Collagen and related research最新文献

{"title":"Characterization of a Monoclonal Antibody Recognizing Small Collagenous Proteins in Fetal Bone","authors":"Fumiyuki Kuwata ,&nbsp;Masao Maeno ,&nbsp;Kam-Ling Yao ,&nbsp;Carmelo Domenicucci ,&nbsp;Harvey A. Goldberg ,&nbsp;Safia Wasi ,&nbsp;Jane E. Aubin ,&nbsp;Jaro Sodek","doi":"10.1016/S0174-173X(87)80020-1","DOIUrl":"10.1016/S0174-173X(87)80020-1","url":null,"abstract":"<div><p>A monoclonal antibody (MBP-322) that recognizes two small collagenous, apatite-binding (SCAB) proteins associated with the mineral phase of fetal bone, has been prepared. The SCAB proteins, which are quantitatively extracted from bone with EDTA, have been shown by immunotransf er analyses to have M_rs of 28K and 25K and both were selectively degraded by bacterial collagenase. Amino acid analysis of the collagenase-digested protein revealed a hypro:pro:gly ratio of approximately 0.5:1:0.7 for both proteins and indicated that one-third of the protein could have a collagen-like sequence. The SCAB proteins, unlike other collagens and collagen fragments tested bound quantitatively to hydroxylapatite in the presence of 4M guanidine hydrochloride and appear to be unique to bone. The antibody, however, was not specific for the SCAB proteins and showed comparable immunoreactivity against denatured α1 chains of types I, II and III collagens and the α2 chains of types I and V collagens but not type IV collagen nor native collagens I–V. The epitope was further localized to the CB6 fragment in the α1(I) chain and the CB5 fragment of a1 (III) chain, and was present in both the TC^A and TC^B fragments of α2(I). Despite the immunological reactivity, the properties of the SCAB proteins were not consistent with their being derived from known collagen types.</p><p>Immunocytochemical staining of permeabilized bone cells with MPB-322 showed a perinuclear, punctate staining pattern in most cells with some cells showing specific nuclear staining. In non-permeabilized cells, the antibody stained various sized spherical particles, many of which were closely associated with the cell surface. Immunoblots of cell proteins revealed a number of immunoreactive proteins sensitive to collagenase digestion including two proteins with Mrs similar to the SCAB proteins. The MBP-322 antibody appears useful for identifying sequence homology in various collagens, and for recognizing denatured collagen and specific collagen fragments in tissues, as well as being important for the further characterization of the SCAB proteins.</p></div>","PeriodicalId":77694,"journal":{"name":"Collagen and related research","volume":"7 1","pages":"Pages 39-55"},"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)80020-1","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14427145","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":"Effect of Polyanions on Fibrillogenesis by Type XI Collagen","authors":"Gerald N. Smith Jr. ,&nbsp;James M. Williams ,&nbsp;Kenneth D. Brandt","doi":"10.1016/S0174-173X(87)80018-3","DOIUrl":"10.1016/S0174-173X(87)80018-3","url":null,"abstract":"<div><p>Type XI collagen (1α, 2α, 3α) from bovine articular cartilage forms fibrils at 4 °C in 0.15 M NaCl at pH 7.4, but fibrillogenesis is inhibited by the addition of 1 M glucose or by raising the NaCl concentration to 1 M. Removal of the glucose or NaCl by dialysis allows fibril formation. When proteoglycans, heparin, or chondroitin sulfate were added to type XI collagen in 1 M NaCl both fibrillogenesis and polyanion-collagen interaction were inhibited by the high NaCl concentration. When the mixture was dialysed against 0.15 M NaCl, a new aggregate type was seen, scattered among shortened and branched fibers. The new aggregates were either X-, Y-, or wheel-shaped structures with electron dense cores. They were apparently formed by collagen molecules intersecting approximately 200 nm from one end. In contrast, when the polyanion was mixed with the collagen in 1 M glucose, which inhibits fibrillogenesis but not polyanion-collagen interaction, a different type of aggregate appeared following dialysis. These aggregates were discrete 280 × 40 nm structures with an asymmetric banding pattern. They are similar to SLS aggregates, and probably are composed of collagen molecules lined up in register. The results are different from those seen with the interstitial collagens and emphasize the unique character of the interaction of polyanions, including proteoglycan, with type XI collagen.