Genealogy of mammalian cysteine proteinase inhibitors

FEBS Letters

Kellermann, Josef²  Lottspeich, Friedrich²  Machleidt, Werner⁴  Fritz, Hans¹  Müller-Esterl, Werner¹  Turk, Vito³ 

[1] Abteilung für Klinische Chemie und Klinische Biochemiein der Chirurgischen Klinik Innenstadt der Universität München,Nussbaumstr. 20, D-8000 München 2, FRG;Max-Planck-Institut für Biochemie, Am Klopferspitz, D-8033 Martinsried, München 2, FRG;Department of Biochemistry, J. Stefan Institute, Jamova 39, Yu-61000 Ljubljana, Yugoslavia;Institut für Physiologische Chemie, Physikalische Biochemie und Zellbiologie, Universität München, Goethestr. 33,D-8000 München 2, FRG

关键词: Cysteine proteinase inhibitor;    Stefin;    Cystatin;    Kininogen;    Evolution;    Sequence homology;   

DOI  :  10.1016/0014-5793(85)80012-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A model for the evolution of mammalian cysteine proteinase inhibitors has been constructed on the basis of sequence homology. This model suggests that the diversity of cysteine proteinase inhibitors has evolved from two ancestral units forming the building blocks of stefin and cystatin. Gene triplication of the archetypal inhibitor generated the kininogen heavy chain which contains three cystatin-like copies. Hence, the superfamily of mammalian cysteine proteinase inhibitors is constituted by at least three distinct families, with stefin, cystatin and kininogen as their prototypes.

【 授权许可】

Unknown