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Molecular Analyses of Human and Rat Dipeptidyl Peptidase IV

  • C. A. Abbott
  • M. D. Gorrell
  • M. T. Levy
  • G. W. Mccaughan
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 421)

Abstract

Dipeptidyl peptidase IV (DPP IV) is a highly glycosylated 110 kDa multifunctional protease. DPP IV has a broad tissue distribution but is mainly expressed in epithelial cells, endothelial cells and lymphocytes in both rat and human tissues1–3. DPP IV on the human T cell surface binds or coassociates with adenosine deaminase (ADA)4, 5, collagen6–8 and CD459 and has a role in T cell costimulation7, 10. Our group has investigated the role of DPP IV in hepatocyte function. DPP IV levels are altered during liver regeneration11, human cirrhosis12 and liver tumorigenesis13. It is still unclear which DPP IV functions are involved in hepatocyte growth and regulation. DPP IV is a type II protein, its N terminus is anchored to the cell surface through a hydrophobic domain with a short, six amino acid cytoplasmic tail. Thus, most of the protein is extracellular. Recent work in our group has concentrated on understanding the DPP IV glycoprotein at the molecular level.

Keywords

Adenosine Deaminase Catalytic Triad Dipeptidyl Peptidase Prolyl Endopeptidase Serine Protease Family 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer Science+Business Media New York 1997

Authors and Affiliations

  • C. A. Abbott
    • 1
  • M. D. Gorrell
    • 1
  • M. T. Levy
    • 1
  • G. W. Mccaughan
    • 1
  1. 1.A.W Morrow Gastroenterology and Liver Centre Centenary Institute for Cancer Medicine and Cell BiologyRoyal Prince Alfred HospitalSydneyAustralia

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