</p></div>","PeriodicalId":77694,"journal":{"name":"Collagen and related research","volume":"7 1","pages":"Pages 17-25"},"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)80018-3","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14243764","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":"IVth International Symposium on Renal Basement Membranes and Related Research","authors":"","doi":"10.1016/S0174-173X(87)80023-7","DOIUrl":"https://doi.org/10.1016/S0174-173X(87)80023-7","url":null,"abstract":"","PeriodicalId":77694,"journal":{"name":"Collagen and related research","volume":"7 1","pages":"Page 91"},"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)80023-7","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"136849396","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"The Gene Coding for Tropoelastin is Represented as a Single Copy Sequence in the Haploid Sheep Genome","authors":"Louise Olliver ,&nbsp;Phyllis A. Luvalle ,&nbsp;Jeffrey M. Davidson ,&nbsp;Joel Rosenbloom ,&nbsp;Christopher G. Mathew ,&nbsp;Andre J. Bester ,&nbsp;Charles D. Boyd","doi":"10.1016/S0174-173X(87)80022-5","DOIUrl":"10.1016/S0174-173X(87)80022-5","url":null,"abstract":"<div><p>The identity of the primary <em>in vitro</em> translation products of fetal sheep nuchal ligament elastin mRNA was confirmed as two distinct polypeptides of 63 Kdal and 65Kdal in both rabbit reticulocyte and wheat germ extract cell-free translation systems. Both polypeptides were co-translationally processed by a microsomal membrane signal peptidase, with the removal of 20–25 amino acid residues. A single (3.5 kb) RNA species encodes both tropoelastin polypeptides. Restriction endonuclease mapping of sheep genomic DNA by hybridisation with two radiolabelled genomic DNA fragments containing sequences coding for sheep tropoelastin (pSE1-1.3 and pSE1-0.7,) indicated the presence of a single elastin gene. The elastin gene copy number was further quantitated by comparison of hybridisation of pSE1-1.3 and pSE1-0.7 to slot-blots and Southern transfers of sheep genomic DNA and to standard curves constructed with each clone. These results clearly demonstrate that each of these sequences is represented only once per haploid genome, suggesting that the two tropoelastin polypeptides are products of a single elastin gene.</p></div>","PeriodicalId":77694,"journal":{"name":"Collagen and related research","volume":"7 1","pages":"Pages 77-89"},"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)80022-5","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14729585","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":"Comparison of Axial Banding Patterns in Fibrils of Type V Collagen and Type I Collagen","authors":"Eijiro Adachi ,&nbsp;Toshihiko Hayashi","doi":"10.1016/S0174-173X(87)80019-5","DOIUrl":"10.1016/S0174-173X(87)80019-5","url":null,"abstract":"<div><p>Type V collagen and type I collagen were obtained from human placenta, essentially by salt fractionation. Precipitates were formed from mixed solutions of type V collagen and type I collagen in various ratios. They were incubated at 37°C for 1 hour and negatively stained with 0.5% uranyl acetate (pH 4.4) at 37°C. The specimens, seen by electron microscopy, were fibrils with a D-periodic banding pattern. Axial electron density profiles of collagen fibrils were obtained from selected electron micrographs by densitometric tracing. The sl width corresponded to 1.5 nm. The relative electron densities of overlap region vs. hole region were lower than 20% in fine fibrils containing a significant amount of type V collagen. It is suggested that the overlap region of such collagen fibrils may be loosely packed, being accessible to uranyl acetate, or the hole region may be filled by larger non-collagenous portions of type V collagen, resulting in loss of the light and dark alternation. Six to 8 white transverse lines were discerned per period and labeled consecutively with Arabic numerals. White lines 2 and 5 tended to merge with lines 1 and 4, respectively, in collagen fibrils formed from a solution containing a significant amount of type I collagen or pure type I collagen. The eight white lines corresponded to c2, c1, b2, b1, a4, a1, e1 and d with reference to their locations in the D-period. The locations of white lines in collagen fibrils which contain significant amount of type V collagen were identical with those in type I collagen fibrils. This is consistent with the primary structure that the axial distribution of charged amino acids in type V collagen is quite similar to that in type I collagen.