Collagen and related research最新文献

{"title":"Immunochemical Studies on the Synthesis and Secretion of Link Protein and Aggregating Proteoglycan by Chondrocytes","authors":"A. Ratcliffe ,&nbsp;C. Hughes ,&nbsp;P.R. Fryer ,&nbsp;F. Saed-Nejad ,&nbsp;T. Hardingham","doi":"10.1016/S0174-173X(87)80039-0","DOIUrl":"10.1016/S0174-173X(87)80039-0","url":null,"abstract":"<div><p>Chondrocytes from pig laryngeal cartilage were maintained in culture, and the biosynthesis and secretion of link protein and proteoglycan were studied using immunochemical, biochemical and immunolocalisation techniques. In the presence of monensin there was a dose-dependent inhibiton of link protein secretion which was very similar to that of aggregating proteoglycan, and suggested that they followed the same intracellular pathway during biosynthesis. In the presence of cycloheximide there was a similar dose-dependent inhibition of the secretion of both link protein and proteoglycan. Kinetics of secretion following inhibition of synthesis by cycloheximide showed that both proteins had similar intracellular pool sizes. Analysis of protein core and glycosaminoglycan biosynthesis showed that the time for synthesis and glycosylation of proteoglycan was 22 minutes, and this was quickly followed (within 6 minutes) by secretion. Intracellular electron microscopic immunolocalisation using protein A-gold showed link protein to be present in the Golgi cisternae and vesicles, and doublelabelling experiments showed link protein only to be detected in vesicles that also labelled for proteoglycan protein core. When chondrocytes were maintained in monolayer culture for 10 days the rate of biosynthesis and secretion of proteoglycan increased although that of link protein remained constant. The control of their biosynthesis was thus shown to be independent. Within 4 hours of secretion a high proportion of link protein was incorporated into proteoglycan aggregates.</p></div>","PeriodicalId":77694,"journal":{"name":"Collagen and related research","volume":"7 6","pages":"Pages 409-421"},"PeriodicalIF":0.0,"publicationDate":"1987-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0174-173X(87)80039-0","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14571572","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":"Modulation of Fibroblast Growth and Glycosaminoglycan Synthesis by Interleukin-1","authors":"Rebecca E. Bronson,&nbsp;Charles N. Bertolami ,&nbsp;Elizabeth P. Siebert","doi":"10.1016/S0174-173X(87)80025-0","DOIUrl":"10.1016/S0174-173X(87)80025-0","url":null,"abstract":"<div><p>Cellular response to inflammatory mediators is central to the regulation of new scar tissue formation. Fibroblasts derived from normal dermis and from 14-day old skin wound granulation tissue were compared with regard to production of non-collagenous extracellular matrix and response to interleukin-1 (IL-1). Following a serum-free 48 hour labeling with [³H]-glucosamine, the cellular, pericellular and medium fractions from the two cell types were collected, precipitated with cetylpyridinium chloride (CPC), and analyzed by cellulose acetate electrophoresis. In addition, susceptibility of precipitates to the polysaccharidases <em>Streptomyces</em> hyaluronidase and chondroitinase ABC was determined. Labeled conditioned medium from both cell types contained dermatan sulfate (DS) and hyaluronate (HA), although the relative amounts of these glycosaminoglycans (GAGs) were different. Medium from normal dermal fibroblasts contained more DS than HA, while 14-day granulation tissue culture medium contained a proportionately larger amount of HA. The amount of HA in the medium fraction of normal dermal fibroblasts was increased approximately 10-fold in the presence of 5 U/ml IL-1, while HA in the medium of wound-derived fibroblasts was quantitatively unaffected by addition of the mediator. Pericellular GAG consisted of heparan sulfate (HS) and chondroitin sulfate (CS), with no observable differences between the two cell types and no effect of IL-1 on this profile for either cell type. Conditioned medium from both cell types contained IL-1 activity (measured by thymocyte proliferation assay), with medium from 14-day granulation tissue fibroblasts containing 10-fold higher activity than normal dermal fibroblast medium.