V V Swarte, D H Joziasse, R E Mebius, D H van den Eijnden, G Kraal
{"title":"L-selectin-mediated lymphocyte aggregation: role of carbohydrates, activation and effects on cellular interactions.","authors":"V V Swarte, D H Joziasse, R E Mebius, D H van den Eijnden, G Kraal","doi":"10.3109/15419069809010790","DOIUrl":"https://doi.org/10.3109/15419069809010790","url":null,"abstract":"<p><p>L-selectin on lymphocytes reacts with glycosylated ligands on high endothelial venule walls in lymphoid organs. Through this carbohydrate-dependent interaction, rolling and initial attachment of lymphocytes to endothelium is mediated. Here we have studied an earlier described L-selectin-induced homotypic aggregation, to further elucidate the events that occur after engagement of L-selectin. It was found that the interaction of L-selectin with fucoidan, but not with other carbohydrates, or with monoclonal antibodies directed against the carbohydrate recognition domain of L-selectin, resulted in homotypic aggregation among both B- or T lymphocytes. Importantly, this aggregation was shown to be both lymphocyte function-associated antigen-1 (LFA-1) and calcium-independent. Furthermore, for aggregation metabolic energy was required, and signalling via protein tyrosine kinase appeared to be involved. Neither de novo protein synthesis, protein kinase C mediated signalling, Gi-protein mediated signal transduction, nor calcium mobilization were required for aggregation. During aggregation, L-selectin was not shed from the lymphocyte's cell surface. Finally, it was found that the lymphocyte binding capacity to high endothelial venules on cryostat sections was not altered upon triggering these lymphocytes via L-selectin. Interestingly, L-selectin-triggered cells showed increased binding to paracortical areas in peripheral lymph nodes. Our data suggest that signals via L-selectin, might lead to altered expression of cell surface molecules, important in interactions other than the first stage of lymphocyte rolling.</p>","PeriodicalId":79325,"journal":{"name":"Cell adhesion and communication","volume":"6 4","pages":"311-22"},"PeriodicalIF":0.0,"publicationDate":"1998-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/15419069809010790","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"20773619","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}
E Schuuring, H van Damme, E Schuuring-Scholtes, E Verhoeven, R Michalides, E Geelen, C de Boer, H Brok, V van Buuren, P Kluin
{"title":"Characterization of the EMS1 gene and its product, human Cortactin.","authors":"E Schuuring, H van Damme, E Schuuring-Scholtes, E Verhoeven, R Michalides, E Geelen, C de Boer, H Brok, V van Buuren, P Kluin","doi":"10.3109/15419069809004475","DOIUrl":"https://doi.org/10.3109/15419069809004475","url":null,"abstract":"<p><p>We have identified a novel gene, EMS1, that is consistently amplified and overexpressed in human carcinomas with an amplification of the chromosome 11q13 region. Comparisons of the EMS1 sequences with those present in the GenBank databases revealed a high identity with chicken cortactin. Southern and western blot analyses confirm the high sequence conservation during evolution. An antiserum specific for human cortactin, showed in gene transfer experiments that both human p80 and p85 isoforms are encoded by the EMS1 cDNA. Further comparisons demonstrated an high sequence and structural homology with HS1 that is implicated in signal transduction in lymphoid cells only. Expression of EMS1/cortactin mRNA was restricted to tumor cell lines derived from non-lymphoid origin. Cortactin contains (i) a filamentous actin binding tandem repeat domain, (ii) a proline-rich SH3-binding and (iii) a SH3 domain that is common in proteins involved in signal transduction. Our data suggest that human EMS1/cortactin has a function in signal transmission between cell-matrix contact sites and the cytoskeleton and, as such, its overexpression due to 11q13 amplification might effect adhesive properties of human carcinomas.</p>","PeriodicalId":79325,"journal":{"name":"Cell adhesion and communication","volume":"6 2-3","pages":"185-209"},"PeriodicalIF":0.0,"publicationDate":"1998-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/15419069809004475","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"20733938","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":"Integrin signaling: cytoskeletal complexes, MAP kinase activation, and regulation of gene expression.","authors":"E H Danen, R M Lafrenie, S Miyamoto, K M Yamada","doi":"10.3109/15419069809004477","DOIUrl":"https://doi.org/10.3109/15419069809004477","url":null,"abstract":"<p><p>Members of the integrin family of adhesion receptors mediate interactions of cells with the extracellular matrix. Besides their role in tissue morphogenesis by anchorage of cells to basement membranes and migration along extracellular matrix proteins, integrins are thought to play a key role in mediating the control of gene expression by the extracellular matrix. Studies over the past 10 years have shown that integrin-mediated cell adhesion can trigger signal transduction cascades involving translocation of proteins and protein tyrosine phosphorylation events. In this review, we discuss approaches used in our lab to study early events in integrin signalling as well as further downstream changes.