</p></div>","PeriodicalId":77694,"journal":{"name":"Collagen and related research","volume":"7 1","pages":"Pages 27-38"},"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)80019-5","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14729584","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":"Abscorbate Effects on Type I Procollagen Synthesis by Human Adult Skin Fibroblasts: Different Migration Positions of Type I Procollagen Chains on SDS Polyacrylamide Gel after Incubation with Ascorbate","authors":"Kazuhiko Takehara,&nbsp;Gary R. Grotendorst,&nbsp;Maria Trojanowska,&nbsp;E. Carwile Leroy","doi":"10.1016/S0174-173X(87)80045-6","DOIUrl":"10.1016/S0174-173X(87)80045-6","url":null,"abstract":"<div><p>The effects of ascorbate and steroids on type I procollagen synthesis by human skin fibroblasts were studied. Ascorbate treatment (50 μg/ml) for 24 hours stimulated a 2–3 fold increase in type I procollagen synthesis and an unexpected-shift in the mobility of type I procollagen on SDS polyacrylamide gels. The kinetics of the increase in procollagen synthesis (4 hours) and the shift in electrophoretic mobility (1 hour) were dissimilar, suggesting different controlling mechanisms. This was confirmed by the addition of α-α'-dipyridyl to ascorbate-treated cultures which eliminated the ascorbate-induced shift in electrophoretic mobility without altering the amount of procollagen synthesis. In contrast, hydrocortisone (1.5 μM) reduced the ascorbate-induced stimulation of type I procollagen synthesis by 80% but did not affect the ascorbate-induced shift in electrophoretic mobility. These studies indicate that the ascorbate-induced increase in type I procollagen synthesis is due to increased levels of type I procollagen mRNA and is independent of the level of hydroxylation of the procollagen.</p></div>","PeriodicalId":77694,"journal":{"name":"Collagen and related research","volume":"6 6","pages":"Pages 455-466"},"PeriodicalIF":0.0,"publicationDate":"1987-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0174-173X(87)80045-6","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14703590","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":"Authors Index","authors":"","doi":"10.1016/S0174-173X(87)80051-1","DOIUrl":"https://doi.org/10.1016/S0174-173X(87)80051-1","url":null,"abstract":"","PeriodicalId":77694,"journal":{"name":"Collagen and related research","volume":"6 6","pages":"Pages 533-534"},"PeriodicalIF":0.0,"publicationDate":"1987-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0174-173X(87)80051-1","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"136475753","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Acidic Glycosaminoglycans, Isolation and Structural Analysis of a Proteodermatan Sulfate from Dermatosparactic Calf Skin","authors":"Etsuji Matsunaga ,&nbsp;Hiroshi Shinkai ,&nbsp;Betty Nusgens ,&nbsp;Charles M. Lapière","doi":"10.1016/S0174-173X(87)80046-8","DOIUrl":"10.1016/S0174-173X(87)80046-8","url":null,"abstract":"<div><p>Dermatan sulfate and hyaluronic acid are the major glycosaminoglycan components of dermatosparactic and normal calf skin but the ratio of hyaluronic acid to dermatan sulfate is 50–70% higher in dermatosparactic calf skin than that in normal calf skin. Hyaluronic acid in normal calf skin could be extracted to 93% of the total by NaCl and guanidine hydrochloride, while in dermatosparactic calf skin 57% of hyaluronic acid remained in the insoluble material after NaCl and guanidine hydrochloride extraction. The recovery of proteodermatan sulfate in NaCl extracts was similar in normal and dermatosparactic skin. The amount of proteodermatan sulfate extracted in guanidine hydrochloride form normal calf skin was 2–4 fold higher than that from dermatosparactic calf skin. No significant difference between dermatosparactic and normal calf skin proteodermatan sulfate could be detected in terms of size of the core protein (M_r = 55,000) by sodium dodecyl sulfate polyacrylamide gel electrophoresis, amino acid analysis, immunological cross-reactivity using polyclonal antibodies against either dermatosparactic or normal calf skin core protein, tryptic peptides or size of dermatan sulfate chains (M_r = 17000-18000) on gel chromatography.