Literature DB >> 2985077

Binding to erythrocyte membrane is the physiological mechanism for activation of Ca2+-dependent neutral proteinase.

S Pontremoli, E Melloni, B Sparatore, F Salamino, M Michetti, O Sacco, B L Horecker.   

Abstract

In the presence of micromolar concentrations of Ca2+ the catalytic 80 kDa subunit of human erythrocyte procalpain binds to the cytosolic surface of the erythrocyte membrane. Binding is rapid, highly specific and is reversed by the removal of Ca2+. In the bound form the 80 kDa catalytic subunit undergoes a rapid conversion to calpain, the active 75 kDa Ca2+-requiring proteinase. The activated proteinase produces extensive degradation of membrane components, particularly of band 4.1 and 2.1 proteins. Binding to membranes may represent an obligatory physiological mechanism for the conversion of procalpain to calpain.

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Year:  1985        PMID： 2985077     DOI： 10.1016/0006-291x(85)91683-3

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN： 0006-291X            Impact factor:   3.575


  14 in total

1.  Calcium-activated neutral protease activities in brain trauma.

Authors:  E Arrigoni; F Cohadon
Journal:  Neurochem Res       Date:  1991-04       Impact factor: 3.996

2.  Investigation of the structural basis of the interaction of calpain II with phospholipid and with carbohydrate.

Authors:  C Crawford; N R Brown; A C Willis
Journal:  Biochem J       Date:  1990-01-15       Impact factor: 3.857

3.  A possible physiological role of the Ca-dependent protease calpain and its inhibitor calpastatin on the Ca current in guinea pig myocytes.

Authors:  B Belles; J Hescheler; W Trautwein; K Blomgren; J O Karlsson
Journal:  Pflugers Arch       Date:  1988-10       Impact factor: 3.657

4.  Binding of protein kinase C to neutrophil membranes in the presence of Ca2+ and its activation by a Ca2+-requiring proteinase.

Authors:  E Melloni; S Pontremoli; M Michetti; O Sacco; B Sparatore; F Salamino; B L Horecker
Journal:  Proc Natl Acad Sci U S A       Date:  1985-10       Impact factor: 11.205

5.  An endogenous activator of the Ca2+-dependent proteinase of human neutrophils that increases its affinity for Ca2+.

Authors:  S Pontremoli; E Melloni; M Michetti; F Salamino; B Sparatore; B L Horecker
Journal:  Proc Natl Acad Sci U S A       Date:  1988-03       Impact factor: 11.205

6.  Site-directed activation of calpain is promoted by a membrane-associated natural activator protein.

Authors:  F Salamino; R De Tullio; P Mengotti; P L Viotti; E Melloni; S Pontremoli
Journal:  Biochem J       Date:  1993-02-15       Impact factor: 3.857

7.  Degradation of skeletal muscle plasma membrane proteins by calpain.

Authors:  S I Zaidi; H T Narahara
Journal:  J Membr Biol       Date:  1989-09       Impact factor: 1.843

8.  Mechanisms of antagonistic action of internal Ca2+ on serotonin-induced potentiation of Ca2+ currents in Helix neurones.

Authors:  P G Kostyuk; E A Lukyanetz
Journal:  Pflugers Arch       Date:  1993-06       Impact factor: 3.657

9.  Calcium dependent thiol protease caldonopain and its specific endogenous inhibitor in Leishmania donovani.

Authors:  J Bhattacharya; R Dey; S C Datta
Journal:  Mol Cell Biochem       Date:  1993-09-08       Impact factor: 3.396

10.  Widespread activation of calcium-activated neutral proteinase (calpain) in the brain in Alzheimer disease: a potential molecular basis for neuronal degeneration.

Authors:  K Saito; J S Elce; J E Hamos; R A Nixon
Journal:  Proc Natl Acad Sci U S A       Date:  1993-04-01       Impact factor: 11.205
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