Collagen and related research最新文献

{"title":"Polar-Apolar Characteristics and Fibrillogenesis of Glycosylated Collagen","authors":"S. Amudeswari ,&nbsp;J.N. Liang ,&nbsp;B. Chakrabarti","doi":"10.1016/S0174-173X(87)80011-0","DOIUrl":"10.1016/S0174-173X(87)80011-0","url":null,"abstract":"<div><p>To find the effect of carbohydrate on collagen fibrillogenesis, type I skin collagen was glycosylated by glycosyltransferase, and type II cartilage collagen was deglycosylated by glycosidase. The secondary structures remained unchanged, but the tertiary structures were altered, as shown by increased TNS fluorescence of the bound probe in the glycosylated form. Since TNS binds preferentially to the hydrophobic region of a protein molecule, glycosylation caused an apparent increase in the available hydrophobic sites for the dye. Glycosylation also resulted in a longer lag time and a slower growth rate of fibrillogenesis, although the amount of fibrils formed was unchanged. Deglycosylation resulted in a shorter lag time and an increased rate of fibrillogenesis. Neither glycosylation nor deglycosylation changed the stability of the molecule, as was evident from the melting temperature.</p></div>","PeriodicalId":77694,"journal":{"name":"Collagen and related research","volume":"7 3","pages":"Pages 215-223"},"PeriodicalIF":0.0,"publicationDate":"1987-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0174-173X(87)80011-0","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14773073","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"XIth Meeting of the Federation of European Connective Tissue Societies, Amsterdam, The Netherlands","authors":"","doi":"10.1016/S0174-173X(87)80014-6","DOIUrl":"https://doi.org/10.1016/S0174-173X(87)80014-6","url":null,"abstract":"","PeriodicalId":77694,"journal":{"name":"Collagen and related research","volume":"7 3","pages":"Page 233"},"PeriodicalIF":0.0,"publicationDate":"1987-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0174-173X(87)80014-6","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"137405173","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Production of Monoclonal Antibodies Recognising N-Ethylmaleimide During Attempted Generation of Monoclonal Antibodies to Human Type I Procollagen","authors":"Keith M. Dawson ,&nbsp;Christopher H.J. Sear ,&nbsp;Carroll M. Moorhouse","doi":"10.1016/S0174-173X(87)80004-3","DOIUrl":"10.1016/S0174-173X(87)80004-3","url":null,"abstract":"<div><p>Mice were immunised for the production of monoclonal antibodies to human procollagen (I) using antigen purified from fibroblast conditioned medium. The procedure for procollagen (I) preparation included the addition of proteinase inhibitors <em>N</em>-ethylmaleimide, phenylmethylsulphonyl fluoride and ethylenediaminetetraacetic acid to prevent damage by proteolytic cleavage. Four of the five monoclonal antibodies subsequently produced were found to recognise the thiol proteinase inhibitor <em>N</em>-ethylmaleimide but not type I procollagen prepared in the absence of <em>N</em>-ethylmaleimide. One of these monoclonal antibodies was examined further and shown to recognise β-galactosidase after it had been reacted with <em>N</em>-ethylmaleimide. As far as we are aware this is the first time that monoclonal antibodies have been produced which recognise <em>N</em>-ethylmaleimide. Our findings indicate an unexpected reaction between procollagen and N<em>N</em>-ethylmaleimide and prompt the suggestion that the use of <em>N</em>-ethylmaleimide in the purification of procollagen and other proteins should be reexamined.</p></div>","PeriodicalId":77694,"journal":{"name":"Collagen and related research","volume":"7 2","pages":"Pages 125-134"},"PeriodicalIF":0.0,"publicationDate":"1987-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0174-173X(87)80004-3","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14244094","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Collagen Synthesis and Degradation In Vivo. Evidence for Rapid Rates of Collagen Turnover with Extensive Degradation of Newly Synthesized Collagen in Tissues of the Adult Rat","authors":"Robin J. McAnulty ,&nbsp;Geoffrey J. Laurent","doi":"10.1016/S0174-173X(87)80001-8","DOIUrl":"10.1016/S0174-173X(87)80001-8","url":null,"abstract":"<div><p>Collagen turnover is now known to occur more rapidly in body tissues than traditionally believed, but the kinetics and mechanisms for degradation are still poorly understood. Here we measure collagen synthesis rates and the proportion of newly synthesized collagen (probably procollagen) which is rapidly degraded, in tissues of the adult rat after injection of [¹⁴C] -proline with a large “flooding” dose of unlabelled proline. Incorporation of [¹⁴C]-proline into lung, heart, skeletal muscle and skin collagen and its appearance as hydroxy [¹⁴C]-proline, free or in small molecular weight moieties, at various times up to one hour, suggested extremely rapid synthesis and degradation for some tissues of the adult rat. Values in heart, lung, skeletal muscle and skin (with the proportion of degradation of newly synthesized collagen shown in parentheses) were 5.2±0.7%/day (53±5%),9.0±0.7%/day (37±2%),2.2±0.3%/day (38±7%) and 4.4±1.3 %/day (8.8±0.5 %). These data provide in vivo evidence, which are consistent with the observation in isolated cells, that a proportion of newly synthesized collagen is degraded rapidly, and probably intracellularly, after its synthesis. They also indicate that collagen may be synthesized and degraded rapidly in normal rat tissues, but the mean turnover rates and the proportions of collagen degraded intracellularly vary widely between tissues.