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 50,377 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Collagen-like proteins have been found in the egg shell membranes of the hen. Materials similar to types I and V collagens were detected in each of the two layers of this membrane, the thick outer membrane and the thin inner membrane. Collagen was extracted by acid-pepsin digestion and isolated by differential salt precipitation. Identification of type-specific collagen-like material was established by coelectrophoresis on SDS-polyacrylamide gels using known collagen standards. These bands were susceptible to digestion by bacterial collagenase. From differential staining of the gels it was estimated that the ratio of collagen types I:V was approximately 100:1. Further confirmation of these biochemical results was obtained with immunofluorescence microscopy using type-specific antisera against chicken types I and V collagen with the indirect sandwich technique. Both the inner and outer shell membranes contained the two types of collagen. Within each membrane, the large, coarse 2.5-micron fibers contained predominantly type I collagen-like material, while type V collagen was mainly associated with the delicate narrower fibers of approximately 0.6-micron diameter. These tended to be concentrated in the inner membrane. At the electron microscopic level, both types of fibers were coated with glycoproteins that stained positively with ruthenium red. The deposition of these collagen-like substances by the hen oviduct on to the surface of the developing egg is an additional example of interstitial-type collagen synthesis and secretion by epithelial rather than by mesenchymal cells.
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PMID:Collagen in the egg shell membranes of the hen. 620 93

Synthesis of collagen types I, II, III, and IV in cells from the embryonic chick cornea was studied using specific antibodies and immunofluorescence. Synthesis of radioactively labeled collagen types I and III was followed by fluorographic detection of cyanogen bromide peptides on polyacrylamide slab gels and by carboxymethylcellulose chromatography followed by disc gel electrophoresis. Type III collagen had been detected previously by indirect immunofluorescence in the corneal epithelial cells at Hamburger-Hamilton stages 20--30 but not in the stroma at any age. Intact corneas from embryos older than stage 30 contain and synthesize type I collagen but no detectable type III collagen. However, whole stromata subjected to collagenase treatment and scraping (to remove epithelium and endothelium) and stromal fibroblasts from such corneas inoculated in vitro begin synthesis of type III collagen within a few hours while continuing to synthesize type I collagen. As demonstrated by double-antibody staining, most corneal fibroblasts contain collagen types I and III simultaneously. Collagen type III was identified biochemically in cell layers and media after chromatography on carboxymethylcellulose be detection of disulfide-linked alpha l (III)3 by SDS gel electrophoresis. The conditions under which the corneal fibroblasts gain the ability to synthesize type III collagen are the same as those under which they lose the ability to synthesize the specific proteoglycan of the cornea: the presence of corneal-type keratan sulfate.
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PMID:Synthesis of type III collagen by fibroblasts from the embryonic chick cornea. 624 16

The granule fraction of human polymorphonuclear leucocytes (PMNs), the concentrated product of gingival washing from 2 human volunteers and the culture fluid of samples of human gingiva were incubated with neutral salt soluble collagen from rat skin and the patterns of collagen degradation were studied by SDS polyacrylamide gel electrophoresis. Collagenase from human gingiva cleaved the collagen molecules in a fashion similar to that of the PMN granule fraction. Collagen was also attacked by elastase from human PMNs and, to a lesser extent, by elastase from the gingival washings.
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PMID:Collagen breakdown by gingival collagenase and elastase. 624 88

Collagen synthesis and the ratios of collagen types I and III were assayed from the skin lesions of five subjects with tuberous sclerosis. Collagen synthesis, measured by the activities of prolyl hydroxylase and galactosylhydroxylysyl glucosyltransferase, was clearly increased in three angiofibromas of these patients and in one soft tumour of the face, but it was unchanged in shagreen patches. The total collagen content was decreased in angiofibromas, indicating either increased turnover of collagen or an increased amount of cellular or other macromolecular elements in these lesions. The proportions of types I and III collagens, estimated by cyanogenbromide digestion and SDS-gel electrophoresis, were 80-90% and 10-20%, respectively, in all samples except two angiofibromas, in which the relative amount of type III collagen was increased. This may indicate that angiofibromas of tuberous sclerosis are heterogenous with respect to the collagen types they contain, and that there may be disturbed cell growth or collagen synthesis, with individual variation from case to case.
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PMID:Types I and III collagens and the activities of prolyl hydroxylase and galactosylhydroxylysyl glucosyltransferase in skin lesions of tuberous sclerosis. 629 27

Pepsin-soluble collagen was extracted from three histologically proven cases of chordoma and nucleus pulposus. The collagen types of these materials were investigated by differential salting-out, SDS-PAGE (sodium dodecyl sulphate-polyacrylamide gel electrophoresis) of native collagen and their CNBr (cyanogen bromide) cleaved peptides, and their amino acid compositions. Although the collagen of nucleus pulposus was type II, that of chordoma was largely type I. Collagen of notochord, the origin of nucleus pulposus, is known to be type II. Further investigation is necessary in view of the fact that collagen of chordoma, a tumor believed to be derived from notochord, is not type II.
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PMID:Type of collagen in chordoma. 643 58

