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rdf:type |
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lifeskim:mentions |
umls-concept:C0006556,
umls-concept:C0017953,
umls-concept:C0033195,
umls-concept:C0083957,
umls-concept:C0135615,
umls-concept:C0441635,
umls-concept:C0678594,
umls-concept:C1135183,
umls-concept:C1413159,
umls-concept:C1418388,
umls-concept:C1418389,
umls-concept:C1418600,
umls-concept:C1709694
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pubmed:issue |
3
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pubmed:dateCreated |
1992-10-26
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pubmed:databankReference |
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pubmed:abstractText |
The complete cDNA structure of the porcine (p) pro-protein and pro-hormone convertase PC2 (pPC2) was obtained from a cDNA library of pituitary neurointermediate lobes mRNA. The deduced amino acid sequence revealed that pPC2 exhibits a 99-97% sequence identity to the human, mouse and rat homologues. The 3' end of the 2.1 kb cDNA is the least conserved segment. On Northern blots of pars intermedia poly A+ RNA two transcripts of 3 and 5 kb were detected. Molecular analysis of the N-terminal glycopeptide products of porcine pro-opiomelanocortin (pPOMC) co-expressed with vaccinia virus recombinants of PC1 or PC2, revealed that in cells devoid or containing secretory granules both convertases can cleave pPOMC with PC1 releasing the 1-80, 1-107 and 1-148 glycopeptide fragments, and PC2 cleaving pPOMC directly into pPOMC 1-107.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Glycopeptides,
http://linkedlifedata.com/resource/pubmed/chemical/Pcsk1 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Pituitary Hormones,
http://linkedlifedata.com/resource/pubmed/chemical/Pro-Opiomelanocortin,
http://linkedlifedata.com/resource/pubmed/chemical/Proprotein Convertase 1,
http://linkedlifedata.com/resource/pubmed/chemical/Proprotein Convertase 2,
http://linkedlifedata.com/resource/pubmed/chemical/Proprotein Convertases,
http://linkedlifedata.com/resource/pubmed/chemical/Serine Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/proopiocortin fragments
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0014-5793
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
5
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pubmed:volume |
310
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pubmed:geneSymbol |
PC1,
PC2
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
235-9
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:1397279-Amino Acid Sequence,
pubmed-meshheading:1397279-Animals,
pubmed-meshheading:1397279-Base Sequence,
pubmed-meshheading:1397279-Glycopeptides,
pubmed-meshheading:1397279-Models, Biological,
pubmed-meshheading:1397279-Molecular Sequence Data,
pubmed-meshheading:1397279-Peptide Fragments,
pubmed-meshheading:1397279-Pituitary Gland,
pubmed-meshheading:1397279-Pituitary Hormones,
pubmed-meshheading:1397279-Pro-Opiomelanocortin,
pubmed-meshheading:1397279-Proprotein Convertase 1,
pubmed-meshheading:1397279-Proprotein Convertase 2,
pubmed-meshheading:1397279-Proprotein Convertases,
pubmed-meshheading:1397279-Protein Processing, Post-Translational,
pubmed-meshheading:1397279-Sequence Analysis, DNA,
pubmed-meshheading:1397279-Serine Endopeptidases,
pubmed-meshheading:1397279-Substrate Specificity,
pubmed-meshheading:1397279-Swine
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pubmed:year |
1992
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pubmed:articleTitle |
The cDNA structure of the porcine pro-hormone convertase PC2 and the comparative processing by PC1 and PC2 of the N-terminal glycopeptide segment of porcine POMC.
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pubmed:affiliation |
J.A. DeSève Laboratories of Biochemical, Clinical Research Institute of Montreal, Que., Canada.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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