</p></div>","PeriodicalId":77694,"journal":{"name":"Collagen and related research","volume":"7 2","pages":"Pages 93-104"},"PeriodicalIF":0.0,"publicationDate":"1987-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0174-173X(87)80001-8","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14620284","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Influence of Fibronectin on the Fibrillogenesis of Type I and Type III Collagen","authors":"Maria Luisa Speranza ,&nbsp;Giovanna Valentini ,&nbsp;Alberto Calligaro","doi":"10.1016/S0174-173X(87)80003-1","DOIUrl":"10.1016/S0174-173X(87)80003-1","url":null,"abstract":"<div><p>The <em>in vitro</em> self-assembly of type I and type III calf skin collagen in the presence of fibronectin was studied turbidimetrically. Fibronectin delayed the fibrillogenesis of type III collagen but accelerated that of type I collagen. The effect of fibronectin was concentration-dependent.</p><p>The lag phase was more altered than the growth phase in the presence of fibronectin while the final turbidity and the amount of fibrils formed were unmodified.</p><p>Fibrils obtained in the presence of fibronectin all showed native banding pattern. Fibronectin bound partly to collagen fibrils; the amount of bound fibronectin was similar for the two types of collagen and tended to be constant at increasing fibronectin concentrations. It is suggested that the antithetic effect of fibronectin on type I and type III collagen fibrillogenesis may arise both from the different affinity of fibronectin to the two types of collagen and the different aggregation properties of each collagen type.</p></div>","PeriodicalId":77694,"journal":{"name":"Collagen and related research","volume":"7 2","pages":"Pages 115-123"},"PeriodicalIF":0.0,"publicationDate":"1987-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0174-173X(87)80003-1","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14742706","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"The Effect of Proteoglycans on the Morphology of Collagen Fibrils Formed In Vitro","authors":"Kathryn G. Vogel ,&nbsp;John A. Trotter","doi":"10.1016/S0174-173X(87)80002-X","DOIUrl":"10.1016/S0174-173X(87)80002-X","url":null,"abstract":"<div><p>The morphology of collagen fibrils at various times during formation <em>in vitro</em> was quantitatively examined by negative staining and by scanning electron microscopy. The presence of a small dermatan sulfate proteoglycan from bovine tendon (5 μg proteoglycan/100 μg collagen) resulted in collagen fibrils that were significantly thinner in width at all times by both methodologies. The rate of fibril diameter increase was also retarded by the small proteoglycans, suggesting that they inhibited the lateral aggregation of forming collagen fibrils. Large proteoglycans from cartilage did not produce this effect.</p></div>","PeriodicalId":77694,"journal":{"name":"Collagen and related research","volume":"7 2","pages":"Pages 105-114"},"PeriodicalIF":0.0,"publicationDate":"1987-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0174-173X(87)80002-X","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14742846","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Effects of 1-Hydroxyethylidene-1, 1-Bisphosphonate (HEBP) on the Synthesis of Dentin Matrix Proteins in the Mouse","authors":"T. van den Bos ,&nbsp;W. Beertsen","doi":"10.1016/S0174-173X(87)80005-5","DOIUrl":"10.1016/S0174-173X(87)80005-5","url":null,"abstract":"<div><p>The drug 1-hydroxyethylidene-1,1-bisphosphonate (HEBP) is known to inhibit the mineralization of bone and dentin. Its mechanism of action, however, has not yet been elucidated. In order to study its effects on dentinogenesis, mice were supplied with either physiological saline or HEBP in a dose of 10 mg P/kg body weight. This dose is known to interfere with the deposition of mineral crystallites in dentin matrix. The animals were then given a combined injection of [³H]-serine and [¹⁴C] -proline (or [¹⁴C]-glycine) and killed 8–9 days thereafter. The dentin proteins were isolated and fractionated in soluble proteins among which phosphoproteins, CNBr-peptides of collagen and collagen-associated phosphoproteins. It was found that HEBP had a strong inhibitory effect on the synthesis of phosphoproteins and to a lesser extent on that of collagen. The inhibition of the formation of these proteins is supposed to be related to the impaired calcification of dentin under the influence of the bisphosphonate.