Document Detail

Racemization of aspartic acid in human articular cartilage.
MedLine Citation:
PMID:  1468204     Owner:  NLM     Status:  MEDLINE    
The rate of racemization of aspartic acid was measured in young and aged human femoral head cartilage. Normal femoral heads were obtained at postmortem, osteoarthritic specimens at operations for total hip replacement. In order to distinguish between the aspartic acid racemization in collagen from that in proteoglycan (PG), in addition to native tissue, we tested cartilage specimens from which PG had been enzymatically removed. Preliminary results indicate that there is only a very slow collagen turnover in normal adult cartilage. The same is true of residual cartilage from osteoarthritic femoral heads, indicating no rapid repair except where osteophytes are formed. Native, PG-containing cartilage, whether normal or osteoarthritic was found to have unexpectedly high racemization rates.
A Maroudas; G Palla; E Gilav
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Connective tissue research     Volume:  28     ISSN:  0300-8207     ISO Abbreviation:  Connect. Tissue Res.     Publication Date:  1992  
Date Detail:
Created Date:  1993-01-28     Completed Date:  1993-01-28     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0365263     Medline TA:  Connect Tissue Res     Country:  ENGLAND    
Other Details:
Languages:  eng     Pagination:  161-9     Citation Subset:  IM    
Julius Silver Institute of Biomedical Sciences, Department of Biomedical Engineering, Technion-Israel Institute of Technology, Haifa.
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MeSH Terms
Aged, 80 and over
Aspartic Acid / chemistry,  metabolism*
Cartilage, Articular / chemistry,  metabolism*,  physiopathology
Femur Head / chemistry,  metabolism,  physiopathology
Osteoarthritis / metabolism,  physiopathology
Racemases and Epimerases / chemistry,  metabolism*
Reg. No./Substance:
56-84-8/Aspartic Acid; EC 5.1.-/Racemases and Epimerases

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