Literature DB >> 6641941

The glycopeptide domain of the rat vasopressin precursor.

M T Chauvet, J Chauvet, R Acher.   

Abstract

The vasopressin precursor is composed of 3 domains, namely vasopressin, MSEL-neurophysin and a glycopeptide. Processing occurs during axonal transport from hypothalamus to neurohypophysis from which the 3 fragments can be isolated. The glycopeptide fragment of the rat vasopressin precursor has been purified and sequenced. Despite the fact that rat MSEL-neurophysin is shortened (93 residues instead of 95 for other mammals), rat glycopeptide has 39 residues, as do the other mammalian glycopeptides, suggesting a similar processing. Fifteen substitutions are however observed when compared to ox glycopeptide. The C-terminal part of MSEL-neurophysin (residues 77-93) and the glycopeptide are encoded by the same exon and the homologies when compared with their bovine counterparts are 58% and 62% respectively. In contrast, the central part of rat MSEL-neurophysin (residues 10-76), which is encoded by a separate exon, displays 96% of homology; vasopressin and the N-terminal part of MSEL-neurophysin (residues 1-9), encoded by a third exon, are nearly invariant.

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Year:  1983        PMID: 6641941     DOI: 10.1016/0014-5793(83)80830-8

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


  1 in total

1.  Detection of Provasopressin in Invasive and Non-invasive (DCIS) Human Breast Cancer Using a Monoclonal Antibody Directed Against the C-terminus (MAG1).

Authors:  Brendan P Keegan; Vincent A Memoli; Wendy A Wells; William G North
Journal:  Breast Cancer (Auckl)       Date:  2010-04-08
  1 in total

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