</p></div>","PeriodicalId":77694,"journal":{"name":"Collagen and related research","volume":"6 6","pages":"Pages 467-479"},"PeriodicalIF":0.0,"publicationDate":"1987-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0174-173X(87)80046-8","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14703591","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":"Morphometric Study of Cauliflower Collagen Fibrils in Dermatosparaxis of the Calves","authors":"Gérald E. Piérard,&nbsp;Trinh Lê,&nbsp;Jean-François Hermanns,&nbsp;Betty V. Nusgens,&nbsp;Charles M. Lapière","doi":"10.1016/S0174-173X(87)80047-X","DOIUrl":"10.1016/S0174-173X(87)80047-X","url":null,"abstract":"<div><p>The abnormal cauliflower collagen fibrils present in the skin of dermatosparactic calves were studied by electron microscopy and computerized image analysis.</p><p>The structure of the fibrils is heterogeneous and varies according to their location in the dermis. Cauliflower fibrils seems due to a defect in the lateral cohesion between the constitutive procollagen polymers. This is associated with the presence of a non-collageneous material larger than the aminopropeptide surrounding the procollagen polymers, while the volume occupied by procollagen in each fibril is comparable to that of collagen in normal fibrils.</p></div>","PeriodicalId":77694,"journal":{"name":"Collagen and related research","volume":"6 6","pages":"Pages 481-492"},"PeriodicalIF":0.0,"publicationDate":"1987-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0174-173X(87)80047-X","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14703592","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":"Contraction of Hydrated Collagen Gels by Fibroblasts: Evidence for Two Mechanisms by which Collagen Fibrils are Stabilized","authors":"Clyde Guidry,&nbsp;Frederick Grinnell","doi":"10.1016/S0174-173X(87)80050-X","DOIUrl":"10.1016/S0174-173X(87)80050-X","url":null,"abstract":"<div><p>Studies were conducted to learn more about the mechanism by which fibroblasts contract hydrated collagen gels, a process that may be important in the supramolecular organization of the extracellular matrix. Removal of cells from contracted gels by two different methods, treatment with detergent or treatment with trypsin/EDTA solution, had no visible effect on the bundles of collagen fibrils that had been organized in frameworks around and in between the cells. There was, however, a portion of the collagen gels that expanded after the cells were removed. We conclude that during concentration of collagen gels by fibroblasts, rearranged collagen fibrils were stabilized in place by two different mechanisms. At first, the fibrils were mechanically held in place by the cells. Subsequently, the fibrils were stabilized by non-covalent chemical interactions that are independent of cells. A model system for studying collagen gel reorganization in the absence of cells was developed based on centrifugation of the gels. The overall features of collagen gel reorganization by centrifugation were similar to the features of collagen gel contraction by cells. The collagen fibrils of gels reorganized by centrifugation were at first stabilized mechanically and the gels expanded after centrifugation was stopped. With additional time, the collagen fibrils were stabilized by non-covalent chemical interactions, and then the gels no longer expanded after centrifugation was stopped.</p></div>","PeriodicalId":77694,"journal":{"name":"Collagen and related research","volume":"6 6","pages":"Pages 515-529"},"PeriodicalIF":0.0,"publicationDate":"1987-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0174-173X(87)80050-X","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14703595","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}