</p></div>","PeriodicalId":77694,"journal":{"name":"Collagen and related research","volume":"7 5","pages":"Pages 323-332"},"PeriodicalIF":0.0,"publicationDate":"1987-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0174-173X(87)80025-0","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14624958","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":"Immunocytochemical Demonstration of Simultaneous Synthesis of Types I, III and V Collagen and Fibronectin in Mouse Embryonic Palatal Mesenchymal Cells In Vitro","authors":"K. Kurisu ,&nbsp;Y. Ohsaki,&nbsp;K. Nagata,&nbsp;T. Kukita,&nbsp;H. Yoshikawa,&nbsp;T. Inai","doi":"10.1016/S0174-173X(87)80026-2","DOIUrl":"10.1016/S0174-173X(87)80026-2","url":null,"abstract":"<div><p>An immunocytochemical study was made on the palatal mesenchymal cells obtained from mouse embryos during palatal development with special reference to synthesis of types of collagen and fibronectin <em>in vitro</em>. Most cells showed positive staining with antibodies against the four proteins examined. The staining for type I collagen was most intense among the four proteins and was distributed perinuclearly. The staining for type III collagen was quite similar as that for type I collagen but less intense, whereas that for type V collagen was weak and its staining pattern was different from those for types I and III collagen in that the surface of the plasma membrane, in addition to the perinuclear cytoplasm, showed weak staining for type V collagen. Antibodies to fibronectin showed perinuclear and extracellular fibrous staining. These data suggest that palatal mesenchymal cells synthesize types I, III, and V collagen and fibronectin simultaneously.</p></div>","PeriodicalId":77694,"journal":{"name":"Collagen and related research","volume":"7 5","pages":"Pages 333-340"},"PeriodicalIF":0.0,"publicationDate":"1987-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0174-173X(87)80026-2","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14447097","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":"Acceleration of Cartilage and Bone Differentiation on Collagenous Substrata","authors":"Gila Maori ,&nbsp;Klaus Von Der Mark ,&nbsp;Hari Reddi ,&nbsp;Dick Heinegard ,&nbsp;Ahnders Franzen ,&nbsp;Michael Silbermann","doi":"10.1016/S0174-173X(87)80028-6","DOIUrl":"10.1016/S0174-173X(87)80028-6","url":null,"abstract":"<div><p>Chondroprogenitor cells of newborn murine mandibular condyles were cultured on top of collagen sponges for up to 18 days. After 24 h in culture, new chondroblasts developed which subsequently matured showing signs of hypertrophy, while the extracellular matrix revealed positive reactivity for type II collagen, cartilage proteoglycans and mineralization. Light and electron microscopy examinations showed signs of new osteoid formation, a feature that was preceeded by positive immunohistochemical reaction for type I collagen, fibronectin and bone specific sialoprotein. A close temporal and spatial association was noted between the development of mature, mineralized cartilage and new osteoid. The differentiation of new cartilage and bone cells was linked to an increased activity of DNA synthesis and cellular proliferation. The <em>de novo</em> bone formation was accompanied by increasing rates of alkaline phosphatase activity and uptake of [⁴⁵Ca] features that were found to be tightly correlated to each other. The collagen substrata appeared also to facilitate the migration of cells, their replication and their subsequent differentiation to their respective cellular lineage. Hence, collagen sponges <em>in vitro</em> appear to serve as a promising substrata for culture systems involved with the growth and differentiation of mineralizing tissues such as cartilage and bone.</p></div>","PeriodicalId":77694,"journal":{"name":"Collagen and related research","volume":"7 5","pages":"Pages 351-370"},"PeriodicalIF":0.0,"publicationDate":"1987-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0174-173X(87)80028-6","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14447057","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":"Interaction of Cartilage Collagens with Heparin","authors":"Gerald N. Smith Jr. ,&nbsp;Kenneth D. Brandt","doi":"10.1016/S0174-173X(87)80024-9","DOIUrl":"10.1016/S0174-173X(87)80024-9","url":null,"abstract":"<div><p>Type XI collagen (1α2α3α) extracted from bovine articular cartilage by pepsin digestion binds strongly to heparin immobilized on agarose. The collagens from cartilage will bind to heparin-agarose in 0.1 M NaCl/2 M urea/0.01 M Tris-HC1 and can be eluted with a linear gradient of NaCl. Type XI begins to elute at NaCl concentrations higher than 0.28 M and is totally eluted at 0.40 M NaCl. The peak of elution occurs at 0.37 M NaCl. The other collagens of cartilage bind more weakly and are fully eluted when the NaCl concentration reaches 0.25 M. Collagen types I, III, and V are also bound to the column at low salt concentrations but are fully eluted before type XI begins to elute. All of the type XI preparation binds to heparin-agarose, suggesting that there is at least one binding site per molecule. Denatured 1 α and 2α chains bind strongly, suggesting that at least one binding site exists on both of these chains. These data confirm that the interaction between polyanions and type XI collagen is stronger than that with other known collagens and provide a method for purification of type XI without any type II contamination.