</p>","PeriodicalId":79325,"journal":{"name":"Cell adhesion and communication","volume":"6 2-3","pages":"217-24"},"PeriodicalIF":0.0,"publicationDate":"1998-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/15419069809004477","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"20733940","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}
R van der Zee, T Murohara, J Passeri, M Kearney, D A Cheresh, J M Isner
{"title":"Reduced intimal thickening following alpha(v)beta3 blockade is associated with smooth muscle cell apoptosis.","authors":"R van der Zee, T Murohara, J Passeri, M Kearney, D A Cheresh, J M Isner","doi":"10.3109/15419069809109146","DOIUrl":"https://doi.org/10.3109/15419069809109146","url":null,"abstract":"<p><p>The adhesion integrin alpha(v)beta3 is expressed by both activated endothelial cells (ECs) and smooth muscle cells (SMCs). Peptide and antibody antagonists of alpha(v)beta3 have been shown to block angiogenesis by initiating unscheduled programmed cell death of proliferating ECs. The present study was designed to determine if antagonism of alpha(v)beta3 immediately following balloon injury might similarly lead to programmed cell death among activated SMCs, and thereby inhibit intimal thickening. LM609, a monoclonal antibody antagonist of alpha(v)beta3, was administered locally and/or systemically immediately after balloon angioplasty in a rabbit model of vascular injury. Immunohistochemical studies documented that LM609, even when administered systemically, localized to sites of vascular injury. LM609 administered immediately following balloon injury of the external iliac artery markedly reduced intimal thickening at 2 and 4 wk post-injury. Apoptosis was abundant where balloon injury resulted in expression of alpha(v)beta3. At both 2 and 4 wk, re-endothelialization at the site of balloon injury was not retarded in LM609-treated rabbits versus controls. Thus, blockade of alpha(v)beta3 inhibits intimal thickening when administered immediately following balloon injury. This favorable impact on neointimal thickening is associated with apoptosis of activated SMCs expressing alpha(v)beta3. These findings may explain the reduction in restenosis observed clinically following beta3 integrin blockade.</p>","PeriodicalId":79325,"journal":{"name":"Cell adhesion and communication","volume":"6 5","pages":"371-9"},"PeriodicalIF":0.0,"publicationDate":"1998-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/15419069809109146","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"21093230","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":"Conserved amphipathic helices near the N-terminus and C-terminus of the alpha subunit of cranin (dystroglycan).","authors":"N R Smalheiser","doi":"10.3109/15419069809109148","DOIUrl":"https://doi.org/10.3109/15419069809109148","url":null,"abstract":"<p><p>Cranin (dystroglycan) is a ubiquitously expressed extracellular matrix receptor, synthesized as a single precursor, which is cleaved into an extracellular subunit (alpha) and a transmembrane subunit (beta). The primary sequence of cranin (dystroglycan) is known from cDNA cloning, and the protein has been strongly implicated in morphogenesis, cell adhesion and human disease. Nevertheless, the domain structure of the alpha subunit has not been well studied; although the protein binds to matrix proteins, to the beta subunit, to cell surfaces, and possibly to other membrane proteins such as sarcoglycans, the domains responsible for mediating these interactions remain unknown. Here I report computer analyses that identify two distinctive amphipathic alpha-helical regions near the N-terminus and C-terminus of the alpha subunit, which are conserved in all species for which sequence information is currently available. This finding should stimulate and guide experimental studies designed to understand how the alpha subunit is associated with the cell surface and with its various ligands.