Zena Werb , Patrice Tremble , Zena Werb , Caroline H. Damsky , Patrice Tremble , Caroline H. Damsky
{"title":"Regulation of extracellular matrix degradation by cell—extracellular matrix interactions","authors":"Zena Werb , Patrice Tremble , Zena Werb , Caroline H. Damsky , Patrice Tremble , Caroline H. Damsky","doi":"10.1016/0922-3371(90)90043-V","DOIUrl":"10.1016/0922-3371(90)90043-V","url":null,"abstract":"<div><p>An appropriate balance of extracellular matrix synthesis and degradation is required for normal morphogenesis and maintenance of tissue architecture. Extracellular matrix molecules and their receptors, as well as proteinases and their inhibitors, are all involved in matrix remodeling. In this report we show that signal transduction through extracellular matrix receptors regulates matrix remodeling.</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 299-306"},"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)90043-V","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13305286","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}
Magnus Hook , Martin J. McGavin , Rampyari Raja , Giuseppe Raucci , Magnus Hook , Lech M. Switalski , Per-Eric Lindgren , Martin Lindberg , Christer Signas
{"title":"Interactions of bacteria with extracellular matrix proteins","authors":"Magnus Hook , Martin J. McGavin , Rampyari Raja , Giuseppe Raucci , Magnus Hook , Lech M. Switalski , Per-Eric Lindgren , Martin Lindberg , Christer Signas","doi":"10.1016/0922-3371(90)90060-A","DOIUrl":"10.1016/0922-3371(90)90060-A","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 433-438"},"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)90060-A","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13125121","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}
Carl G. Gahmberg, Pekka Nortamo, Carmela Kantor, Matti Autero, Pekka Kotovuori, Leena Hemiö, Rosalba Salcedo, Manuel Patarroyo
{"title":"The pivotal role of the Leu-CAM and ICAM molecules in human leukocyte adhesion","authors":"Carl G. Gahmberg, Pekka Nortamo, Carmela Kantor, Matti Autero, Pekka Kotovuori, Leena Hemiö, Rosalba Salcedo, Manuel Patarroyo","doi":"10.1016/0922-3371(90)90036-V","DOIUrl":"10.1016/0922-3371(90)90036-V","url":null,"abstract":"<div><p>Cellular adhesion is of fundamental importance in leukocyte physiology. It is a complex, strictly regulated process, which involves the participation of several cell surface glycoproteins. Among the most important are the Leu-CAMs or the DC11 / CD18 integrin receptors, and their adhesion ligands ICAM-1 (CD54) and ICAM-2. In this review we summarize some recent work on various aspects of these molecules.</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 239-245"},"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)90036-V","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13140906","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":"Detailed contents","authors":"","doi":"10.1016/0922-3371(90)90064-4","DOIUrl":"https://doi.org/10.1016/0922-3371(90)90064-4","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 456-457"},"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)90064-4","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"137398916","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":"Proteolytic balance and capillary morphogenesis","authors":"M.S. Pepper , R. Montesano","doi":"10.1016/0922-3371(90)90046-Y","DOIUrl":"10.1016/0922-3371(90)90046-Y","url":null,"abstract":"<div><p>Angiogenesis is the process by which new capillary blood vessels are formed from preexisting vessels. A number of components of this morphogenetic process, including endothelial cell invasion and capillary lumen formation, are believed to be dependent on tightly controlled proteolytic degradation of the extracellular matrix. The critical importance of an appropriate balance between proteases and protease inhibitors in these processes is suggested by two sets of observations. Firstly, that extracellular matrix invasion and capillary lumen formation are inhibited in the presence of an excess of protease inhibitors. Secondly, that when unchecked by protease inhibitors, excessive proteolysis is incompatible with normal capillary morphogenesis. These results clearly suggest that a precisely regulated proteolytic balance is necessary for normal capillary morphogenesis.</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 319-327"},"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)90046-Y","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12876097","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}
Pier Carlo Marchisio , Ranieri Cancedda , Michele De Luca
