Studies on the assembly of the rat lens capsule. Biosynthesis and partial characterization of the collagenous components

Heathcote, G; Sear, Christopher H. J.; Grant, Michael E.

doi:10.1042/bj1760283

Cited by 79 publications

(34 citation statements)

References 47 publications

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“…Furthermore, the absence of 3-hydroxyproline from glycoprotein MFP I (Fig. 6) also argues against its being related to type-IV collagen (Heathcote et al, 1978) or to the 3-hydroxyproline-rich type-I procollagen associated with newly anchored fibroblasts (Lembach et al, 1977;Schwartz et al, 1979). Type-V collagen also appears to be more highly hydroxylated than is glycoprotein MFP I (for review see Bornstein & Sage, 1980) and, although we have detected this collagen in foetal bovine nuchal ligaments, other studies in our laboratory indicate that antiserum to bovine type-V collagen does not recognize glycoprotein MFP I (K. R. Knight & M. E. Grant, unpublished work).…”

Section: Discussionmentioning

confidence: 99%

“…3, and Grant & Jackson, 1976) appeared to support this hypothesis. Supplementation of ligament-cellculture medium with ascorbate produced an lysine-residue hydroxylation (Grant et al, 1972;Heathcote et al, 1978, as well as its insolubility in (NH4)2SO4 at 30% saturation (Crouch & Bornstein, 1979;Alitalo et al, 1980;Alitalo, 1980). Furthermore, the absence of 3-hydroxyproline from glycoprotein MFP I (Fig.…”

Section: Discussionmentioning

confidence: 99%

“…The ultrafiltration membranes (type PM30) were purchased from Amicon, High Wycombe, Bucks., U.K. All other reagents and materials were obtained from sources previously described (Sear et al, 1977a;Heathcote et al, 1978).…”

Section: Experimental Materialsmentioning

confidence: 99%

See 2 more Smart Citations

The nature of the microfibrillar glycoproteins of elastic fibres. A biosynthetic study

Sear¹,

Grant²,

Jackson³

1981

Biochemical Journal

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

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The nature of the microfibrillar glycoproteins of elastic fibres. A biosynthetic study

Sear¹,

Grant²,

Jackson³

1981

Biochemical Journal

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“…A tunicamycin-sensitive, asparagine-linked glycosylation step may also occur prior to secretion (13). Although collagen IV is structurally analogous to procollagens of other types, there is apparently no proteolytic processing of procollagen IV chains, at least in most tissues (13)(14)(15)(16). Thus, we denote it as collagen IV.…”

mentioning

confidence: 99%

Isolation of cDNA clones specific for collagen IV and laminin from mouse teratocarcinoma cells.

Wang¹,

Gudas²

1983

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

142

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The synthesis of the proteins laminin and collagen IV is stimulated =20-fold in F9 mouse teratocarcinoma stem cells after treatment of the cells with retinoic acid and N6, O2 dibutyryl-cAMP (Bt2cAMP). A cDNA library from F9 cells treated with retinoic acid, Bt2cAMP, and theophylline (F9-R+DBC cells) was constructed to isolate cDNA coding for collagen IV or laminin. The recombinant plasmids were screened by differential colony hybridization to cDNA synthesized from poly(A)+ RNA isolated from F9 stem and F9-R+DBC cells. Differentially hybridizing plasmids were then used as probes to hybridize to RNA transfer blots to determine the size of their specific mRNA. Only plasmids containing cDNA sequences specific for high molecular weight mRNA were further analyzed. Studies by hybridization-selection, in vitro translation, and immunoprecipitation showed that a plasmid clone, pcI5, contains cDNA homologous to collagen IV (a2) mRNA, and another plasmid clone, pcI56, contains cDNA homologous to laminin B mRNA. By RNA blot analyses, the size of mRNAcodingfor collagen IV (a2) is 7.6 kilobases; the size of mRNA for laminin is 6.8 kilobases. Using the technique of RNA blot hybridization, we studied the time course of the increase in mRNA coding for collagen IV (&2) and laminin B in F9 cells after retinoic acid and Bt2cAMP treatment. Both collagen IV (a2) and laminin B mRNAs are present in F9 stem cells. Collagen IV (a2) mRNA and laminin B mRNA levels increase slightly at approximately 12 hr after retinoic acid and Bt2cAMP addition, with a dramatic increase between 12 and 24 hr after drug treatment.

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“…Although the predominance of the 140,000 Mr component in preparations of human and bovine basement:membranes suggests that the major type IV collagen in tissues is at least the size of types I and III p-collagens, it is not known whether a completely intact procollagen represents the predominant form of type IV collagen in basement membranes. Proteolytic conversion of type IV procollagens to p-collagens or a chains has generally not been observed in vitro or in organ cultures (13,(21)(22)(23); nevertheless, limited processing of the procollagen to p-collagen could occur in vivo.…”

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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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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Studies on the assembly of the rat lens capsule. Biosynthesis and partial characterization of the collagenous components

Cited by 79 publications

References 47 publications

The nature of the microfibrillar glycoproteins of elastic fibres. A biosynthetic study

The nature of the microfibrillar glycoproteins of elastic fibres. A biosynthetic study

Isolation of cDNA clones specific for collagen IV and laminin from mouse teratocarcinoma cells.

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

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