RGD Reference Report - Alteration of the extracellular matrix of smooth muscle cells by ascorbate treatment. - Rat Genome Database

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Alteration of the extracellular matrix of smooth muscle cells by ascorbate treatment.

Authors: Barone, LM  Faris, B  Chipman, SD  Toselli, P  Oakes, BW  Franzblau, C 
Citation: Barone LM, etal., Biochim Biophys Acta. 1985 Jun 18;840(2):245-54.
RGD ID: 9585689
Pubmed: PMID:2859894   (View Abstract at PubMed)

The protein composition in the extracellular matrix of cultured neonatal rat aortic smooth muscle cells has been monitored over time in culture. The influence of ascorbate on insoluble elastin and collagen has been described. In the absence of ascorbate, the cells accumulate an insoluble elastin component which can account for as much as 50% of the total protein in the extracellular matrix. In the presence of ascorbate, the amount of insoluble collagen increases, while the insoluble elastin content is significantly less. When ascorbate conditions are varied at different times during the culture, the extracellular matrices are altered with respect to collagen and elastin ratios. The decrease in elastin accumulation in the presence of ascorbate may be explained by an overhydroxylation of tropoelastin. Approximately 1/3 of the prolyl residues in the soluble elastin fractions isolated from cultures grown in the presence of ascorbate are hydroxylated. Since the insoluble elastin accumulated in these cultures contain the unique lysine-derived cross-links in amounts comparable to aortic tissue, this culture system proves ideal for studying the influence of extracellular matrix elastin on cell growth and metabolism.



Gene Ontology Annotations    Click to see Annotation Detail View

Biological Process

  
Object SymbolSpeciesTermQualifierEvidenceWithNotesSourceOriginal Reference(s)
ElnRatcellular response to L-ascorbic acid  IEP  RGD 

Objects Annotated

Genes (Rattus norvegicus)
Eln  (elastin)


Additional Information