{"title":"Structural and functional studies of integrin receptors in cultured human keratinocytes","authors":"Pier Carlo Marchisio , Ranieri Cancedda , Michele De Luca","doi":"10.1016/0922-3371(90)90050-7","DOIUrl":"10.1016/0922-3371(90)90050-7","url":null,"abstract":"<div><p>In human keratinocytes cultured in conditions which allow differentiation and stratification and which are suitable to reconstitute a fully functional epidermis, the integrin α<sub>6</sub>β<sub>4</sub> and two members of the β<sub>1</sub> integrin family (α<sub>2</sub>β<sub>1</sub> and α<sub>3</sub>β<sub>1</sub>) were polarized to the basal and lateral domains of the plasma membrane both in growing colonies and in the reconstituted epidermis. Conversely, α<sub>v</sub>β<sub>5</sub> integrin was expressed at the basal surface in growing and migrating but not in stationary keratinocytes. The integrin α<sub>6</sub>β<sub>4</sub> was organized in patches and spots corresponding to F-actin-free submembraneous areas and did not colocalize to focal contacts; moreover, α<sub>6</sub>β<sub>4</sub> colocalized with patches of laminin deposited underneath the ventral membrane of individual cells. The two β<sub>1</sub> laminin receptor integrins (α<sub>2</sub>β<sub>1</sub> and α<sub>3</sub>β<sub>1</sub>) were never found in the basal domain but matched the lateral position of vinculin (but not talin), cingulin and desmoplakins. Only the integrin complex α<sub>v</sub>β<sub>5</sub> was associated with talin- and vinculin-containing focal adhesions mostly in the peripheral cells of expanding keratinocyte colonies and in coincidence with fibronectin strands. The topography of β<sub>1</sub> and β<sub>4</sub> integrins reflects a functional role in adhesion and in the maintenance of the state of aggregation of cultured keratinocytes since lateral aggregation was impaired by antibodies to β<sub>1</sub> whereas antibodies to β<sub>4</sub> prevented cell-matrix adhesion.</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 355-359"},"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)90050-7","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13305163","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}
Antti Vaheri , Ross W. Stephens , Eeva-Marjatta Salonen , Jari Pöllänen, Hannele Tapiovaara
{"title":"Plasminogen activation at the cell surface-matrix interface","authors":"Antti Vaheri , Ross W. Stephens , Eeva-Marjatta Salonen , Jari Pöllänen, Hannele Tapiovaara","doi":"10.1016/0922-3371(90)90038-X","DOIUrl":"10.1016/0922-3371(90)90038-X","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 255-262"},"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)90038-X","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13305284","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}
Karl Tryggvason , Pirkko Huhtala , Ari Tuuttila , Louise Chow , Jorma Keski-Oja , Jouko Lohi
{"title":"Structure and expression of type IV collagenase genes","authors":"Karl Tryggvason , Pirkko Huhtala , Ari Tuuttila , Louise Chow , Jorma Keski-Oja , Jouko Lohi","doi":"10.1016/0922-3371(90)90044-W","DOIUrl":"10.1016/0922-3371(90)90044-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 307-312"},"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)90044-W","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13125119","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}
Martin E. Hemler , Mariano J. Elices , Bosco M.C. Chan , Yoshikazu Takada , Bruce Zetter , Nariaki Matsuura
{"title":"Multiple ligand binding functions for VLA-2 α2β1 and VLA-3 (α3β1) in the integrin family","authors":"Martin E. Hemler , Mariano J. Elices , Bosco M.C. Chan , Yoshikazu Takada , Bruce Zetter , Nariaki Matsuura","doi":"10.1016/0922-3371(90)90035-U","DOIUrl":"10.1016/0922-3371(90)90035-U","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 229-238"},"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)90035-U","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13125115","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":"Expression of tenascin and of the ED-B containing oncofetal fibronectin isoform in human cancer","authors":"Guido Nicolò , Sandra Salvi , Gianbattista Oliveri , Laura Borsi , Patrizia Castellani , Luciano Zardi","doi":"10.1016/0922-3371(90)90056-3","DOIUrl":"10.1016/0922-3371(90)90056-3","url":null,"abstract":"<div><p>Tenascin (TN) and the oncofetal ED-B containing fibronectin isoform (B-FN) have been reported to be stromal markers of a number of malignancies. Here we report on studies of the distribution of TN and B-FN in normal adult tissues and in benign and malignant tumors, as well as on the levels of the B-FN mRNA in cultured fetal and non-fetal human fibroblasts originating from different tissues. B-FN has an extremely restricted distribution in normal adult tissues, is not expressed in benign tumors, but is greatly expressed in a high percentage of malignant tumors. On the contrary, human TN in normal adult tissues is less restricted than what has previously been reported and it is largely expressed in a number of both benign and malignant tumors. Moreover, we observed a great variability in the relative amount of B-FN mRNA among the 17 normal human fibroblast cell lines tested. We found very low levels in non-fetal skin fibroblasts and higher levels in fetal lung fibroblasts. We also found differences in the relative amounts of B-FN mRNA between fibroblast cell lines originating from the skin and the lung of the same subject.</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 401-408"},"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)90056-3","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12876099","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}