Modulation of procarboxypeptidase R (ProCPR) activation by complementary peptides to thrombomodulin

Yasuyo Shimomura, Takeshi Kawamura, Hidefumi Komura, William Campbell, Noriko Okada, Hidechika Okada

Research output: Contribution to journalArticlepeer-review

9 Citations (Scopus)


We designed complementary peptides (C-peptides) using a novel computer program (MIMETIC), which generates a series of peptides designed to interact with a target peptide sequence. Carboxypeptidase R (CPR) is an unstable basic carboxypeptidase found in fresh serum in addition to carboxypeptidase N (CPN) which is stable. CPR is generated from its precursor form (proCPR) by trypsinlike enzymes, and its activation is mediated by thrombin generated in the coagulation cascade. The efficiency of activation is enhanced approximately 1,200-fold when thrombin (T) is bound to thrombomodulin (TM). We attempted to generate C-peptides which recognize the T-binding site within TM assuming that some of these might interfere with the generation of T and TM complexes (T-TM). Among three peptides designed, two inhibited the enhancement in activation of proCPR by T in the presence of TM. One of the peptides at 16 μM reduced the activation of proCPR to the level obtained by T alone.

Original languageEnglish
Pages (from-to)241-245
Number of pages5
Issue number3
Publication statusPublished - 2003
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Microbiology
  • Immunology
  • Virology


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