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

{"title":"Transmembrane interactions at cell adhesion and invasion sites","authors":"Wen-Tien Chen","doi":"10.1016/0922-3371(90)90047-Z","DOIUrl":"10.1016/0922-3371(90)90047-Z","url":null,"abstract":"<div><p>Chicken embryonic fibroblasts transformed by Rous sarcoma virus (RSV-CEF) invade into a film of the extracellular matrix (ECM) by extending membrane protrusions, termed the invadopodia. The invadopodia share similar cytoskeletal components and membrane receptors for ECM components as adhesion sites. However, the organization of these transmembrane components at invadopodia and adhesion sites differs. In addition, degradation of the ECM occurs at sites of the invadopodia, but not at focal adhesions. Thus, the protease and integrin molecules on invadopodia are available for dynamic interactions with the ECM, cleaving established adhesion complexes as well as reconstituting new adhesion sites.</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 329-335"},"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)90047-Z","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13125120","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":"Modulation of the malignant phenotype with the urokinase-type plasminogen activator and the type I plasminogen activator inhibitor","authors":"Bernard Sordat ,&nbsp;Lars Reiter ,&nbsp;Jean-François Cajot","doi":"10.1016/0922-3371(90)90040-4","DOIUrl":"10.1016/0922-3371(90)90040-4","url":null,"abstract":"<div><p>Gene transfer techniques were utilized to evaluate the role of urokinase-type plasminogen activator (uPA) and plasminogen activator inhibitor type 1 (PAI-1) in enhancing or preventing the expression of the invasive malignant phenotype, respectively. Mouse L-cell transfectants expressing human uPA or human PAI-1 as well as mouse B16 transfectants expressing mouse uPA or human PAI-1 were generated. These transfectants were tested using a variety of experimental methods including smooth muscle cell matrix solubilization in vitro, lung colony formation in vivo and co-cultures of antagonist-expressing cells in vitro. Results from these studies provide direct evidence for an enhancing role of uPA in malignant invasion and experimental metastasis and for a modulatory role of PAI-1 in tumor cell-mediated breakdown of extracellular matrices.</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 277-285"},"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)90040-4","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13283354","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":"Mechanisms for organization of fibronectin matrix","authors":"Frances J. Fogerty ,&nbsp;Deane F. Mosher","doi":"10.1016/0922-3371(90)90061-Z","DOIUrl":"10.1016/0922-3371(90)90061-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 439-450"},"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)90061-Z","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13305165","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":"Epithelial integrins","authors":"Vito Quaranta","doi":"10.1016/0922-3371(90)90051-W","DOIUrl":"10.1016/0922-3371(90)90051-W","url":null,"abstract":"<div><p>We have undertaken the study of integrins specifically or predominantly expressed in epithelial cells, as they may be involved in establishing and maintaining properties peculiar to epithelia, such as polarization and morphogenetic movements. We describe here recent results regarding two such integrins. One of these contains the novel β chain, β₆, whose structure was deduced from cDNA clones. Some initial results on distribution and possible α chain associated to β₆ are discussed. Structural data are then summarized on another epithelial integrin, α₆β₄. The α₆ subunit and a variant form of the β₄ subunit were recently cloned in our laboratory. Adhesion assay results indicate that α₆β₄ may mediate attachment of epithelial cells to basement membranes.</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 361-365"},"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)90051-W","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13305164","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":"Plasminogen receptors in the mediation of pericellular proteolysis","authors":"Edward F. Plow ,&nbsp;Lindsey A. Miles","doi":"10.1016/0922-3371(90)90042-U","DOIUrl":"10.1016/0922-3371(90)90042-U","url":null,"abstract":"<div><p>A wide variety of cells bind plasminogen with very high capacity, with similar affinity and recognize the same structural features within the plasminogen molecule. As a consequence of binding to cell surfaces, plasminogen is more readily activated to plasmin. Plasmin remains cell-bound where it can degrade matrix constituents and is protected from inactivation by α₂-antiplasmin. Thus, the functional consequence of plasminogen binding to cells is pericellular proteolysis, permitting cell migration. Both proteins and nonprotein cell-surface constituents function as plasminogen binding sites. Gangliosides exhibit the appropriate properties of the non-protein plasminogen receptors.</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 293-298"},"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)90042-U","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13125118","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":"Integrins in human cells and tumors","authors":"Ismo Virtanen ,&nbsp;Matti Korkohen ,&nbsp;Liisa Laitinen ,&nbsp;Jari Ylänne ,&nbsp;Arja-Leena Kariniemi ,&nbsp;Victor E. Gould","doi":"10.1016/0922-3371(90)90034-T","DOIUrl":"10.1016/0922-3371(90)90034-T","url":null,"abstract":"<div><p>We have studied the distribution of the α- and β-subunits of integrins in developing and adult human kidney as well as in selected other tissues and cultured cells. In cultured cells some of the integrin subunits (β₁, α₁, α₂ and α₅) colocalize with talin at focal adhesions when plated on an appropriate ligand. Similarly, in tissues the polarization of β₁-integrins in colocalization with talin appears to indicate adhesive complexes, as demonstrated in adult glomeruli. In human kidney, the α subunits of integrins were seen to be segment-specifically expressed already in fetal tissues. In glomeruli the integrin α₁ subunit characterized mesangial cells while the α₂ and α₃ subunits showed immunoreactivity in endothelial cells and podocytes, respectively. In renal tubuli, the α₆ subunit, complexed with the β₁ subunit, showed a typical polarized distribution coaligning with the tubular basement membrane while the α₃ and α₂ subunits were expressed in distal tubular cells. These results suggested that in kidney the α₂β₁, α₃β₁, and α₆β₁ integrins can function as basement membrane receptors. The α₅ subunit was nearly lacking in the kidney and it appears to be mainly expressed in some smooth muscle cells. In other tissues distinct patterns in the expression of integrins were found. Thus, in many glandular epithelial cells the α₃β₁ integrin appeared to function as a basement membrane receptor while in various stratified epithelia and in the breast such a polarized localization could be found for the α₆β₄ integrin. Finally, although presenting a clearly polarized distribution for β₁ integrins, none of the α subunits could be found in cardiac or skeletal muscle cells and none of the integrins could be revealed in neuronal cells of human developing and adult cerebrum or cerebellum, although neurons in peripheral tissues contained abundantly the α₆β₁ integrin complex. In human tumors, the tumor cells, including also metastastatic tumors, generally presented the same integrins as their tissues of origin. In some poorly differentiated tumors both a population heterogeneity and even a lack of expression or a disorganization of basement membrane receptor integrins was obvious.</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 215-227"},"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)90034-T","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13254601","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":"Differential expression of tenascin splicing variants in the chick gizzard and in cell cultures","authors":"Yoichiro Matsuoka,&nbsp;Jürg Spring,&nbsp;Kurt Ballmer-Hofer,&nbsp;Urs Hofer,&nbsp;Ruth Chiquet-Ehrismann","doi":"10.1016/0922-3371(90)90058-5","DOIUrl":"10.1016/0922-3371(90)90058-5","url":null,"abstract":"<div><p>Tenascin is a large disulfide-linked hexameric extracellular matrix glycoprotein. It is a multidomain protein containing many repeated structural units such as heptad-, EGF-like-, and fibronectin type III repeats, as well as a homology to the globular domains of β- and γ-fibrinogen. In the chick embryo three major tenascin variants exist. They arise from one gene by alternative splicing of three of its 11 fibronectin type III repeats. Monoclonal antibodies against the alternatively spliced domains allowed us to study the expression of tenascin variants in tissue sections and in cell cultures. In the gizzard, the largest tenascin variant was only detected in the smooth muscle layer and the connective tissue below the epithelium of the villi, whereas the shortest tenascin variant was predominant in the tendons and the intramuscular connective tissue. Differential expression of tenascin variants was also obtained in cell cultures of chick embryo fibroblasts. Fetal calf serum equally stimulated the accumulation of all three tenascin variants, whereas after transformation with polyomavirus middle-T only the secretion of the largest tenascin variant was greatly enhanced.</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 417-423"},"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)90058-5","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12876048","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":"Serine protease and metallo protease cascade systems involved in pericellular proteolysis","authors":"James P. Quigley ,&nbsp;Mitchell B. Berkenpas ,&nbsp;Ronald T. Aimes ,&nbsp;Jinq May Chen","doi":"10.1016/0922-3371(90)90039-Y","DOIUrl":"10.1016/0922-3371(90)90039-Y","url":null,"abstract":"<div><p>Cultures of transformed fibroblasts actively involved in extracellular matrix degradation have been examined for initial activation of serine and metallo protease cascade systems. Rous sarcoma virus transformed chick embryo fibroblasts (RSVCEF), in contrast to transformed mammalian cells, produce active, two chain urokinase-type plasminogen activator (tcu-PA). Active tcu-PA is found in serum-free, plasmin-free conditioned medium from RSVCEF cultures as determined by two independent methods, immunoprecipitation and differential DFP sensitivity. RSVCEF cultures synthesize and secrete inactive, single chain uPA (scu-PA) which is converted to tcu-PA in a time dependent manner by a catalytic mechanism that appears to involve a functioning uPA receptor on the surface of intact cells. The enzyme activity responsible for this conversion may represent the initiating catalytic event in the PA/plasminogen serine protease cascade system.</p><p>A 70 kDa prometalloprotease capable of degrading denatured collagen following its activation also is significantly elevated in RSVCEF cultures over that of normal CEF. Trace amounts of the active 62 kDa form of the metalloprotease (gelatinase) is found in the transformed RSVCEF cultures indicating that these cultures produce a natural activator of the prometalloprotease. Plasmin and/or PA do not appear to be the activator of this enzyme as determined by indirect inhibition assays and direct assays employing purified enzymes. The possible central position of pro PA and the 70 kDa prometalloprotease in an interacting, complex protease cascade system involved in extracellular matrix degradation is discussed.</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 263-275"},"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)90039-Y","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13125117","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":"Ligand binding to integrins: Common and ligand specific recognition mechanisms","authors":"M.H. Ginsberg ,&nbsp;J.C. Loftus ,&nbsp;S. D'Souza ,&nbsp;E.F. Plow","doi":"10.1016/0922-3371(90)90033-S","DOIUrl":"10.1016/0922-3371(90)90033-S","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 203-213"},"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)90033-S","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13254600","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":"Genetic analysis of the Drosophila PS integrins","authors":"Michael Wilcox","doi":"10.1016/0922-3371(90)90055-2","DOIUrl":"10.1016/0922-3371(90)90055-2","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 391-399"},"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)90055-2","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13283288","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}