissue-specific processing of pro-hormones.
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adrenocorticotropic Hormone,
http://linkedlifedata.com/resource/pubmed/chemical/CHGA protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Chromogranin A,
http://linkedlifedata.com/resource/pubmed/chemical/Chromogranins,
http://linkedlifedata.com/resource/pubmed/chemical/Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Enkephalins,
http://linkedlifedata.com/resource/pubmed/chemical/IRCM-serine protease 1,
http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protease Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Precursors,
http://linkedlifedata.com/resource/pubmed/chemical/Serine Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/proenkephalin
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Jan
|
|
pubmed:issn |
0014-5793
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:day |
26
|
|
pubmed:volume |
211
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
144-50
|
|
pubmed:dateRevised |
2007-4-17
|
|
pubmed:meshHeading |
pubmed-meshheading:3026846-Adrenocorticotropic Hormone,
pubmed-meshheading:3026846-Chromaffin Granules,
pubmed-meshheading:3026846-Chromogranin A,
pubmed-meshheading:3026846-Chromogranins,
pubmed-meshheading:3026846-Endopeptidases,
pubmed-meshheading:3026846-Enkephalins,
pubmed-meshheading:3026846-Humans,
pubmed-meshheading:3026846-Kinetics,
pubmed-meshheading:3026846-Nerve Tissue Proteins,
pubmed-meshheading:3026846-Protease Inhibitors,
pubmed-meshheading:3026846-Protein Precursors,
pubmed-meshheading:3026846-Serine Endopeptidases
|
|
pubmed:year |
1987
|
|
pubmed:articleTitle |
Chromogranin A can act as a reversible processing enzyme inhibitor. Evidence from the inhibition of the IRCM-serine protease 1 cleavage of pro-enkephalin and ACTH at pairs of basic amino acids.
|
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|
