Cell differentiation and development : the official journal of the International Society of Developmental Biologists最新文献

{"title":"Transforming growth factor-β1 induces extracellular matrix formation in glomerulonephritis","authors":"Wayne A. Border ,&nbsp;Erkki Ruoslahti","doi":"10.1016/0922-3371(90)90059-6","DOIUrl":"10.1016/0922-3371(90)90059-6","url":null,"abstract":"<div><p>Extracellular matrices can be important in disease. Glomerulonephritis is an inflammation of the kidney that is characterized by the accumulation of extracellular matrix within the damaged glomeruli. We have shown that transforming growth factor-β1 (TGF-β1) is unique in regulating the production of proteoglycans and matrix glycoproteins by glomerular cells in vitro. In an experimental model of glomerulonephritis in rats, we found increased proteoglycan and fibronectin synthesis by cultured nephritic glomeruli, which was greatly reduced by the addition of antiserum to TGF-β1. Conditioned media from glomerular cultures, when added to normal cultured mesangial cells, induced elevated proteoglycan synthesis. The stimulatory activity of the conditioned media was blocked by addition of TGF-β1 antiserum. Glomerular histology showed mesangial matrix expansion in a time course that roughly paralleled the elevated proteoglycan synthesis by the nephritic glomeruli. At the same time there was an increased expression of TGF-β1 mRNA and TGF-β1 protein in the glomeruli. Administration of anti-TGF-β1 at the time of induction of glomerulonephritis suppressed the elevated extracellular matrix production and dramatically attenuated histological manifestations of the disease. A small proteoglycan, decorin, also inhibits the activity of TGF-β, potentially providing an alternative format for the prevention of TGF-β activity. Our results provide direct evidence for a causal role of TGF-β1 in the pathogenesis of the experimental disease and suggest a new approach to the therapy of glomerulonephritis.</p></div>","PeriodicalId":77508,"journal":{"name":"Cell differentiation and development : the official journal of the International Society of Developmental Biologists","volume":"32 3","pages":"Pages 425-431"},"PeriodicalIF":0.0,"publicationDate":"1990-12-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0922-3371(90)90059-6","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13254603","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":"Growth factor control of extracellular proteolysis","authors":"D.B. Rifkin ,&nbsp;D. Moscatelli ,&nbsp;J. Bizik ,&nbsp;N. Quarto ,&nbsp;F. Blei ,&nbsp;P. Dennis ,&nbsp;R. Flaumenhaft ,&nbsp;P. Mignatti","doi":"10.1016/0922-3371(90)90045-X","DOIUrl":"10.1016/0922-3371(90)90045-X","url":null,"abstract":"<div><p>The involvement of proteases and growth factors in angiogenesis is complex. The angiogenic factor basic fibroblast growth factor (bFGF) induces increased synthesis of both plasminogen activator and collagenase in endothelial cells. In addition, bFGF increases the number of plasminogen activator receptors on the cell surface. Increased production of plasmin may be responsible for the release of soluble complexes of heparan sulfate-bFGF which may be the active form of bFGF. The activity of a negative regulator of angiogenesis, transforming growth factor β (TGF-β), is also regulated by proteases since the released latent form of TGF-β is activated by a surface proteolytic assembly plasminogen activator and plasmin. Since TGF-β induces an inhibitor of plasminogen activator, the activation reaction is self-regulatory.</p></div>","PeriodicalId":77508,"journal":{"name":"Cell differentiation and development : the official journal of the International Society of Developmental Biologists","volume":"32 3","pages":"Pages 313-318"},"PeriodicalIF":0.0,"publicationDate":"1990-12-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0922-3371(90)90045-X","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12876096","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":"Extracellular matrix proteins and their receptors in the normal, hyperplastic and neoplastic breast","authors":"Victor E. Gould ,&nbsp;George K. Koukoulis ,&nbsp;Ismo Virtanen","doi":"10.1016/0922-3371(90)90057-4","DOIUrl":"10.1016/0922-3371(90)90057-4","url":null,"abstract":"<div><p>We studied by immunohistochemistry, the distribution of tenascin (Ten), cellular fibronectin (cFn), laminin and certain pertinent extracellular matrix protein receptors in normal human female breast, variants of fibrocystic disease (FCD), benign tumors, and ductal and lobular carcinomas. Monoclonal antibodies (mAb) to Ten, extradomain A containing cFn (EDAcFn), A and B chains of laminin, and beta-1 (β-1) and different α subunits of integrins were used.