Document Detail


Cysteine string protein beta is prominently associated with nerve terminals and secretory organelles in mouse brain.
MedLine Citation:
PMID:  20338151     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Cysteine string proteins (CSPs) are associated with regulated secretory organelles in organisms ranging from fruit flies to man. Mammals have three csp genes (alpha, beta and gamma), and previous work indicated that expression of the csp-beta and -gamma genes was restricted to the testes. For the current investigation, antibodies specific for CSP-beta were developed. Unexpectedly, immunoblot analysis indicated that CSP-beta was prominently expressed throughout mouse brain. Upon sub-cellular fractionation, CSP-beta was enriched in synaptosomes and synaptic vesicle fractions. Interestingly, CSP-beta existed almost exclusively as part of a high mass complex both in testis and brain. This complex required aggressive denaturation to release monomeric CSP-beta. By Northern analysis CSP-beta mRNA was present at very low abundance as a approximately 1.0kb species in mouse brain. Collectively, the enrichment of CSP-beta in synaptosomes and the association of CSP-beta with synaptic vesicles suggest that CSP-beta, like CSP-alpha, may be an important component of the regulated secretory machinery in mouse brain.
Authors:
Cameron B Gundersen; Sirus A Kohan; Puneet Souda; Julian P Whitelegge; Joy A Umbach
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2010-03-23
Journal Detail:
Title:  Brain research     Volume:  1332     ISSN:  1872-6240     ISO Abbreviation:  Brain Res.     Publication Date:  2010 May 
Date Detail:
Created Date:  2010-05-07     Completed Date:  2010-08-10     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0045503     Medline TA:  Brain Res     Country:  Netherlands    
Other Details:
Languages:  eng     Pagination:  1-11     Citation Subset:  IM    
Copyright Information:
Copyright 2010 Elsevier B.V. All rights reserved.
Affiliation:
The Department of Molecular and Medical Pharmacology, David Geffen School of Medicine at UCLA, Los Angeles, CA 90095, USA. cgundersen@mednet.ucla.edu
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Animals
Blotting, Northern
Brain / metabolism*
HSP40 Heat-Shock Proteins / genetics,  metabolism*
Heart Ventricles / metabolism
Male
Membrane Proteins / genetics,  metabolism*
Mice
Mice, Inbred C57BL
Molecular Sequence Data
Neurons / metabolism*
RNA, Messenger / metabolism
Synapses / metabolism*
Synaptic Vesicles / metabolism*
Synaptosomes / metabolism*
Testis / metabolism
Xenopus
Chemical
Reg. No./Substance:
0/HSP40 Heat-Shock Proteins; 0/Membrane Proteins; 0/RNA, Messenger; 0/cysteine string protein

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


Previous Document:  Reprogramming of somatic cells induced by fusion of embryonic stem cells using hemagglutinating viru...
Next Document:  Whisker stimulation increases expression of nerve growth factor- and interleukin-1beta-immunoreactiv...