</p><p>Cartilage collagens include several minor collagen types in addition to type II (Burgeson and Hollister, 1979; Reese and Mayne, 1981). Type XI, the collagen composed of the a chains designated lα, 2α, and 3α, binds to the high density proteoglycans of cartilage <em>in vitro</em>, apparently in a non-specific manner (Smith et al., 1985). This binding is stable in increasing concentrations of NaCl until the collagen fibrils begin to dissolve. Heparin and dextran sulfate are extremely potent inhibitors of the interaction.</p><p>The ability of heparin and dextran sulfate to inhibit the binding of fibrillar collagen to cartilage proteoglycans suggested that binding might also occur between type XI collagen and these highly sulfated polyanions. If so, this would provide a method to purify the cartilage collagens and to assess the relative strength of the interactions between the polyanion and the various collagen types in cartilage.</p><p>In this paper, we demonstrate the binding of soluble collagens to heparin immobilized on Sepharose 4B and examine the concentration of NaCl required to disrupt this binding.</p></div>","PeriodicalId":77694,"journal":{"name":"Collagen and related research","volume":"7 5","pages":"Pages 315-321"},"PeriodicalIF":0.0,"publicationDate":"1987-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0174-173X(87)80024-9","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14810974","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":"Monoclonal Antibodies to Bovine Collagenase Inhibitor","authors":"Shuji Kodama ,&nbsp;Jun-Ichi Kishi ,&nbsp;Ken-Ichi Obata ,&nbsp;Kazushi Iwata ,&nbsp;Taro Hayakawa","doi":"10.1016/S0174-173X(87)80027-4","DOIUrl":"10.1016/S0174-173X(87)80027-4","url":null,"abstract":"<div><p>Hybridoma antibodies against bovine collagenase inhibitor were produced by fusion of myeloma cells NS-1 (P3-NS 1-1) with spleen cells from mice hyperimmunized with collagenase inhibitor purified from the explant medium of bovine dental pulps. Hybridomas positive by an enzyme-linked immunosorbent assay (ELISA) for bovine collagenase inhibitor were cloned by the dilution method. Seventeen hybridomas producing antibodies were isolated, four of which also recognized purified human collagenase inhibitor in the ELISA. Using a monoclonal antibody-Sepharose affinity column, we easily purified both bovine and human collagenase inhibitors to homogeneity. They showed the same mobility on sodium dodecyl sulfate-polyacrylamide gel electrophoresis, corresponding to a molecular mass of 32,000 daltons.</p></div>","PeriodicalId":77694,"journal":{"name":"Collagen and related research","volume":"7 5","pages":"Pages 341-350"},"PeriodicalIF":0.0,"publicationDate":"1987-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0174-173X(87)80027-4","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14447056","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":"Supernatant from an Activated Human CD4+ T-Cell Clone Modulates the Proliferation and Collagen Synthesis of Human Dental Pulp Fibroblast","authors":"Martine Melin ,&nbsp;Sem Saeland ,&nbsp;Henry Magloire ,&nbsp;Daniel J. Hartmann ,&nbsp;Sylviane Guerret ,&nbsp;Dominique Blanchard ,&nbsp;Jacques Banchereau ,&nbsp;Jean-Alexis Grimaud","doi":"10.1016/S0174-173X(87)80029-8","DOIUrl":"https://doi.org/10.1016/S0174-173X(87)80029-8","url":null,"abstract":"<div><p>Several studies indicate a relationship between immunocompetent cells and fibroblast functions such as proliferation and collagen synthesis, which may be of importance in understanding the process of fibrosis. We demonstrate here the activity of supernatant from an activated human CD4+ proliferative T-cell clone (2F1) in stirhulating the proliferation of human dental pulp fibroblasts, while inhibiting their soluble type I collagen secretion in either growing or confluent cultures. Taken together, our results indicate that T-cell derived lymphokines may be of importance in regulating normal dental pulp fibroblast functions.