Collagen polymorphism in cell cultures derived from guinea pig aortic smooth muscle: Comparison with three populations of fibroblasts

Mayne, Richard; Vail, Margaret S.; Miller, Edward J.; Blose, Stephen H.; Chacko, Samuel

doi:10.1016/0003-9861(77)90252-1

Cited by 43 publications

(29 citation statements)

References 33 publications

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“…Previous studies in which cells or tissues were labeled in the presence of @-aminopropionitrile, and the collagen subsequently isolated by limited proteolysis with pepsin at low temperature, have shown that type 111 collagen is extracted entirely as a y component consisting of three disulfide-bonded a1 (111) chains (Chung et al, 1975;Mayne et al, 1977). T h e y component isolated from monkey smooth muscle cell cultures also consisted entirely of type 111 collagen and this was shown in several ways.…”

Section: Resultsmentioning

confidence: 99%

“…In most experiments collagen was isolated from the combined cell layer, medium, and wash as described in previous publications (Mayne et al, 1975(Mayne et al, ,1977, with theexception that pepsin was present a t concentrations of either 100 pg/mL or 1 mg/mL. Occasionally, the medium and the cell layer were analyzed separately in which case human type I collagen (0.1 mg/mL) was dissolved in the medium before precipitation with ammonium sulfate (25% saturation).…”

Section: Methodsmentioning

confidence: 99%

“…These were performed as described in an earlier publication (Mayne et al, 1977). EFFLUENT VOLUME, rnl.…”

Section: Methodsmentioning

confidence: 99%

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Characterization of the collagen chains synthesized by cultured smooth muscle cells derived from rhesus monkey thoracic aorta

Mayne¹,

Vail²,

Miller³

1978

Biochemistry

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129

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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.

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Section: Resultsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

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Characterization of the collagen chains synthesized by cultured smooth muscle cells derived from rhesus monkey thoracic aorta

Mayne¹,

Vail²,

Miller³

1978

Biochemistry

Self Cite

129

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“…Endothelial cells which are believed to synthesize type IV 36 collagen~vivo (Howard,~~, 1976, Barnes, et~., 1978, synthesize (McCullough and Balian, 1975;Leung, et i,l, 1976, Barnes, et i,l, 1976, Mayne,~~, 1977. In the case of human fetal smooth muscle cells only type I was detected in culture (Layman and Titus, 1975).…”

Section: B the Phenotypic Alteration Of Collagen Types In Culturementioning

confidence: 99%

The Differentiated State of Normal and Malignant Cells or How to Define a “Normal” Cell in Culture

Bissell

1981

International Review of Cytology

198

112

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“…These cells synthesize various matrix proteins including proteoglycan (1), elastin (2), and types I, III, and V collagen (3)(4)(5)(6). Because atherosclerotic plaques are composed in large part of smooth muscle cells and the extracellular products they produce (7), there is much interest in factors that regulate the growth and distribution of these cells.…”

mentioning

confidence: 99%

Attachment of smooth muscle cells to collagen and their migration toward platelet-derived growth factor.

Grotendorst¹,

Seppä²,

Kleinman³

et al. 1981

Proc. Natl. Acad. Sci. U.S.A.

434

154

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Smooth muscle cells use fibronectin to bind to type I and type Im collagens but bind to type V collagen by a trypsin-resistant intrinsic glycoconjugate. The binding site on type V collagen is located in the aA chain. By using collagen-coated filters in a modified Boyden chamber assay for chemotaxis, it was observed that the platelet-derived growth factor was chemotactic for smooth muscle cells but that several other growth factors were inactive. We suggest that the migration of smooth muscle cells from the media to the intima of a blood vessel, which leads to the formation of an atherosclerotic plaque, may be the result of a chemotactic migration of cells responsive to the platelet-derived growth factor.Smooth muscle cells are connective tissue cells that are present in blood vessels and other pulsatile tissues. These cells synthesize various matrix proteins including proteoglycan (1), elastin (2), and types I, III, and V collagen (3)(4)(5)(6). Because atherosclerotic plaques are composed in large part of smooth muscle cells and the extracellular products they produce (7), there is much interest in factors that regulate the growth and distribution of these cells.Current theories suggest that the formation of the atherosclerotic plaque is initiated at sites where endothelial cells are lost from the basement membrane (for reviews, see refs. 7-9), leading to an accumulation ofplatelets and other blood elements at those sites. Under such conditions, platelets release the platelet-derived growth factor (PDGF), a potent mitogen for smooth muscle but not for endothelial cells (10,11). It is assumed that PDGF causes the proliferation of smooth muscle cells beyond the basement membrane to the inner surface of the blood vessel. Interestingly, Benditt and Benditt (12) found that the cells in many plaques are monoclonal suggesting that a single cell or a single type of cell (13) proliferated to form a plaque.Recently, we and others have studied the attachment and migration of connective tissue cells. Fibroblasts, for example, are attracted to lymphokines (14), macrophage factors (15), activated serum (16), fibronectin (17), the cell binding fragment of fibronectin (18), and collagen fragments (19). Fibroblasts require a substrate of collagen of types I-IV for attachment and migration in the Boyden chamber assays for chemotaxis (14).Here, we confirm earlier work on smooth muscle cells that indicates that smooth muscle cells use fibronectin to attach to types I and III collagens (20). We have extended these studies to show that smooth muscle cells attach preferentially to type V collagen without a requirement for fibronectin. When attached to collagen, the cells migrate toward PDGF in the Boyden chamber assay for chemotaxis. The chemotactic activity of PDGF may be of importance in the early stages of atherosclerosis.MATERIALS AND METHODS Materials. Tissue culture media were purchased from GIBCO. Fetal calf serum and bovine serum albumin were obtained from Reheis Chemical (Kankakee, IL). Trypsin and elastase were fro...

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Collagen polymorphism in cell cultures derived from guinea pig aortic smooth muscle: Comparison with three populations of fibroblasts

Cited by 43 publications

References 33 publications

Characterization of the collagen chains synthesized by cultured smooth muscle cells derived from rhesus monkey thoracic aorta

Characterization of the collagen chains synthesized by cultured smooth muscle cells derived from rhesus monkey thoracic aorta

The Differentiated State of Normal and Malignant Cells or How to Define a “Normal” Cell in Culture

Attachment of smooth muscle cells to collagen and their migration toward platelet-derived growth factor.

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