</p><p>In in-situ ductal and lobular carcinomas, laminin staining had focal gaps, Ten-immunoreactivity displayed periductal or periacinar bands, and cFn showed broad and intense periductal staining; strong reactions for β-1 and α-6 were noted in the basal cytoplasm of non-neoplastic myoepithelial cells while few tumor cells stained weakly. In infiltrating ductal and lobular carcinomas (IDC, ILC), laminin reactivity was weak, uneven or absent around neoplastic clusters whereas stromal staining for Ten and cFn was extensive and strong. In most IDC, moderate β-1 and α-6 staining involved variable subpopulations; one mucinous carcinoma stained strongly and diffusely. In 20–40% of cells in ILC, β-1 and α-6 were localized in delicate, ramified cytoplasmic processes. Indirect immunofluorescence studies with mAbs to other α-integrin subunits suggest that in various breast carcinomas only α-3 is expressed in tumor cells and that the vessels contained α-1 integrin.</p><p>As compared with the normal breast, FCD and benign tumors, reactivity for Ten and cFn is increased in breast carcinomas while laminin is attenuated and decreased or absent; yet, Ten cannot be regarded as a carcinoma marker since it can be detected in benign tumors, FCD, and even in the normal breast. Reactivity for β-1 and α-6 integrin subunits is decreased in all breast carcinomas; however, the comparatively strong and distinctly localized reactions noted in lobular vs ductal carcinomas may well reflect biological and clinical differences between these two main breast carcinoma phenotypes.</p></div>","PeriodicalId":77508,"journal":{"name":"Cell differentiation and development : the official journal of the International Society of Developmental Biologists","volume":"32 3","pages":"Pages 409-416"},"PeriodicalIF":0.0,"publicationDate":"1990-12-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0922-3371(90)90057-4","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12876047","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":"Syndecan and tenascin: Induction during early tooth morphogenesis and possible interactions","authors":"Irma Thesleff,&nbsp;Seppo Vainio,&nbsp;Markku Salmivirta,&nbsp;Markku Jalkanen","doi":"10.1016/0922-3371(90)90054-Z","DOIUrl":"10.1016/0922-3371(90)90054-Z","url":null,"abstract":"","PeriodicalId":77508,"journal":{"name":"Cell differentiation and development : the official journal of the International Society of Developmental Biologists","volume":"32 3","pages":"Pages 383-389"},"PeriodicalIF":0.0,"publicationDate":"1990-12-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0922-3371(90)90054-Z","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12876098","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 molecular basis for the assembly and modulation of adherens-type junctions","authors":"Benjamin Geiger,&nbsp;Dorit Ginsberg,&nbsp;Daniela Salomon,&nbsp;Tova Volberg","doi":"10.1016/0922-3371(90)90049-3","DOIUrl":"10.1016/0922-3371(90)90049-3","url":null,"abstract":"","PeriodicalId":77508,"journal":{"name":"Cell differentiation and development : the official journal of the International Society of Developmental Biologists","volume":"32 3","pages":"Pages 343-353"},"PeriodicalIF":0.0,"publicationDate":"1990-12-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0922-3371(90)90049-3","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13283287","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":"Role of cell-matrix contacts in cell migration and epithelial-mesenchymal transformation","authors":"Elizabeth D. Hay","doi":"10.1016/0922-3371(90)90052-X","DOIUrl":"10.1016/0922-3371(90)90052-X","url":null,"abstract":"<div><p>Epithelial cells make contact with extracellular matrix via receptors on the basal surface that interact with the basal actin cortex. In 3D matrix, the mesenchymal cell makes contact with matrix all around its circumference via similar receptors. When moving, the fibroblast is constantly constructing a new front end. We postulate in a ‘fixed cortex’ theory of cell motility that the circumferential actin cortex is firmly attached to matrix and that the myosin-rich endoplasm slides past it into the continually forming new front end. During epithelial-mesenchymal transformation, the presumptive mesenchymal cell seems to turn on the new front end mechanism as a way of emigrating from the epithelium into the underlying matrix with which it makes ‘fixed’ contacts. Master genes may exist that regulate the expression of epithelial genes on the one hand, and mesenchymal genes on the other.