Literature DB >> 3135841

Cell-specific processing of pro-cholecystokinin and pro-gastrin.

J F Rehfeld1, L Bardram, P Cantor, L Hilsted, T W Schwartz.   

Abstract

The present review argues that the gastrin-cholecystokinin family is a suitable model for the study of cell-specific processing of pro-hormones. First, the homologous active site of the hormones is a precisely defined tetrapeptide amide, which is well preserved during evolution. Second, the genes of both hormones are translated in a variety of cells (neurons, endocrine cells, paracrine cells, lymphocytes, etc,), but to a varying degree during ontogenesis and pathogenesis of various diseases. Third, each pro-hormone contains multiple processing sites (mono- and dibasic cleavage sites, amidation sites and consensus sequences for seryl phosphorylation and tyrosyl sulfation) leaving ample room for variations in the post-translational processing. The review discusses examples of cell-specific processing that appears to be functionally expedient.

Entities:  

Mesh:

Substances:

Year:  1988        PMID: 3135841     DOI: 10.1016/0300-9084(88)90155-1

Source DB:  PubMed          Journal:  Biochimie        ISSN: 0300-9084            Impact factor:   4.079


  4 in total

1.  Mutual relationships between chromogranins A and B and gastrin in individual gastrin cells.

Authors:  Y Cetin; G Bargsten; D Grube
Journal:  Proc Natl Acad Sci U S A       Date:  1992-04-01       Impact factor: 11.205

Review 2.  Towards a functional significance of peptides and biogenic amines produced by the anterior pituitary.

Authors:  H Houben; D Tilemans; C Denef
Journal:  J Endocrinol Invest       Date:  1990-11       Impact factor: 4.256

3.  Chromostatin, a chromogranin A-derived bioactive peptide, is present in human pancreatic insulin (beta) cells.

Authors:  Y Cetin; D Aunis; M F Bader; E Galindo; A Jörns; G Bargsten; D Grube
Journal:  Proc Natl Acad Sci U S A       Date:  1993-03-15       Impact factor: 11.205

4.  A novel 1745-dalton pyroglutamyl peptide derived from chromogranin B is in the bovine adrenomedullary chromaffin vesicle.

Authors:  T Flanagan; L Taylor; L Poulter; O H Viveros; E J Diliberto
Journal:  Cell Mol Neurobiol       Date:  1990-12       Impact factor: 5.046

  4 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.