Abstract
Primate arterial smooth muscle cells and skin fibroblasts were examined for their ability to synthesize elastin in culture. In the presence of the lathyrogen beta-aminopropionitrile, the smooth muscle cells incorporate [3H]lysine into a lysyl oxidase substrate that was present in the medium and associated with the cell layer. A component having a mol wt of 72,000 and an electrophoretic mobility similar to that of authentic tropoelastin was isolated from the labeled smooth muscle cells by coacervation and fractionation with organic solvents. In the absence of beta-aminopropionitrile, long-term cultures of smooth muscle cells incorporated [14C]lysine into desmosine and isodesmosine, the cross-link amino acids unique to elastin. In contrast, no desmosine formation occurred in the fibroblast cultures. These characteristics demonstrate that arterial smooth muscle cells are capable of synthesizing both soluble and cross-lined elastin in culture.
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Selected References
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- Abraham P. A., Smith D. W., Carnes W. H. Synthesis of soluble elastin by aortic medial cells in culture. Biochem Biophys Res Commun. 1974 Jun 4;58(3):597–604. doi: 10.1016/s0006-291x(74)80461-4. [DOI] [PubMed] [Google Scholar]
- Green R. A., Foster J. A., Sandberg L. B. Rapid procedure for the isolation of polyfunctional amino acids in elastin. Anal Biochem. 1973 Apr;52(2):538–541. doi: 10.1016/0003-2697(73)90059-6. [DOI] [PubMed] [Google Scholar]
- Greenlee T. K., Jr, Ross R., Hartman J. L. The fine structure of elastic fibers. J Cell Biol. 1966 Jul;30(1):59–71. doi: 10.1083/jcb.30.1.59. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Miller E. J., Martin G. R., Mecca C. E., Piez K. A. The biosynthesis of elastin cross-links. The effect of copper deficiency and a lathyrogen. J Biol Chem. 1965 Sep;240(9):3623–3627. [PubMed] [Google Scholar]
- Narayanan A. S., Page R. C., Martin G. R. On the preparation of tropoelastin from embryonic chick aorta. Biochim Biophys Acta. 1974 May 10;351(1):126–132. doi: 10.1016/0005-2795(74)90071-3. [DOI] [PubMed] [Google Scholar]
- Peterkofsky B., Diegelmann R. Use of a mixture of proteinase-free collagenases for the specific assay of radioactive collagen in the presence of other proteins. Biochemistry. 1971 Mar 16;10(6):988–994. doi: 10.1021/bi00782a009. [DOI] [PubMed] [Google Scholar]
- Ross R., Bornstein P. The elastic fiber. I. The separation and partial characterization of its macromolecular components. J Cell Biol. 1969 Feb;40(2):366–381. doi: 10.1083/jcb.40.2.366. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Ross R., Klebanoff S. J. The smooth muscle cell. I. In vivo synthesis of connective tissue proteins. J Cell Biol. 1971 Jul;50(1):159–171. doi: 10.1083/jcb.50.1.159. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Ross R. The smooth muscle cell. II. Growth of smooth muscle in culture and formation of elastic fibers. J Cell Biol. 1971 Jul;50(1):172–186. doi: 10.1083/jcb.50.1.172. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Siegel R. C., Martin G. R. Collagen cross-linking. Enzymatic synthesis of lysine-derived aldehydes and the production of cross-linked components. J Biol Chem. 1970 Apr 10;245(7):1653–1658. [PubMed] [Google Scholar]
- Smith D. W., Brown D. M., Carnes W. H. Preparation and properties of salt-soluble elastin. J Biol Chem. 1972 Apr 25;247(8):2427–2432. [PubMed] [Google Scholar]
- Veis A., Anesey J. Modes of intermolecular cross-linking in mature insoluble collagen. J Biol Chem. 1965 Oct;240(10):3899–3908. [PubMed] [Google Scholar]
- Weber K., Osborn M. The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis. J Biol Chem. 1969 Aug 25;244(16):4406–4412. [PubMed] [Google Scholar]