</p></div>","PeriodicalId":77694,"journal":{"name":"Collagen and related research","volume":"7 5","pages":"Pages 371-381"},"PeriodicalIF":0.0,"publicationDate":"1987-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0174-173X(87)80029-8","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"92003794","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":"Collagenolytic Cathepsins of Rabbit Spleen: A Kinetic Analysis of Collagen Degradation and Inhibition by Chicken Cystatin","authors":"Rose A. Maciewicz ,&nbsp;David J. Etherington ,&nbsp;Janko Kos ,&nbsp;Vito Turk","doi":"10.1016/S0174-173X(87)80035-3","DOIUrl":"10.1016/S0174-173X(87)80035-3","url":null,"abstract":"<div><p>We have investigated the steady state kinetics of the degradation of native fibrillar collagen at pH 3.4 by four collagenolytic cathepsins of rabbit spleen. For each enzyme, the dependence of initial velocity on collagen concentration was well described by the Michaelis-Menten mechanism. K_m, expressed as the concentration of triple-helical chains, and k_cat values were determined for cathepsins B, L, N and S. The ratio of K_cat to K_m suggest that cathepsins L and N are far more effective at collagen solubilization than either cathepsins S or B. K; values were determined for the inhibition of collagenolytic activity at pH 3.4 using cystatin, a naturally-occurring cysteine proteinase inhibitor. All four cysteine proteinases were inhibited by cystatin in this assay system, although it was found to be a tighter binding inhibitor of cathepsin L, than for cathepsins N and S (approximately 5-fold less), or cathepsin B (approximately 500-fold less).</p></div>","PeriodicalId":77694,"journal":{"name":"Collagen and related research","volume":"7 4","pages":"Pages 295-304"},"PeriodicalIF":0.0,"publicationDate":"1987-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0174-173X(87)80035-3","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14785468","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":"Carrageenin-Stimulated Peritoneal Macrophages Release In Vitro Collagenase and Gelatinase","authors":"Ricardo López-Escalera,&nbsp;Annie Pardo","doi":"10.1016/S0174-173X(87)80031-6","DOIUrl":"10.1016/S0174-173X(87)80031-6","url":null,"abstract":"<div><p>Guinea pig macrophages were obtained by intraperitoneal injection of carrageenin, and in contrast with peritoneal cells from non-stimulated animals, release <em>in vitro</em> an active collagenase into the culture medium. Short time trypsin incubations and treatment of enzyme preparations with 4-APMA failed to reveal latent enzyme activity. Metallopeptidases specific for gelatin paralleled the presence of collagenase in the media of stimulated cells. Raw medium was fractionated by affinity chromatography with heparin-sepharose, collagenase activity bound to heparin sepharose while a gelatinase with an apparent molecular weight of 54,800 did not. When macrophages were grown <em>in vitro</em> in the presence of albumin, the gelatinase activity showed affinity for heparin and an apparent molecular weight of 113,000.</p></div>","PeriodicalId":77694,"journal":{"name":"Collagen and related research","volume":"7 4","pages":"Pages 249-257"},"PeriodicalIF":0.0,"publicationDate":"1987-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0174-173X(87)80031-6","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13960296","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":"Induction and Suppression of Type I Collagenase in Cultured Human Cells","authors":"Chu Chang Chua ,&nbsp;Denis Barritault ,&nbsp;Deborah E. Geiman ,&nbsp;Roger L. Ladda","doi":"10.1016/S0174-173X(87)80033-X","DOIUrl":"10.1016/S0174-173X(87)80033-X","url":null,"abstract":"<div><p>A number of peptide growth factors have been shown to induce the secretion of type I collagenase into the medium of human fibroblast cultures (Chua et al., 1985). In this study the ability of eye-derived growth factor, lectin and tumor-promoting agents on collagenase induction in human fibroblast cells were examined. These agents were found to be able to induce collagenase production to a similar extent as epidermal growth factor. Dexamethasone at 10-100 nM was found to suppress collagenase induction in human fibroblast cells. The cell-type specifictiy of this enzyme induction by growth factors was studied by using a human epidermoid carcinoma cell line, A-431. An M, 55,000 band appeared in the medium of A-431 cells upon 22 h exposure to EGF. Two-dimensional peptide pattern of the Mr 55,000 band in A-431 cells was identical to the counterpart in HF cells. Our results indicated that the induction of collagenase was not unique to human fibroblast cultures.</p></div>","PeriodicalId":77694,"journal":{"name":"Collagen and related research","volume":"7 4","pages":"Pages 277-284"},"PeriodicalIF":0.0,"publicationDate":"1987-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0174-173X(87)80033-X","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13961021","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}