</p></div>","PeriodicalId":77508,"journal":{"name":"Cell differentiation and development : the official journal of the International Society of Developmental Biologists","volume":"32 3","pages":"Pages 367-375"},"PeriodicalIF":0.0,"publicationDate":"1990-12-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0922-3371(90)90052-X","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13254602","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":"Interactions between type 1 plasminogen activator inhibitor, extracellular matrix and vitronectin","authors":"D. Seiffert ,&nbsp;J. Mimuro ,&nbsp;R.R. Schleef ,&nbsp;D.J. Loskutoff","doi":"10.1016/0922-3371(90)90041-T","DOIUrl":"10.1016/0922-3371(90)90041-T","url":null,"abstract":"<div><p>Regulation of plasminogen activation is a key process in controlling proteolytic events in the extracellular matrix (ECM) and this regulation is achieved through the action of specific plasminogen activator (PA) inhibitors (PAIs). Type I PAI (PAI-1) is the physiological inhibitor both of urinary-type PA (u-PA) and tissue-type PA (t-PA) (Loskutoff et al., 1989) and is a major component of the ECM of cultured cells. This inhibitor may protect ECM constituents against cellular proteases and thus influence the cell migration and tissue destruction that occurs during development, inflammation and tumor metastasis. In this review, we discuss the properties of PAI-1 and the evidence that the binding of PAI-1 to ECM is mediated by serum-derived vitronectin (Vn).</p></div>","PeriodicalId":77508,"journal":{"name":"Cell differentiation and development : the official journal of the International Society of Developmental Biologists","volume":"32 3","pages":"Pages 287-292"},"PeriodicalIF":0.0,"publicationDate":"1990-12-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0922-3371(90)90041-T","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12876095","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":"Actin—membrane interaction in focal adhesions","authors":"Keith Burridge,&nbsp;Glen Nuckolls,&nbsp;Carol Otey,&nbsp;Fredrick Pavalko,&nbsp;Keiko Simon,&nbsp;Christopher Turner","doi":"10.1016/0922-3371(90)90048-2","DOIUrl":"10.1016/0922-3371(90)90048-2","url":null,"abstract":"<div><p>Focal adhesions are regions of the plasma membrane where cells in tissue culture adhere strongly to the underlying extracellular matrix, and which at their cytoplasmic face serve to anchor bundles of actin microfilaments. They provide an experimental model for studying the links between the cytoskeleton and the extracellular matrix. Members of the integrin family of extracellular matrix receptors are prominent components, spanning the membrane in focal adhesions, but there is evidence that other membrane components are also needed for these structures to form. A number of proteins are concentrated at the cytoplasmic face of focal adhesions. Recent efforts have sought to determine the links between actin and the integrin cytoplasmic domains. Using in vitro binding assays, two potential bridges between actin and integrin have been identified. One involves talin, which has recently been shown to bind actin directly. The other involves the actin-binding protein, α-actinin, which has been found to interact with several integrins. The physiological significance of these two potential bridges between actin and integrin remains to be determined in vivo.</p></div>","PeriodicalId":77508,"journal":{"name":"Cell differentiation and development : the official journal of the International Society of Developmental Biologists","volume":"32 3","pages":"Pages 337-342"},"PeriodicalIF":0.0,"publicationDate":"1990-12-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0922-3371(90)90048-2","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13283286","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 urokinase receptor and regulation of cell surface plasminogen activation","authors":"Francesco Blasi ,&nbsp;M. Vittoria Cubellis ,&nbsp;M. Teresa Masucci ,&nbsp;Lisbeth B. Møller ,&nbsp;David P. Olson ,&nbsp;Nina Pedersen ,&nbsp;Niels Behrendt ,&nbsp;Vincent Ellis ,&nbsp;Leif R. Lund ,&nbsp;Michael Ploug ,&nbsp;Ebbe Rønne ,&nbsp;Keld Danø","doi":"10.1016/0922-3371(90)90037-W","DOIUrl":"10.1016/0922-3371(90)90037-W","url":null,"abstract":"","PeriodicalId":77508,"journal":{"name":"Cell differentiation and development : the official journal of the International Society of Developmental Biologists","volume":"32 3","pages":"Pages 247-253"},"PeriodicalIF":0.0,"publicationDate":"1990-12-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0922-3371(90)90037-W","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13125116","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 expression and interactions of laminin in the developing nervous system","authors":"David Edgar","doi":"10.1016/0922-3371(90)90053-Y","DOIUrl":"10.1016/0922-3371(90)90053-Y","url":null,"abstract":"<div><p>This review discusses some of the recent developmental and molecular biological observations that have been made on laminin expression, distribution and neuronal interactions, in an attempt to delineate what might be the physiological function of laminin in the nervous system.</p></div>","PeriodicalId":77508,"journal":{"name":"Cell differentiation and development : the official journal of the International Society of Developmental Biologists","volume":"32 3","pages":"Pages 377-381"},"PeriodicalIF":0.0,"publicationDate":"1990-12-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0922-3371(90)90053-Y","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13140907","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}