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AbstractAbstract
[en] Aortic smooth muscles cells have been implicated in the etiology of lesions which occur in atherosclerosis and hypertension. Both diseases involve proliferation of smooth muscle cells and accumulation of excessive amounts of extracellular matrix proteins, including collagen type I and type III produced by the smooth muscle cells. To better understand the sites of regulation of collagen biosynthesis and to correlate these with the growth rate of the cells, cultured bovine aortic smooth muscle cells were studied as a function of the number of days (3 to 14) in second passage. Cells grew rapidly up to day 6 when confluence was reached. The total incorporation of [3H]-proline into proteins was highest at day 3 and decreased to a constant level after the cultures reached confluence. In contrast, collagen protein production was lowest before confluence and continued to increase over the entire time course of the experiments. cDNA clones for the α1 and α2 chains of type I and the α1 chain of type III collagen were used to quantitate the steady state level of collagen mRNAs. RNA was tested in a cell-free translation system. Changes in the translational activity of collagen mRNAs parallelled the observed increases in collagen protein production. Thus, at later time points, collagen mRNAs are more active in directing synthesis of preprocollagens, even though less collagen mRNA is present. The conclusion is that the site of regulation of the expression of collagen genes is a function of the growth rate of cultured smooth muscle cells
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Source
1986; 169 p; University Microfilms Order No. 86-06,870; Thesis (Ph. D.).
Record Type
Report
Literature Type
Thesis/Dissertation
Country of publication
AMINES, AMINO ACIDS, ANIMALS, ARTERIES, AZOLES, BLOOD VESSELS, BODY, CARBOXYLIC ACIDS, CARDIOVASCULAR SYSTEM, DOMESTIC ANIMALS, HETEROCYCLIC ACIDS, HETEROCYCLIC COMPOUNDS, HYDROGEN COMPOUNDS, MAMMALS, ORGANIC ACIDS, ORGANIC COMPOUNDS, ORGANIC NITROGEN COMPOUNDS, ORGANS, PROTEINS, PYRROLES, PYRROLIDINES, RUMINANTS, SCLEROPROTEINS, SYNTHESIS, VERTEBRATES
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