Cell adhesion and communication最新文献

{"title":"Integrin signaling: cytoskeletal complexes, MAP kinase activation, and regulation of gene expression.","authors":"E H Danen,&nbsp;R M Lafrenie,&nbsp;S Miyamoto,&nbsp;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}

{"title":"Adhesion and signaling mediated by the cytoplasmic tails of leucocyte integrins.","authors":"Y van Kooyk,&nbsp;M Lub,&nbsp;C G Figdor","doi":"10.3109/15419069809004480","DOIUrl":"https://doi.org/10.3109/15419069809004480","url":null,"abstract":"<p><p>Integrins not only mediate cell adhesion but also contribute to a variety of other cellular processes including proliferation, cytokine production, cytotoxicity and apoptosis. They act as bi-directional signal transducers, mediating signaling from inside-to-outside the cell and from outside-to-inside the cell. Evidence is emerging that signaling through leukocyte integrins (beta 2 and beta 7) is distinct from signaling by the more widely distributed beta 1 integrins. Here we discuss the role of the cytoplasmic domains of leukocyte integrins and that of cytosolic proteins that bind integrins in mediating signal transduction. Distinct sites in the alpha as well as the common beta chain contribute to this process. We also show that beta 2 integrin distribution on the cell surface is of particular relevance for leukocytes to rapidly alter their adhesive state and display their highly dynamic adhesive behavior. From these and recently published findings the picture is arising that particular cell functions may be supported by integrin-specific signaling pathways.</p>","PeriodicalId":79325,"journal":{"name":"Cell adhesion and communication","volume":"6 2-3","pages":"247-54"},"PeriodicalIF":0.0,"publicationDate":"1998-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/15419069809004480","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"20734546","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":"Making a little affinity go a long way: a topological view of LFA-1 regulation.","authors":"M L Dustin","doi":"10.3109/15419069809004481","DOIUrl":"https://doi.org/10.3109/15419069809004481","url":null,"abstract":"Lymphocytes utilize adhesion to navigate in the body and to transiently interact with a variety of potential antigen presenting cells. Interactions of adhesion molecules are governed by the law of mass action and the less understood rules of apposed biological membranes. Biochemical parameters such as adhesion molecule affinity only tell part of the story. Factors such as lateral mobility, membrane alignment and cytoskeletal interactions are equally important in determining the final outcome. Therefore it is important to determine mechanisms by which the properties of cell membranes and the cytoskeleton reinforce or hinder adhesion molecule interactions. Work from my lab has shown that one mechanism by which lymphocyte adhesion molecules cooperate is to align adhering membranes with nanometer precision. Here, I discuss a model for LFA-1 regulation that is dependent on three independent processes: LFA-1 lateral mobility, ligand induced generation of a small amount of high affinity LFA-1 and local membrane alignment. I propose that coordination of these processes allows rapid interconversion between stable adhesion and detachment.","PeriodicalId":79325,"journal":{"name":"Cell adhesion and communication","volume":"6 2-3","pages":"255-62"},"PeriodicalIF":0.0,"publicationDate":"1998-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/15419069809004481","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"20734547","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 multistep process of homotypic neutrophil aggregation: a review of the molecules and effects of hydrodynamics.","authors":"S I Simon,&nbsp;S Neelamegham,&nbsp;A Taylor,&nbsp;C W Smith","doi":"10.3109/15419069809004482","DOIUrl":"https://doi.org/10.3109/15419069809004482","url":null,"abstract":"<p><p>Homotypic adhesion of neutrophils stimulated with chemoattractant is analogous to capture on vascular endothelium in that both processes are supported by L-selectin and beta 2-integrin adhesion receptors. Under hydrodynamic shear, cell adhesion requires that receptors bind sufficient ligand over the duration of intercellular contact to withstand the hydrodynamic stresses. Using cone and plate viscometry to apply a uniform linear shear field to suspensions of neutrophils and flow cytometry to quantitate the size distribution of aggregates formed over the time course of formyl peptide stimulation, we conducted a detailed examination of the affect of shear rate and shear stress on the kinetics of cell aggregation. The efficiency of aggregate formation was fit from a mathematical model based on Smoluchowski's two-body collision theory. Over a range of venular shear rates (400-800 s-1), approximately 90% of the single cells are recruited into aggregates ranging from doublets to grouping larger than sextuplets. Adhesion efficiency fit to the kinetics of aggregation increased with shear rate from approximately 20% at 100 s-1 to a maximum level of approximately 80% at 400 s-1. This increase to peak adhesion efficiency was dependent on L-selectin and beta 2-integrin, and was resistant to shear stress up to approximately 7 dyn/cm2. When L-selectin was blocked with antibody, beta 2-integrin (CD11a,b) supported adhesion at low shear rates (< 400 s-1). Aggregates formed over the rapid phase of aggregation remain intact and resistant to shear up to 120 s. At the end of this plateau phase of stability, aggregates spontaneously dissociate back to singlets. The rate of cell disaggregation is linearly proportional to the applied shear rate. The binding kinetics of selectin and integrin appear to be optimized to function within discrete ranges of shear rate and stress, providing an intrinsic mechanism for the transition from neutrophil tethering to firm but reversible adhesion.</p>","PeriodicalId":79325,"journal":{"name":"Cell adhesion and communication","volume":"6 2-3","pages":"263-76"},"PeriodicalIF":0.0,"publicationDate":"1998-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/15419069809004482","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"20734548","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,&nbsp;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}

{"title":"Early atherosclerotic plaques in the aorta following cytomegalovirus infection of mice.","authors":"K Berencsi,&nbsp;V Endresz,&nbsp;D Klurfeld,&nbsp;L Kari,&nbsp;D Kritchevsky,&nbsp;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}

{"title":"CD44 variant isoforms are essential for the function of epidermal Langerhans cells and dendritic cells.","authors":"J M Weiss,&nbsp;A C Renkl,&nbsp;J Sleeman,&nbsp;H Dittmar,&nbsp;C C Termeer,&nbsp;S Taxis,&nbsp;N Howells,&nbsp;E Schöpf,&nbsp;H Ponta,&nbsp;P Herrlich,&nbsp;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,&nbsp;C P Carron,&nbsp;D M Meyer,&nbsp;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,&nbsp;P Rousselle,&nbsp;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}