Document Detail


Role of mu-calpain in proteolytic cleavage of brain L-glutamic acid decarboxylase.
MedLine Citation:
PMID:  18377878     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Glutamic acid decarboxylase (GAD) is the rate-limiting enzyme for gamma-aminobutyric acid (GABA) biosynthesis. Previously, we reported the presence of truncated forms of GAD in vivo and in vitro. In addition, an unidentified endogenous protease responsible for proteolytic cleavage of full-length GAD (fGAD) to its truncated form (tGAD) was also observed. In this communication, we report that mu-calpain is a good candidate for conversion of fGAD(67) to tGAD(67). This conclusion is based on the following observations: 1. purified recombinant GAD(67) is cleaved by mu-calpain at specific sites; 2. in brain synaptosomal preparation, GAD(67) is cleaved to its truncated form by an endogenous protease which is inhibited by specific calpain inhibitors; 3. in mu-calpain knockout mice, the level of tGAD in the brain is greatly reduced compared with the wild type; 4. when mu-calpain gene is silenced by siRNA, the level of tGAD is also markedly reduced compared to the control group; and 5. mu-calpain is activated by neuronal stimulation and Ca(2+)-influx. The physiological significance of calpain in regulation of GABA synthesis and GABAergic neurotransmission is also discussed.
Authors:
Di Sha; Ying Jin; Heng Wu; Jianning Wei; Chun-Hua Lin; Yi-Hsuan Lee; Chandana Buddhala; Shafi Kuchay; Athar H Chishti; Jang-Yen Wu
Related Documents :
18439218 - Co-localization of excitatory and inhibitory transmitters in the brain.
21044648 - A modified rapid enzymatic microtiter plate assay for the quantification of intracellul...
1749748 - Clonidine differentially modulates the release of endogenous gaba in various rat brain ...
18372188 - Comparative studies of 177lu-edtmp and 177lu-dotmp as potential agents for palliative r...
14756528 - Cloning and expression of pyrroloquinoline quinone (pqq) genes from a phosphate-solubil...
10561598 - Neu5acalpha3gal is part of the helicobacter pylori binding epitope in polyglycosylceram...
Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.     Date:  2008-03-04
Journal Detail:
Title:  Brain research     Volume:  1207     ISSN:  0006-8993     ISO Abbreviation:  Brain Res.     Publication Date:  2008 May 
Date Detail:
Created Date:  2008-04-18     Completed Date:  2008-08-13     Revised Date:  2009-11-18    
Medline Journal Info:
Nlm Unique ID:  0045503     Medline TA:  Brain Res     Country:  Netherlands    
Other Details:
Languages:  eng     Pagination:  9-18     Citation Subset:  IM    
Affiliation:
Department of Biomedical Sciences, Florida Atlantic University, Boca Raton, FL 33431, USA.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Animals
Brain / drug effects,  metabolism*,  ultrastructure
Calcium / metabolism
Calpain / pharmacology,  physiology*
Cells, Cultured
Cyclic AMP-Dependent Protein Kinases / pharmacology
Enzyme-Linked Immunosorbent Assay / methods
Gene Deletion
Glutamate Decarboxylase / drug effects,  metabolism*
Mice
Mice, Knockout / genetics
Neurons / drug effects,  physiology
Protein Processing, Post-Translational
RNA, Small Interfering / genetics,  pharmacology
Rats
Rats, Sprague-Dawley
Subcellular Fractions
Synaptosomes / drug effects,  metabolism
Transfection / methods
Grant Support
ID/Acronym/Agency:
NS37851/NS/NINDS NIH HHS; R01 NS037851-04/NS/NINDS NIH HHS
Chemical
Reg. No./Substance:
0/RNA, Small Interfering; 7440-70-2/Calcium; EC 2.7.11.11/Cyclic AMP-Dependent Protein Kinases; EC 3.4.22.-/Calpain; EC 3.4.22.-/mu-calpain; EC 4.1.1.15/Glutamate Decarboxylase; EC 4.1.1.15/glutamate decarboxylase 1
Comments/Corrections

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  Multielectrode array recordings reveal physiological diversity of intrinsically photosensitive retin...
Next Document:  Hyperpolarization-activated current (I(h)) contributes to excitability of primary sensory neurons in...