Protein synthesis by human chondrosarcoma tissue and normal articular cartilage was studied in organ and primary monolayer cell culture systems. Protein synthesis by cell cultures was evaluated at 2.7 and 21 days after plating. When compared to normal, incorporation of 3H-proline and 35S-methionine into proteins was elevated in chondrosarcoma samples under both culture conditions. Hydroxyproline analyses of tissue hydrolysates indicated that chondrosarcoma samples contained significantly less collagen than normal articular cartilage, yet were incorporating significantly greater amounts of 3H-proline into 3H-hydroxyproline. Collagen production by cell cultures was assessed by digestion of samples with purified clostridial collagenase. Chondrosarcoma cells produced more collagenase-sensitive protein than normal cells at all intervals. SDS polyacrylamide gel analyses of all preparations showed two collagenase-sensitive proteins with apparent molecular weights of 165,000 and 175,000. Decreased synthesis of another major protein, apparent molecular weight 210-220,000 was noted in chondrosarcoma preparations in both culture systems.
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PMID:De novo protein synthesis by human chondrosarcoma in cell and organ culture: evidence of unusually high collagen production by a neoplastic tissue. 645 Jun 65

Collagen chains separated on 5% SDS-acrylamide gels were stained with a 0.1% Sirius F3BA solution in saturated aqueous picric acid. After destaining the gels with methanol: acetic acid: water (30: 7 : 63), they were scanned at 540 nm and the area under each peak was determined. After that, the bands were sliced and the slices incubated overnight with trypsin at 37 degrees C. The color of the slices was eluted completely when the denatured collagen was ingested with trypsin. The absorbance of the color eluted was determined at 540 nm. The results obtained demonstrated that both procedures are reproducible and linear from 10 to at least 120 micrograms of protein. The correlation coefficient between both procedures was greater than 95%. The color is stable and the same end-point is obtained after destaining. In order to test the usefulness of the procedure in the typing of collagens from parenchymatous tissues, liver biomatrix was prepared from normal and cirrhotic human specimens obtained at autopsy. Over 95% of the collagen originally present in each liver was recovered in the corresponding biomatrix . We also showed that over 80-85% of biomatrix collagen could be solubilized with pepsin. These extracts were neutralized to pH 7.0 to inactivate pepsin and were applied onto the acrylamide gels. After electrophoresis and staining with Sirius red the types of collagen were determined by densitometric analysis. Our findings confirmed the results obtained by others using more complex and time consuming methodologies, mainly that type I and type III collagens are present in the normal liver in equal concentrations and that the ratio of I/III is 1. In all the cirrhotic livers investigated, the ratio of type I/type III collagen was greater than 1 due to an increase in type I collagen.
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PMID:A simple quantitative method for collagen typing in tissue samples: its application to human liver with schistosomiasis. 672 51

It is known that cartilage collagen in higher vertebrates conforms to Type II collagen but very little is known of the nature of shark cartilage. This study was undertaken to determine the differences, if any, between shark cartilage collagen and that of higher vertebrates. Collagen was obtained from shark cartilage by pepsin solubilization and characterized by amino acid analysis and determination of chain composition by SDS-polyacrylamide gel electrophoresis and CM-cellulose chromatography. Results indicated the presence not only of Type II collagen but also of Type I collagen. Type I collagen accounted for about one third of the total collagen content of shark cartilage.
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PMID:Distribution of different molecular species of collagen in the vertebral cartilage of shark (Carcharius acutus). 672 6

Collagen types in normal human and keratoconus corneas were separated by salt fractionation and thermal gelation in the pepsin-soluble fraction of the lyophilized tissues. Peptic digestion indicated no significant differences between normal and keratoconus corneas. Further collagen characterization was performed using SDS-PAGE. Collagen concentration were determined via hydroxyproline. Soluble collagens from normal human cornea represent 85% collagen type I, maximally 10% collagen type III and 5% collagen type V. Soluble collagens of keratoconus corneas consist of 90% type I collagen and maximally 5% type II and type V collagen.
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PMID:Collagen types in keratoconus. 709 51

After extraction of bovine corneal stroma with 1M CaC1(2) and subsequent digestion of the insoluble residue with purified bacterial collagenase, two crude structural glycoprotein (SPG) fractions were obtained; one which precipitated upon dialysis against water of the collagenase solubilized material and the other which was extracted by 8M urea from the collagenase insoluble material. Amino acid analyses of these crude SGP fractions indicated that they were primarily non-collagenous but that very small amounts of collagen-derived amino acids were present. Upon gel filtration of these SGP fractions on Sepharose 4B-CL, void volume fractions were isolated from each of the crude fractions which were enriched, relative to the original crude fractions, in the collagen-derived amino acids. Carbohydrate analysis indicated that the void volume fractions had the properties of glycoproteins rather than proteoglycans. Upon disulfide reduction and SDS-PAGE, each of these fractions was resolved into five major protein bands with molecular weights of 155,000, 137,000, 117,000 82,000 and 34,000. Only the three largest bands contained the collagen derived amino acids. These data are consistent with the presence within bovine corneal stroma of a large structural glycoprotein complex comprised of at least five protein components associated through disulfide bonds. Collagen apparently is associated with three of these, either through covalent crosslinkage, or as part of the primary structure.
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PMID:Isolation and preliminary characterization of a structural glycoprotein complex from bovine corneal stroma. 718 8


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