Physicochemical characterization and molecular organization of the collagen A and B chains

Rhodes, R K; Miller, Edward J.

doi:10.1021/bi00610a003

Cited by 332 publications

(138 citation statements)

References 13 publications

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“…In contrast, A and B collagens isolated from placental membranes and thought to be basal lamina in origin had a low 3-hydroxyproline content (35,36).…”

Section: Discussionmentioning

confidence: 95%

Human glomerular visceral epithelial cells synthesize a basal lamina collagen in vitro.

Killen¹,

Striker²

1979

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

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Isolated human glomeruli were digested with purified bacterial collagenase yielding epithelial cells. These cells grew to saturation density and did not become multilayered. They were identified as visceral glomerular epithelial cells by their morphologic appearance by phase and electron microscopy and by the presence of surface receptors for C3b. Neither Factor VIII antigen nor Fc receptors were observed. The glomerular epithelial cells synthesized a collagenous protein that was antigenically similar to human glomerular basal lamina. Proteins precipitated from visceral epithelial cell medium with affinity purified antibody against noncollagenous glomerular basal lamina antigens yielded a single collagenase labile protein that by sodium dodecyl sulfate/polyacylamide gel electrophoresis migrated with an apparent Mr of 168,000 in the presence of reducing agents. Analysis of hydro roline isomers yielded a ratio of 3-hydroxyproline to total hydroproline of 0.17. Pepsin digestion yielded a disulfide-bonded multimer which, with reduction, migrated with an apparent Mr of 148,000. These data demonstrate that human gloiherular visceral epithelial cells can be isolated and propagated in vitro and that they synthesize a collagen similar to that found in vivo.The glomerular b.asal lamina (GBL) is a part of the filtration barrier and functions to maintain the shape and elasticity of the glomerulus in the face of a high intraluminal pressure (1). Glomerular diseases leading to significant morbidity and mortality are associated with changes in the width, charge, and staining properties of the human GBL. The biochemical correlates of-these changes, including the nature of the GBL biosynthetic subunits, their site(s) and synthesis, mechanism of degradation, and the factors regulating these processes, have not been eludicated.

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“…In contrast, A and B collagens isolated from placental membranes and thought to be basal lamina in origin had a low 3-hydroxyproline content (35,36).…”

Section: Discussionmentioning

confidence: 95%

Human glomerular visceral epithelial cells synthesize a basal lamina collagen in vitro.

Killen¹,

Striker²

1979

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

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“…Precipitated collagen was recovered by centrifugation, dialysed against 0.1 M acetic acid and freezedried. [N&l] in the supernatant was increased serially to 1,2 M and 2.0 M, the precipitates being recovered at each step [1,2,7]. Similar fractions were prepared from cortical bone (ground in liquid NZ and decalcified by 0.5 M EDTA), articular cartilage and fetal calf dermis.…”

Section: Extraction Of Collagenmentioning

confidence: 99%

“…With hyaline cartilage under these conditions, 96% of the type II collagen precipitates at 0.7 M NaCl [2,7]. The identity of the al(V) chain was confirmed by its CNBr-peptide profile ( fig.2) and its amino acid composition (table 1) determined on the electrophoretic band excised from the gel.…”

mentioning

confidence: 99%

Collagen of fibrocartilage: a distinctive molecular phenotype in bovine meniscus

Eyre

1983

FEBS Letters

161

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Fibrocartilage of bovine knee meniscus was analyzed for major and minor collagen constituents. The main fraction (-98%) of pepsin-solubilized collagen consisted of type I with a small proportion (< 10%) of type III molecules. The minor fraction (l-2%) isolated by salt pr~ipitation could be further resolved into type V collagen that consisted of al(V) and cu2(V) chains and a type II-like molecule with chains that had all the characteristics of the 3cr variant of tul(I1) found in hyaline cartilage. The articular surface zone of the meniscus appeared 2-3-fold enriched in these minor collagens compared with deeper tissue, though qualitatively the same distinctive collagen phenotype was evident throughout. Bovine Cartilage Collagen

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“…On the other hand, it was concluded [3] that basement membranes were composed of many different collagenous peptides. More recently analysis of pepsin digests of placental membrane revealed, in addition to types I and III colIagens, a new basement membrane-like collagen [4- [9] in a 2: 1 ratio. Antibodies raised against this collagen confirmed its identity as a basement membrane-associated collagen by immunofluorescent localization, the attached trophoblasts being clearly visible along the intensely stained membrane of the placental villi [ lo] .…”

Section: Introductionmentioning

confidence: 99%

Partial characterization of a second basement membrane collagen in human placenta

et al. 1979

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Physicochemical characterization and molecular organization of the collagen A and B chains

Cited by 332 publications

References 13 publications

Human glomerular visceral epithelial cells synthesize a basal lamina collagen in vitro.

Human glomerular visceral epithelial cells synthesize a basal lamina collagen in vitro.

Collagen of fibrocartilage: a distinctive molecular phenotype in bovine meniscus

Partial characterization of a second basement membrane collagen in human placenta

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