Biochemical and structural insights into mesotrypsin: An unusual human trypsin

Moh'd A. Salameh, Evette S. Radisky

Research output: Contribution to journalReview articlepeer-review

16 Scopus citations

Abstract

Thirty five years ago mesotrypsin was first isolated from the human pancreas. It was described as a minor trypsin isoform with the remarkable property of near total resistance to biological trypsin inhibitors. Another unusual feature of mesotrypsin was discovered later, when it was found that mesotrypsin has defective affinity toward many protein substrates of other trypsins. As the younger sibling of the two major trypsins secreted by the pancreas, cationic and the anionic trypsin, it has been speculated to represent an evolutionary waste with no apparent function. We know now that mesotrypsin is functionally very different from the other trypsins, with novel substrate specificity that hints at distinct physiological functions. Recently, evidence has begun to emerge implicating mesotrypsin in direct involvement in cancer progression. This review will explore the biochemical characteristics of mesotrypsin and structural insights into its specificity, function, and inhibition.

Original languageEnglish (US)
Pages (from-to)129-139
Number of pages11
JournalInternational Journal of Biochemistry and Molecular Biology
Volume4
Issue number3
StatePublished - 2013

Keywords

  • Cancer progression
  • Mesotrypsin
  • Protease inhibitors
  • Protein crystallography
  • Serine protease
  • Substrate specificity
  • Trypsin

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

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