Cellular and Molecular Life Sciences

, Volume 65, Issue 16, pp 2541–2553

Recent progress in understanding the diversity of the human ov-serpin/clade B serpin family

  • K. Izuhara
  • S. Ohta
  • S. Kanaji
  • H. Shiraishi
  • K. Arima
Review

DOI: 10.1007/s00018-008-8049-7

Cite this article as:
Izuhara, K., Ohta, S., Kanaji, S. et al. Cell. Mol. Life Sci. (2008) 65: 2541. doi:10.1007/s00018-008-8049-7

Abstract.

The inhibitory mechanism against proteases is important in the maintenance of homeostasis or health in the body. The human ovalbumin serpin (ovserpin)/ clade B serpin family is one group of the human serpins, a family of serine protease inhibitors. They have acquired diversity in the profiles of target proteases, inhibitory mechanisms, and localization patterns during their evolution. Most serpins target serine proteases, however, some ov-serpins target only cysteine proteases or both serine and cysteine proteases and furthermore, several ov-serpins do not possess inhibitory activities. Although the ov-serpins act primarily as intracellular serpins, some show extracellular and nuclear localizations. Such diversity enables the ov-serpins to play multiple physiological roles in the body. Recent analyses have revealed that the functions of human ov-serpins are more diversified than we previously knew. In this article, we describe recent progress in our understanding of how the human ov-serpin/clade B serpin family demonstrates diversity.

Keywords.

Serpin ov-serpin clade B evolution cysteine protease secretion nuclear serpin localization 

Copyright information

© Birkhaueser 2008

Authors and Affiliations

  • K. Izuhara
    • 1
    • 2
  • S. Ohta
    • 2
  • S. Kanaji
    • 1
  • H. Shiraishi
    • 1
  • K. Arima
    • 1
  1. 1.Department of Biomolecular SciencesSaga Medical SchoolSagaJapan
  2. 2.Department of Clinical Chemistry and Laboratory MedicineSaga Medical SchoolSagaJapan

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