Partial characterization of a second basement membrane collagen in human placenta

Bailey, Allen J.; Sims, Trevor J.; Duance, Victor Colin; Light, Nicholas

doi:10.1016/0014-5793(79)80992-8

Cited by 72 publications

(35 citation statements)

References 14 publications

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“…Equal aliquots of the digests were loaded into each well. Lane 1, control; lane 2, incubated with pepsin, 24 hr at 15°C; lane 3, control; lane 4, pepsin digest, 6 hr at 4°C; lane 5, pepsin digest, 24 hr at 4°C; lane 6, pepsin digest, 6 hr at 15°C; lanes 7 and 9, digest of acetic acid-insoluble procollagen, 24 hr at 4°C; lanes 8 and 10, digest of medium procollagen, 24 hr at 15°C. Mr are shown (X10-3).…”

Section: Resultsmentioning

confidence: 99%

“…that are both larger and smaller than a chains from interstitial collagens (types I-III) (3)(4)(5)(6). Comparable heterogeneity has been described for type IV collagen isolated from human placenta, and evidence has recently been obtained which suggests that the collagen fragments could be derived from two, genetically distinct, type IV collagen chains (7)(8)(9)(10).…”

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Structural basis for apparent heterogeneity of collagens in human basement membranes: type IV procollagen contains two distinct chains.

Crouch¹,

Sage²,

Börnstein³

1980

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

104

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Fetal cells isolated from human amniotic fluid synthesize type IV procollagen when grown in monolayer culture. The procollagen, which contains two biochemically distinct chains, was found to be structurally and immunologically related to type IV collagen chains and collagenous fragments isolated from human placenta. Limited pepsin digestion of the intact procollagen that was deposited in the cell layer during culture produced a heterogeneous population of collagenous peptides comparable to that obtained during isolation of type IV collagens from human tissues. These studies support the hypothesis that basement membranes contain at least two genetically distinct type IV procollagen chains and suggest that the heterogeneity of collagenous components obtained after pepsin digestion of tissues and isolated basement membranes can result from degradative cleavage of the procollagen at a limited number of protease-sensitive sites.Collagen a chains have been isolated from pepsin digests of basement membranes obtained from several tissues, including renal glomerulus and lens capsule, and on the basis of these studies it has been proposed that basement membranes contain a distinct collagen or procollagen composed of three identical chains (1, 2). However, other investigators using renal glomerular basement membranes have described a more h-eterogeneous mixture of collagenous peptides. that are both larger and smaller than a chains from interstitial collagens (types I-III) (3-6). Comparable heterogeneity has been described for type IV collagen isolated from human placenta, and evidence has recently been obtained which suggests that the collagen fragments could be derived from two, genetically distinct, type IV collagen chains (7-10).Epithelioid amniotic fluid cells synthesize a variety of connective tissue macromolecules in culture, including fibronectin (I1), type I and type I trimer procollagens (12), and a type IV procollagen (13). The last protein, which has been purified from culture medium by salt fractionation and ion-exchange chromatography, resembles collagenous proteins extracted from basement membranes in amino acid composition and degree of posttranslational hydroxylation and glycosylation. Although the unreduced procollagen migrated on NaDodSO4/polyacrylamide gel electrophoresis as a single band above type I procollagen, after reduction two closely spaced chains were observed that migrated between collagen 3 components and proal(I) chains. In this paper we present evidence that procollagen from amniotic fluid cells is immunologically and structurally related to type IV collagen fragments isolated from human placenta, and that the heterogeneity of collagenous components obtained after pepsin digestion of tissues is secondary to degradative cleavage of two genetically distinct type IV Isolation of Procollagen and Collagen. Medium procollagen was isolated by salt precipitation and ion-exchange chromatography on DEAE-and carboxymethyl-cellulose (12, 13). To isolate collagenous proteins from the matrix, ...

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Section: Resultsmentioning

confidence: 99%

mentioning

confidence: 99%

Structural basis for apparent heterogeneity of collagens in human basement membranes: type IV procollagen contains two distinct chains.

Crouch¹,

Sage²,

Börnstein³

1980

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

104

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“…Type V (B2A) collagen [4], type IV [7] and the 7s collagen identified [8], and similarly failed to reveal an identity with these collagens. Although not isolated in these studies, the collagen identified [ 141 from placental membranes capable of reduction to 40 000 M, components is unlike type M in that it exists as a high molecular weight aggregate.…”

Section: Discussionmentioning

confidence: 98%

“…The total tissue was treated as in [7,11) and the pepsin digestion carried out at 16°C for 6 h. The solubilised collagens were then subjected to the thermal gelation technique [ 121 to remove the interstitial type I and type III collagens. After di~ysing against 0.5 N acetic acid, the remaining collagen was submitted to salt fractionation [lo].…”

Section: Fig Platen Ta Collagen Preparationmentioning

confidence: 99%

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Identification of a new disulphide bonded collagen from cartilage

Shimokomaki¹,

Duance²,

Bailey³

1980

FEBS Letters

Self Cite

128

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The distribution of collagen types I, III and V (AB) in normal and atherosclerotic human aorta

McCullagh

Duance

Bishop

1980

The Journal of Pathology

141

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Collagen of types I, III and V has been identified and localised in adult human aorta, coronary arteries and atherosclerotic plaques using an indirect immunofluorescent method with specific antibodies to human collagen antigens. The distribution of the three types of collagen was distinct. Type I collagen was found around smooth muscle cells in the aortic media and in large amounts in the atherosclerotic plaque. Type III collagen was found in dense deposits alongside the elastic laminae in the aortic media and in diffuse intimal thickening. In the aortic media, there appeared to be more type III collagen than type I. The reverse was true in advanced atherosclerotic plaques. Type V collagen was distributed throughout the extracellular matrix in the aortic media and in the subendothelial region of plaques. These findings confirm earlier biochemical studies and suggest that a major shift in the nature of collagen synthesis occurs within advanced atherosclerotic plaques.

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Partial characterization of a second basement membrane collagen in human placenta

Cited by 72 publications

References 14 publications

Structural basis for apparent heterogeneity of collagens in human basement membranes: type IV procollagen contains two distinct chains.

Structural basis for apparent heterogeneity of collagens in human basement membranes: type IV procollagen contains two distinct chains.

Identification of a new disulphide bonded collagen from cartilage

The distribution of collagen types I, III and V (AB) in normal and atherosclerotic human aorta

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