</p></div>","PeriodicalId":77694,"journal":{"name":"Collagen and related research","volume":"7 2","pages":"Pages 135-147"},"PeriodicalIF":0.0,"publicationDate":"1987-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0174-173X(87)80005-5","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14246121","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Chromosomal Localization of Human Collagen Genes","authors":"Jeanne C. Myers ,&nbsp;Beverly S. Emanuel","doi":"10.1016/S0174-173X(87)80006-7","DOIUrl":"10.1016/S0174-173X(87)80006-7","url":null,"abstract":"","PeriodicalId":77694,"journal":{"name":"Collagen and related research","volume":"7 2","pages":"Pages 149-159"},"PeriodicalIF":0.0,"publicationDate":"1987-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0174-173X(87)80006-7","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14433808","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Biosynthetic Precursors of Cartilage Chondroitin Sulfate Proteoglycan","authors":"Barbara M. Vertel ,&nbsp;Youssef Hitti","doi":"10.1016/S0174-173X(87)80021-3","DOIUrl":"10.1016/S0174-173X(87)80021-3","url":null,"abstract":"<div><p>Early steps in the biosynthesis of chondroitin sulfate proteoglycan (CSPG) and collagenous cartilage matrix molecules were examined by the comparison of products translated in mRNA-directed cell-free reactions and those synthesized by intact cartilage cells. RNA isolated from embryonic chicken sterna was used to direct cell-free translation reactions. Chicken sternal chondrocytes in culture were pulse-labeled with [³⁵S]-methionine. The CSPG core protein was identified by immunoprecipitation. The M_r of the cartilage cell-synthesized core protein was determined to be 370K, approximately 10–15K greater than that of the comparable cell-free translation product. Experimental results strongly support the view that the observed difference in M_r reflects the cotranslational addition of mannose-rich, <em>N</em>-asparagine-linked oligosaccharides to the cell-synthesized core protein: 1) the cell-synthesized product was labeled with [³H]-mannose and precipitated by concanavalin A-sepharose beads; 2) the incorporated [³H]-mannose could be subsequently removed by digestion with endoglycosidase H (Endo H); 3) the M_r of the cell-synthesized core protein was reduced by Endo H digestion to that of the comparable cell-free translation product; 4) the core protein synthesized by tunicamycin-treated chondrocytes (inhibited in their ability to add <em>N</em>-asparagine-linked mannose-rich oligosaccharides to proteins) was comparable in electrophoretic mobility to that of the core protein cell-free translation product; and 5) the core protein translated in microsome-coupled cell-free reactions had an M_r 8–10K greater than that of the core protein translated in the absence of microsomes. For the purpose of examining biosynthetic intermediates, chondrocytes were labeled continuously or pulse-chase labeled for varying times. No biosynthetic CSPG intermediates migrating between the core protein and the CSPG monomer were detected. However, a band of 355Kdal appeared to share certain characteristics with the 370Kdal core protein (including its immunoprecipitability with CSPG antibodies), and a 340Kdal band was noted.</p><p>Type II procollagen and other collagenase-sensitive products of 205Kda1 and 110Kdal were observed among translation and chondrocyte-synthesized products. In chondrocytes, all three products exhibited labeling or chase time-dependent increases in M_r which were accelerated by ascorbate supplements and inhibited by the addition of α,α′-dipyridyl. These results suggest that the observed time-dependent increases in M_r are a consequence of collagen hydroxylation. The 110Kdal and 205Kdal collagenous proteins may be related to the minor collagens recently described in cartilage.</p></div>","PeriodicalId":77694,"journal":{"name":"Collagen and related research","volume":"7 1","pages":"Pages 57-75"},"PeriodicalIF":0.0,"publicationDate":"1987-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0174-173X(87)80021-3","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14427146","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"The Role of Microtubules in the Phagocytosis of Collagen by Fibroblasts","authors":"Vincent Everts ,&nbsp;Wouter Beertsen","doi":"10.1016/S0174-173X(87)80017-1","DOIUrl":"10.1016/S0174-173X(87)80017-1","url":null,"abstract":"<div><p>The effects of the anti- microtubular agents, colchicine and vinblastine, on the phagocytosis of collagen by fibroblasts were assessed quantitatively in cultured mouse bone explants. It was found that in the absence of the microtubular system the volume density of lysosomal vaocules containing cross-banded collagen fibrils in periosteal cells did not differ from that seen in controls. In contrast, cytochalasin B which interferes with the microfilament system prevented the accumulation of collagen-containing vacuoles in the cytoplasm.</p><p>The data indicate that the phagocytosis of collagen fibrils by fibroblasts does not depend on the integrity of the microtubular apparatus, but seems to require an intact microfilament system.</p></div>","PeriodicalId":77694,"journal":{"name":"Collagen and related research","volume":"7 1","pages":"Pages 1-15"},"PeriodicalIF":0.0,"publicationDate":"1987-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0174-173X(87)80017-1","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14729583","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}