Literature DB >> 9710268

Calpain expression varies among different rat and bovine central nervous system regions.

D C Shields1, S K Ray, G Gantt-Wilford, N L Banik.   

Abstract

Calcium-activated neutral proteinase (calpain) is a ubiquitous, cytosolic endopeptidase which is believed to play a role in many neural functions. In the present study, we examined the transcriptional and translational expression of microcalpain (microcalpain) and millicalpain (mcalpain) isoforms and the endogenous inhibitor calpastatin in rat and bovine spinal cord, brain stem, cerebellum, and cerebral cortex tissues using reverse transcriptase-polymerase chain reaction (RT-PCR) and Western blotting. In rat central nervous system (CNS) samples, the microcalpain and mcalpain transcriptional expression was highest in white matter-enriched areas. Calpastatin mRNA expression demonstrated no significant differences among the CNS areas. Calpain and calpastatin translational expression levels were greatest in the spinal cord. In bovine CNS, microcalpain transcriptional expression was greatest in the spinal cord, while other CNS regions showed no significant differences. Bovine mcalpain transcriptional expression was similar among various CNS regions but marginally greater in the cortex. Translational expression of bovine calpain was greatest in the brain stem, while that of calpastatin was highest in the cerebral cortex. These results indicate that calpain expression varies among different CNS regions and is often highest in white matter-enriched areas.

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Year:  1998        PMID: 9710268     DOI: 10.1002/(SICI)1097-4547(19980815)53:4<482::AID-JNR10>3.0.CO;2-4

Source DB:  PubMed          Journal:  J Neurosci Res        ISSN: 0360-4012            Impact factor:   4.164


  4 in total

Review 1.  Regulation of calpain-2 in neurons: implications for synaptic plasticity.

Authors:  Sohila Zadran; Xiaoning Bi; Michel Baudry
Journal:  Mol Neurobiol       Date:  2010-10-06       Impact factor: 5.590

2.  A putative mechanism of demyelination in multiple sclerosis by a proteolytic enzyme, calpain.

Authors:  D C Shields; K E Schaecher; T C Saido; N L Banik
Journal:  Proc Natl Acad Sci U S A       Date:  1999-09-28       Impact factor: 11.205

3.  Calpain inhibition protects spinal motoneurons from the excitotoxic effects of AMPA in vivo.

Authors:  Juan Carlos Corona; Ricardo Tapia
Journal:  Neurochem Res       Date:  2008-01-25       Impact factor: 3.996

4.  Calpain-dependent cleavage of cain/cabin1 activates calcineurin to mediate calcium-triggered cell death.

Authors:  Min-Jung Kim; Dong-Gyu Jo; Gil-Sun Hong; Byung Ju Kim; Michael Lai; Dong-Hyung Cho; Ki-Woo Kim; Arun Bandyopadhyay; Yeon-Mi Hong; Do Han Kim; Chunghee Cho; Jun O Liu; Solomon H Snyder; Yong-Keun Jung
Journal:  Proc Natl Acad Sci U S A       Date:  2002-07-11       Impact factor: 11.205

  4 in total

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