Literature DB >> 1922659

Calcium-activated neutral protease activities in brain trauma.

E Arrigoni1, F Cohadon.   

Abstract

This paper investigates the level of cytosolic and synaptosomal forms of calcium activated neutral protease activities in the normal brain and their changes following a freezing lesion in the rabbit. From 1 to 24 hours post lesion we observe a progressive disappearing of the enzyme activities from the cytosolic compartment and concurrently their increase in the membranal fraction. These changes are likely to be due to a rise in intracellular calcium concentration, a well documented consequence of many cellular insults. The specific role of the activation of calpain activities in the pathophysiology of trauma is discussed, an enhancement of excitotoxic mechanisms is proposed.

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Year:  1991        PMID: 1922659     DOI: 10.1007/bf00965570

Source DB:  PubMed          Journal:  Neurochem Res        ISSN: 0364-3190            Impact factor:   3.996


  47 in total

Review 1.  Calcium, neuronal hyperexcitability and ischemic injury.

Authors:  F B Meyer
Journal:  Brain Res Brain Res Rev       Date:  1989 Jul-Sep

2.  A NEUTRAL, CALCIUM-ACTIVATED PROTEINASE FROM THE SOLUBLE FRACTION OF RAT BRAIN.

Authors:  G GUROFF
Journal:  J Biol Chem       Date:  1964-01       Impact factor: 5.157

3.  Effects of CDP-choline on phospholipase A2 and cholinephosphotransferase activities following a cryogenic brain injury in the rabbit.

Authors:  E Arrigoni; N Averet; F Cohadon
Journal:  Biochem Pharmacol       Date:  1987-11-01       Impact factor: 5.858

4.  Calpain and calpastatin levels in different organs of the rabbit.

Authors:  K Blomgren; E Nilsson; J O Karlsson
Journal:  Comp Biochem Physiol B       Date:  1989

5.  Subcellular compartmentalization of calcium-dependent and calcium-independent neutral proteases in brain.

Authors:  M Baudry; R DuBrin; G Lynch
Journal:  Synapse       Date:  1987       Impact factor: 2.562

6.  The ultrastructural localization of calcium-activated protease "calpain" in rat brain.

Authors:  L S Perlmutter; R Siman; C Gall; P Seubert; M Baudry; G Lynch
Journal:  Synapse       Date:  1988       Impact factor: 2.562

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

Authors:  S Pontremoli; E Melloni; B Sparatore; F Salamino; M Michetti; O Sacco; B L Horecker
Journal:  Biochem Biophys Res Commun       Date:  1985-04-16       Impact factor: 3.575

Review 8.  Glutamate and the pathophysiology of hypoxic--ischemic brain damage.

Authors:  S M Rothman; J W Olney
Journal:  Ann Neurol       Date:  1986-02       Impact factor: 10.422

9.  Ca2+-dependent neutral proteinase from human erythrocytes: activation by Ca2+ ions and substrate and regulation by the endogenous inhibitor.

Authors:  E Melloni; F Salamino; B Sparatore; M Michetti; S Pontremoli
Journal:  Biochem Int       Date:  1984-04

10.  Muscular dystrophy: inhibition of degeneration in vivo with protease inhibitors.

Authors:  A Stracher; E B McGowan; S A Shafiq
Journal:  Science       Date:  1978-04-07       Impact factor: 47.728

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  2 in total

1.  Specificity of calcium-activated neutral proteinase (CANP) inhibitors for human mu CANP and mCANP.

Authors:  K Saito; R A Nixon
Journal:  Neurochem Res       Date:  1993-02       Impact factor: 3.996

2.  Temporal relationship of peroxynitrite-induced oxidative damage, calpain-mediated cytoskeletal degradation and neurodegeneration after traumatic brain injury.

Authors:  Ying Deng; Brian M Thompson; Xiang Gao; Edward D Hall
Journal:  Exp Neurol       Date:  2007-02-03       Impact factor: 5.330

  2 in total

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