Document Detail


Reversible sedimentation and masking of nerve growth factor (NGF) antigen by high molecular weight fractions from rat brain.
MedLine Citation:
PMID:  9406949     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Nerve growth factor (NGF) was recently found to be largely associated with sedimentable fractions of adult rat brain and treatments of the fractions by alkaline pH increased the measurable amount of their NGF antigen as well as its solubilization [M.C. Hoener, E. Hewitt, J.M. Conner, J.W. Costello and S. Varon, Nerve growth factor (NGF) content in adult rat brain tissues is several-fold higher than generally reported and is largely associated with sedimentable fractions, Brain Res., 728 (1996) 47-56; M.C. Hoener and S. Varon, Effects of sodium chloride, Triton X-100, and alkaline pH on the measurable contents and sedimentability of the nerve growth factor (NGF) antigen in adult rat hippocampal tissue extracts, J. Neurosci. Res., in press (1997); C. Zettler, D.C.McL. Bridges, X.-F. Zhou and R.A. Rush, Detection of increased tissue concentrations of nerve growth factor with improved extraction procedure, J. Neurosci. Res., 46 (1996) 581-594]. We have further investigated the reversibility of these pH effects. Reversal of the pH of an adult rat hippocampal tissue extract from 10.5 to 7.4 led to an almost complete transfer of NGF back from nonsedimentable to sedimentable fractions and to a remasking of the previously unmasked portion of NGF antigen. Thus, molecules causing masking and sedimentation of NGF at pH 7.4 were likely to be present in the alkaline extract. A gel filtration column in PBS, pH 10.5 was used to separate such putative binding molecules from the NGF. All of the NGF antigen from rat hippocampal alkaline extract was found to elute with 19 kDa fractions. The same apparent molecular weight was found for mouse submaxillary beta-NGF and recombinant human beta-NGF. Masking and sedimentation no longer occurred when newly generated 19 kDa rat brain NGF was returned to pH 7.4. When high molecular weight fractions derived from the same gel filtration (in PBS, pH 10.5) were added back to the 19 kDa NGF pool at pH 7.4 and the mixture incubated and centrifuged, the measurability of 19 kDa rat brain NGF antigen was markedly reduced and half of the antigen was recovered in sedimentable fractions. Similar but less dramatic results were obtained when mixing the same high molecular weight fractions with 19 kDa mouse or human beta-NGF. These findings provide new opportunities to identify molecules to which NGF may be bound within intact brain tissues.
Authors:
M C Hoener; S Varon
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Brain research     Volume:  772     ISSN:  0006-8993     ISO Abbreviation:  Brain Res.     Publication Date:  1997 Oct 
Date Detail:
Created Date:  1998-02-19     Completed Date:  1998-02-19     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  0045503     Medline TA:  Brain Res     Country:  NETHERLANDS    
Other Details:
Languages:  eng     Pagination:  1-8     Citation Subset:  IM    
Affiliation:
Department of Biology 0506, University of California San Diego, La Jolla 92093, USA. mhoener@jeeves.ucsd.edu
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MeSH Terms
Descriptor/Qualifier:
Animals
Antigens / isolation & purification*
Brain / immunology*
Centrifugation
Chromatography, Gel
Enzyme-Linked Immunosorbent Assay
Female
Humans
Hydrogen-Ion Concentration
Logistic Models
Mice
Molecular Weight
Nerve Growth Factors / immunology*
Rats
Rats, Sprague-Dawley
Recombinant Proteins / isolation & purification
Solubility
Grant Support
ID/Acronym/Agency:
NS-16349/NS/NINDS NIH HHS
Chemical
Reg. No./Substance:
0/Antigens; 0/Nerve Growth Factors; 0/Recombinant Proteins

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


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