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Chinese Journal of Clinical Pharmacology and Therapeutics ›› 2006, Vol. 11 ›› Issue (6): 601-605.

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Overview and research progress of dipetidyl peptidase I

YANG Ya-bin, YUAN Sheng-tao, ZHANG Lu-yong   

  1. Jiangsu Center for drugscreening, China Pharmaceutical University, Nanjing 210038, Jiangsu, China
  • Received:2006-04-11 Revised:2006-05-15 Online:2006-06-26 Published:2020-12-04

Abstract: Dipeptidyl peptidase I (DPPI), a lysosomal cysteine proteinase also known as cathepsin C, functions as a key enzyme in the activation of many granule serine proteases in the granules of activated cytotoxic T lymphocytes and natural killer cells (granzymes A and B), mast cells (chymase and tryptase), and neutrophils (cathepsin G, proteinase 3 and elastase).It is well established that DPPI-deficient mice have severe defects in serine protease activities in these hemopoietic lineages.In light of the present investigators'work regarding the important role of DPPI-dependent effector on mechanisms in several human pathophysiological processes, the development of selective DPPI inhibitors would provide an important therapeutic tool in the treatment of immune inflammation lymphoma-related diseases.

Key words: dipeptidyl peptidase I, cathepsin C, proenzyme activation, Papillon-Lefevre syndrome, enzyme inhibitor

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