Literature DB >> 1397279

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.

N G Seidah1, H Fournier, G Boileau, S Benjannet, N Rondeau, M Chrétien.   

Abstract

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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Year:  1992        PMID： 1397279     DOI： 10.1016/0014-5793(92)81339-n

Source DB:  PubMed          Journal:  FEBS Lett        ISSN： 0014-5793            Impact factor:   4.124


  8 in total

1.  Effects of cortisol and estradiol on pituitary expression of proopiomelanocortin, prohormone convertase-1, prohormone convertase-2, and glucocorticoid receptor mRNA in fetal sheep.

Authors:  A C Holloway; W L Whittle; J R Challis
Journal:  Endocrine       Date:  2001-04       Impact factor: 3.633

2.  Comparative biosynthesis, covalent post-translational modifications and efficiency of prosegment cleavage of the prohormone convertases PC1 and PC2: glycosylation, sulphation and identification of the intracellular site of prosegment cleavage of PC1 and PC2.

Authors:  S Benjannet; N Rondeau; L Paquet; A Boudreault; C Lazure; M Chrétien; N G Seidah
Journal:  Biochem J       Date:  1993-09-15       Impact factor: 3.857

3.  cDNA structure of the mouse and rat subtilisin/kexin-like PC5: a candidate proprotein convertase expressed in endocrine and nonendocrine cells.

Authors:  J Lusson; D Vieau; J Hamelin; R Day; M Chrétien; N G Seidah
Journal:  Proc Natl Acad Sci U S A       Date:  1993-07-15       Impact factor: 11.205

4.  Effects of labor on pituitary expression of proopiomelanocortin, prohormone convertase (PC)-1, PC-2, and glucocorticoid receptor mRNA in fetal sheep.

Authors:  A C Holloway; S Gyomorey; J R Challis
Journal:  Endocrine       Date:  2000-08       Impact factor: 3.633

5.  Ontogeny of the prohormone convertases PC1 and PC2 in the mouse hypophysis and their colocalization with corticotropin and alpha-melanotropin.

Authors:  M Marcinkiewicz; R Day; N G Seidah; M Chrétien
Journal:  Proc Natl Acad Sci U S A       Date:  1993-06-01       Impact factor: 11.205

6.  Isolation and in situ localization of a cDNA encoding a Kex2-like prohormone convertase in the nematode Caenorhabditis elegans.

Authors:  E Gómez-Saladín; D L Wilson; I M Dickerson
Journal:  Cell Mol Neurobiol       Date:  1994-02       Impact factor: 5.046

7.  First survey and functional annotation of prohormone and convertase genes in the pig.

Authors:  Kenneth I Porter; Bruce R Southey; Jonathan V Sweedler; Sandra L Rodriguez-Zas
Journal:  BMC Genomics       Date:  2012-11-15       Impact factor: 3.969

8.  The role of proopiomelanocortin (POMC) neurones in feeding behaviour.

Authors:  George Wm Millington
Journal:  Nutr Metab (Lond)       Date:  2007-09-01       Impact factor: 4.169
  8 in total

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