Literature DB >> 2426033

Phylogenetic distance from man correlates with immunologic cross-reactivity among liver insulin receptors.

C A Stuart.   

Abstract

The hepatic insulin receptors from evolutionarily diverse species were evaluated to determine their ability to bind human insulin and their immunologic cross-reactivity with the human insulin receptor. We found that the liver membranes of each species possessed insulin receptors with remarkably similar affinities for human insulin. An immunoassay specific for human insulin receptor showed that the amount of shared antigenic determinants differed widely among the species tested and in general decreased as the phylogenetic distance from man increased. These data suggest that the ability to bind insulin has been highly conserved during evolution despite considerable variation in the primary structure of the insulin receptor.

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Year:  1986        PMID: 2426033     DOI: 10.1016/0305-0491(86)90200-2

Source DB:  PubMed          Journal:  Comp Biochem Physiol B        ISSN: 0305-0491


  2 in total

1.  Binding and bioactivity of insulin in primary cultures of carp (Cyprinus carpio) hepatocytes.

Authors:  H Segner; R Böhm; W Kloas
Journal:  Fish Physiol Biochem       Date:  1993-07       Impact factor: 2.794

2.  Tumor necrosis factor alpha binding to bacteria: evidence for a high-affinity receptor and alteration of bacterial virulence properties.

Authors:  G Luo; D W Niesel; R A Shaban; E A Grimm; G R Klimpel
Journal:  Infect Immun       Date:  1993-03       Impact factor: 3.441

  2 in total

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