</p>","PeriodicalId":79325,"journal":{"name":"Cell adhesion and communication","volume":"6 5","pages":"401-4"},"PeriodicalIF":0.0,"publicationDate":"1998-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/15419069809109148","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"21093189","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":"The mesenchymal cadherin-11 is expressed in restricted sites during the ontogeny of the rat brain in modes suggesting novel functions.","authors":"L Simonneau, J P Thiery","doi":"10.3109/15419069809109151","DOIUrl":"https://doi.org/10.3109/15419069809109151","url":null,"abstract":"<p><p>Cadherin-11 (Cad-11), a cell cell adhesion molecule belonging to the \"classical type II\" cadherin family, is a marker of the loosely connected and migratory cellular elements of the mesenchyme. Interestingly, by using in situ hybridization, regional high expression of cad-11 was seen in the brain as well as the spinal cord. We made the following observations in rat embryos and neonates: (1) cad-11 first appears at the lips of the open neural tube; (2) shortly after neural tube closure, cad-11 delineates boundaries in the fore- and midbrain while a metameric signal is detected in the rhombencephalon; (3) cad-11 expression is found in specific neuroepithelia and ependyma; (4) in the fetal developing brain, cad-11 transcripts are present during the formation of precise cortical layers, in various brain nucleus or subsets of nuclei and in circumventricular organs; (5) intense cad-11 expression is located at the point of optic nerve exit and entry; (6) cad-11 signal accompanies, in a spatio-temporal manner, the dynamics of cell migration in the cortex from lateral ganglionic eminence through the cortico-striatal sulcus. These data are discussed, and hypotheses for additional and novel properties for cad-11 are suggested.</p>","PeriodicalId":79325,"journal":{"name":"Cell adhesion and communication","volume":"6 5","pages":"431-50"},"PeriodicalIF":0.0,"publicationDate":"1998-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/15419069809109151","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"21093192","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}
K Berencsi, V Endresz, D Klurfeld, L Kari, D Kritchevsky, E Gönczöl
{"title":"Early atherosclerotic plaques in the aorta following cytomegalovirus infection of mice.","authors":"K Berencsi, V Endresz, D Klurfeld, L Kari, D Kritchevsky, E Gönczöl","doi":"10.3109/15419069809005597","DOIUrl":"https://doi.org/10.3109/15419069809005597","url":null,"abstract":"<p><p>We show here that BALB/c mice inoculated with murine cytomegalovirus (MCMV) express viral antigens in the endothelial and smooth muscle cells of the aortic wall, and that accumulation of inflammatory cells in the aortic lumen, similar to that seen in early atherosclerotic lesions in humans, colocalizes with the site of virus antigen expression. Immunosuppression of the mice at the time of virus infection increased the expression of viral antigens and the size of early atherosclerotic lesions in the intima. The percentage of the low-density lipoprotein cholesterol (LDL-C), the major lipid contributor to atherosclerotic plaques, was significantly increased in the serum of MCMV-infected mice, whether or not the mice were fed a high cholesterol diet. Human cytomegalovirus (HCMV) significantly increased the esterified cholesterol component of the total cholesterol in a human arterial smooth muscle cell line infected in vitro with HCMV. These results suggest that CMV infection is involved in two of the major mechanisms that lead to development of atherosclerosis, i.e., immune injury and high LDL-C.</p>","PeriodicalId":79325,"journal":{"name":"Cell adhesion and communication","volume":"5 1","pages":"39-47"},"PeriodicalIF":0.0,"publicationDate":"1998-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/15419069809005597","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"20556560","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}
J M Weiss, A C Renkl, J Sleeman, H Dittmar, C C Termeer, S Taxis, N Howells, E Schöpf, H Ponta, P Herrlich, J C Simon
{"title":"CD44 variant isoforms are essential for the function of epidermal Langerhans cells and dendritic cells.","authors":"J M Weiss, A C Renkl, J Sleeman, H Dittmar, C C Termeer, S Taxis, N Howells, E Schöpf, H Ponta, P Herrlich, J C Simon","doi":"10.3109/15419069809004472","DOIUrl":"https://doi.org/10.3109/15419069809004472","url":null,"abstract":"<p><p>Upon antigen encounter epidermal Langerhans cells (LC) and dendritic cells (DC) emigrate from peripheral organs and invade lymph nodes through the afferent lymphatic vessels and then assemble in the paracortical T cell zone and present antigen to T lymphocytes. Part of this process is mimicked by metastasizing tumor cells. Since splice variants of CD44 promote metastasis to lymph nodes we explored the expression of CD44 proteins on migrating LC and DC. We show that following antigen contact, LC and DC upregulate pan CD44 epitopes and epitopes encoded by variant exons v4, v5, v6 and v9. Antibodies against CD44 epitopes arrest LC in the epidermis, prevent the binding of activated LC and DC to the T cell zones of lymph nodes, and severely inhibit their capacity to induce a delayed type hypersensitivity reaction to a skin hapten in vivo. Our results demonstrate that CD44 splice variant expression is obligatory for the migration and function of LC and DC.