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Does human attractin have DP4 activity?

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Published/Copyright: January 29, 2007
Biological Chemistry
From the journal Volume 388 Issue 2

Abstract

Mutations in the mouse ATRN gene, which encodes attractin, offer links between this protein and pigmentation, metabolism, immune status and neurodegeneration. However, the mechanisms of attractin action are not understood. The protein was first identified in humans in a circulating form in serum. A protease activity was postulated similar to the membrane-bound ectoenzyme DP4/CD26. In the last decade, both DP4/CD26 and attractin were controversially described to be the major source of human serum DP4 activity. We purified attractin from human plasma, and found that the DP4-like activity of the preparation shows nearly identical kinetic properties to that of recombinant human DP4. In contrast, the native electrophoretic behavior of this activity is clearly different from human and porcine DP4, but co-migrates with the protein band identified as attractin by Western blotting and N-terminal sequencing. Nevertheless, a DP4 impurity could be demonstrated in purified plasma attractin and the activity could be removed by ADA affinity chromatography, resulting in a homogenous attractin preparation without DP4 activity. These results are substantiated by expression of different attractin isoforms, in which no DP4 activity was found either. This indicates that the multidomain protein attractin acts as a receptor or adhesion protein rather than a protease.

Keywords: adenosine deaminase; attractin; CD26; DASH; dipeptidyl peptidase IV; serum
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Published Online: 2007-01-29
Published in Print: 2007-02-01

©2007 by Walter de Gruyter Berlin New York

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  2. Isolation and characterization of the glutaminyl cyclases from Solanum tuberosum and Arabidopsis thaliana: implications for physiological functions
  3. Does human attractin have DP4 activity?
  4. Comparative thermodynamic analysis of cyclic nucleotide binding to protein kinase A
  5. Characterisation and glucoregulatory actions of a novel acylated form of the (Pro3)GIP receptor antagonist in type 2 diabetes
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  10. Metabolic effects of sub-chronic ablation of the incretin receptors by daily administration of (Pro3)GIP and exendin(9–39)amide in obese diabetic (ob/ob) mice
  11. The staphostatin family of cysteine protease inhibitors in the genus Staphylococcus as an example of parallel evolution of protease and inhibitor specificity
  12. The His-Pro-Phe motif of angiotensinogen is a crucial determinant of the substrate specificity of renin
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https://doi.org/10.1515/BC.2007.017
Keywords for this article
adenosine deaminase; attractin; CD26; DASH; dipeptidyl peptidase IV; serum

Articles in the same Issue

  1. l-Arginine influences the structure and function of arginase mRNA in Aspergillus nidulans
  2. Isolation and characterization of the glutaminyl cyclases from Solanum tuberosum and Arabidopsis thaliana: implications for physiological functions
  3. Does human attractin have DP4 activity?
  4. Comparative thermodynamic analysis of cyclic nucleotide binding to protein kinase A
  5. Characterisation and glucoregulatory actions of a novel acylated form of the (Pro3)GIP receptor antagonist in type 2 diabetes
  6. Nef protein of human immunodeficiency virus type 1 binds its own myristoylated N-terminus
  7. Hydrophobic bile salts trigger ceramide formation through endosomal acidification
  8. Apoptotic DNA fragmentation is not related to the phosphorylation state of histone H1
  9. Resveratrol modulates mRNA transcripts of genes related to redox metabolism and cell proliferation in non-small-cell lung carcinoma cells
  10. Metabolic effects of sub-chronic ablation of the incretin receptors by daily administration of (Pro3)GIP and exendin(9–39)amide in obese diabetic (ob/ob) mice
  11. The staphostatin family of cysteine protease inhibitors in the genus Staphylococcus as an example of parallel evolution of protease and inhibitor specificity
  12. The His-Pro-Phe motif of angiotensinogen is a crucial determinant of the substrate specificity of renin
  13. Cysteine protease inhibitors effectively reduce in vivo levels of brain β-amyloid related to Alzheimer's disease
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