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Five different collagen chains and one smaller collagenous fragment have been isolated from the collagens found in the combined cell layer and medium of rhesus monkey aortic smooth muscle cell cultures. The collagen chains which can be identified are alpha1 (III), alpha1(I), alpha2, A and B. The smaller collagenous peptide exhibits an apparent molecular weight of 45 000 and has been designated CP45 (Mayne, R., et al. (1977), Arch. Biochem. Biophys. 181, 462). Smooth muscle cells continue to synthesize the collagens from which these components are derived for at least eight passages in culture. At each passage the alpha1 (III) chain consistently represents about one-half of the total collagen which is recovered after initial fractionation by agarose gel chromatography. The results show that smooth muscle cells derived from rhesus monkey thoracic aorta are phenotypically stable for many generations in vitro.
R Mayne, and
M S Vail, and
E J Miller
March 1977,
Hoppe-Seyler's Zeitschrift fur physiologische Chemie,
R Mayne, and
M S Vail, and
E J Miller
May 1983,
The Journal of biological chemistry,
R Mayne, and
M S Vail, and
E J Miller
May 1987,
The Journal of biological chemistry,
R Mayne, and
M S Vail, and
E J Miller
May 1985,
Proceedings of the National Academy of Sciences of the United States of America,
R Mayne, and
M S Vail, and
E J Miller
April 1984,
Hoppe-Seyler's Zeitschrift fur physiologische Chemie,
R Mayne, and
M S Vail, and
E J Miller
April 1975,
Biochimica et biophysica acta,
R Mayne, and
M S Vail, and
E J Miller
June 1980,
Nature,
R Mayne, and
M S Vail, and
E J Miller
November 1979,
The Journal of pharmacology and experimental therapeutics,
R Mayne, and
M S Vail, and
E J Miller
May 1988,
Biochemical and biophysical research communications,
R Mayne, and
M S Vail, and
E J Miller
January 1992,
Connective tissue research,