</p>","PeriodicalId":79325,"journal":{"name":"Cell adhesion and communication","volume":"6 2-3","pages":"157-60"},"PeriodicalIF":0.0,"publicationDate":"1998-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/15419069809004472","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"20733935","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":"A series of function blocking antibodies against the alpha v beta 3 integrin bind allosteric to the ligand binding site and induce ligand dissociation.","authors":"E C Lin, C P Carron, D M Meyer, J W Smith","doi":"10.3109/15419069809010794","DOIUrl":"https://doi.org/10.3109/15419069809010794","url":null,"abstract":"<p><p>The alpha v beta 3 integrin plays a critical role in bone resorption, angiogenesis, and tumor cell invasion. A blockade of this receptor has therapeutic potential in osteoporosis, vascular restenosis, and cancer. In this report, we characterize the mechanism by which six monoclonal antibodies inhibit the function of alpha v beta 3. All six antibodies interact with a common site that is partially comprised of residues 164-202 within the beta 3 subunit. This domain is physically separate from the RGD binding site, and appears to regulate ligand binding allosterically. Thus, the blocking antibodies function, in part, by inducing the dissociation of ligand from alpha v beta 3. Although this family of antibodies is able to virtually abolish alpha v beta 3-mediated cell adhesion, they only block about one-half of soluble ligand binding to the integrin. This observation is consistent with the idea that two functionally distinct populations of alpha v beta 3 are present on the cell surface. The unique mechanism of action of these antibodies provides new insight in the structure-function relationships of alpha v beta 3, and also suggest that such antibodies are likely to behave differently than RGD mimetics if used as drugs.</p>","PeriodicalId":79325,"journal":{"name":"Cell adhesion and communication","volume":"6 6","pages":"451-64"},"PeriodicalIF":0.0,"publicationDate":"1998-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/15419069809010794","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"20835818","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":"Cadherin mediated cell-cell adhesion is regulated by tyrosine phosphatases in human keratinocytes.","authors":"C Soler, P Rousselle, O Damour","doi":"10.3109/15419069809005595","DOIUrl":"https://doi.org/10.3109/15419069809005595","url":null,"abstract":"<p><p>Normal Human Keratinocytes express on their cell surface E- and P-cadherins, two Ca2+ dependent homophilic cell adhesion molecules that mediate keratinocyte-keratinocyte adherens junctions. In other cell types, adherens-type junctions are reported to be major subcellular targets for tyrosine specific protein phosphorylation (Volberg et al. (1991) Cell Regul., 2, 105-120) involving tyrosine kinases and tyrosine phosphatases. We investigated the role of tyrosine phosphatases in the regulation of cadherin mediated keratinocyte-keratinocyte adhesion. We report the results of a wide tyrosine phosphatase inhibition using pervanadate, a modified vanadate derivative known to inhibit most tyrosine phosphatases. Keratinocytes treated with pervanadate, exhibit an important change in cellular morphology and cadherins/catenins localization as shown by phase contrast microscopy and immunocytochemistry. In this conditions, cadherins and catenins no longer colocalize with the actin cytoskeleton of cells and the amount of E-cadherin bound to the cytoskeleton decreases. A more intense phosphotyrosine labelling is seen at the edges of the treated cells, suggesting that an increase in the phosphorylation rate of some cadherin-catenin complex proteins induces a diminished intercellular adhesion. Finally immunoprecipitation experiments of the E-cadherin/catenin complex from pervanadate treated keratinocytes reveal an increase in the tyrosine phosphorylation rate of E-cadherin, beta catenin and probably gamma catenin. These data suggest an essential role for the protein tyrosine phosphatases in keratinocyte intercellular junctions.</p>","PeriodicalId":79325,"journal":{"name":"Cell adhesion and communication","volume":"5 1","pages":"13-25"},"PeriodicalIF":0.0,"publicationDate":"1998-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/15419069809005595","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"20556558","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}