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Novel Members of Mammalian Kexin Family Proteases, Pace 4C, Pace 4D, PC 7A and PC 7B

  • Y. Matsuda
  • A. Tsuji
  • H. Nagamume
  • T. Akamatsu
  • C. Hine
  • K. Muramatsu
  • K. Mori
  • Y. Tamai
  • K. Yonemoto
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 389)

Abstract

Biologically active peptides, such as peptide hormones, neuropeptides and growth factors, are known to be synthesized as larger precursor proteins and converted to active peptides by proteolytic cleavage at the carboxyl side of paired basic amino acids1,2,3. This process is found also in the activation of membrane-bound receptor proteins such as insulin receptor and many secreted proteins like serum albumin. Kexin family proteases were identified as processing proteases for these proteins; they share a subtilisin-like catalytic domain and require calcium ion for their activities2,3. Kexin family proteases are widely distributed in nature, from yeast, to mammals4,5,6. Currently seven mammalian kexins have been reported: furin4, PCI/37, PC2,8 PACE45,6, PC49, PC5/610, and PC7 11.

Keywords

Paired Basic Amino Acid 
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

© Plenum Press, New York 1996

Authors and Affiliations

  • Y. Matsuda
    • 1
  • A. Tsuji
    • 1
  • H. Nagamume
    • 1
  • T. Akamatsu
    • 1
  • C. Hine
    • 1
  • K. Muramatsu
    • 1
  • K. Mori
    • 1
  • Y. Tamai
    • 1
  • K. Yonemoto
    • 1
  1. 1.Department of Biological Science and Technology Faculty of EngineeringThe University of TokushimaTokushimaJapan

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