Cell adhesion and communication最新文献

{"title":"The relationship between perlecan and dystroglycan and its implication in the formation of the neuromuscular junction.","authors":"H B Peng,&nbsp;A A Ali,&nbsp;D F Daggett,&nbsp;H Rauvala,&nbsp;J R Hassell,&nbsp;N R Smalheiser","doi":"10.3109/15419069809005605","DOIUrl":"https://doi.org/10.3109/15419069809005605","url":null,"abstract":"<p><p>Perlecan is a major heparan-sulfate proteoglycan (HSPG) within the basement membrane surrounding skeletal muscle fibers. The C-terminus of its core protein contains three globular domain modules which are also found in laminin and agrin, two proteins that bind to dystroglycan (DG, cranin) on the muscle surface with these modules. In this study, we examined whether perlecan can also bind to DG and is involved in signaling the formation of the neuromuscular junction (NMJ). By labeling cultured muscle cells with a polyclonal anti-perlecan antibody, this protein is found both within the extracellular matrix in a fibrillar network and at the cell surface in a punctate pattern. In Xenopus muscle cells, the cell-surface perlecan is precisely colocalized with DG. Both perlecan and DG are clustered at ACh receptor clusters induced by spinal neurons or by beads coated with HB-GAM, a heparin-binding growth factor. Blot overlay assays have shown that perlecan binds alpha-DG in a calcium and heparin-sensitive manner. Furthermore, perlecan is present in muscle lysate immunoprecipitated with an anti-DG antibody. Immunolabeling also showed colocalization between HB-GAM and perlecan and between HB-GAM and DG. These data suggest that perlecan is anchored to muscle surface via DG-dystrophin complex. Since DG is also a site of agrin binding, the neural agrin secreted by motoneurons during NMJ formation may compete with the pre-existing perlecan for cell surface binding. This competition may result in the presentation of perlecan-bound growth factors such as HB-GAM to effect synaptic induction.</p>","PeriodicalId":79325,"journal":{"name":"Cell adhesion and communication","volume":"5 6","pages":"475-89"},"PeriodicalIF":0.0,"publicationDate":"1998-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/15419069809005605","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"20703471","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":"Role of Cx43 phosphorylation and MAP kinase activation in EGF induced enhancement of cell communication in human kidney epithelial cells.","authors":"G Vikhamar,&nbsp;E Rivedal,&nbsp;S Mollerup,&nbsp;T Sanner","doi":"10.3109/15419069809005603","DOIUrl":"https://doi.org/10.3109/15419069809005603","url":null,"abstract":"<p><p>Epidermal growth factor (EGF) has been found to induce enhanced gap junctional intercellular communication (GJIC) in the human kidney epithelial cell line K7. This is in contrast to what is reported for other cell types, which all show decreased GJIC in response to EGF. In the present study it is shown that 12-O-tetradecanoylphorbol-13-acetate (TPA) and EGF induce similar phosphorylation pattern of the gap junction protein connexin43 (Cx43) in K7 cells, although their effects on GJIC are opposite. Tyrosine phosphorylation of a 42 kD protein was observed to be induced concomitantly with phosphorylation of Cx43. EGF was however found to induce only serine phosphorylation of Cx43, indicating that the tyrosine kinase activity of the EGF receptor was not directly affecting the gap junction protein. The 42 kD protein phosphorylated on tyrosine was identified to be a mitogen activated protein (MAP) kinase. Both EGF and TPA was found to activate MAP kinase in these cells. Phosphorylation of Cx43 and enhancement of GJIC in response to EGF occurred with difference in time course. Phosphorylation of Cx43 was completed within 15 min, while the enhanced GJIC appeared 2-3 h later. It is therefore possible that regulation of synthesis or transport of Cx43 is responsible for the increase in GJIC, rather than direct involvement of Cx43 phosphorylation. This is in support of our previous finding that protein synthesis is necessary for EGF induced upregulation of GJIC in K7 cells.</p>","PeriodicalId":79325,"journal":{"name":"Cell adhesion and communication","volume":"5 6","pages":"451-60"},"PeriodicalIF":0.0,"publicationDate":"1998-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/15419069809005603","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"20703469","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":"Neutralization of TNF by the antibody cA2 reveals differential regulation of adhesion molecule expression on TNF-activated endothelial cells.","authors":"M T Nakada,&nbsp;S H Tam,&nbsp;D S Woulfe,&nbsp;K A Casper,&nbsp;R A Swerlick,&nbsp;J Ghrayeb","doi":"10.3109/15419069809005606","DOIUrl":"https://doi.org/10.3109/15419069809005606","url":null,"abstract":"<p><p>Upregulation of adhesion proteins plays an important role in mediating inflammation. The induction of adhesive molecules has been well studied, but the reversibility of their expression has not been well characterized. A neutralizing anti-TNF monoclonal antibody (cA2) was used to study the down regulation of TNF-induced E-selectin, vascular cell adhesion molecule-1 (VCAM-1) and intercellular adhesion molecule-1 (ICAM-1) on cultured human umbilical vein endothelial cells (HUVECs). Addition of cA2 following TNF stimulation of HUVECs enhanced the rate of E-selectin and VCAM-1 down-regulation from the cell surface and also reduced steady state E-selectin and VCAM-1 mRNA levels. The cA2-mediated disappearance of E-selectin, but not VCAM-1 protein was microtubule and not microfilament dependent. Neutralization of TNF only slightly reduced ICAM-1 cell surface levels following initial TNF stimulation, suggesting a slower turnover of ICAM-1 compared to E-selectin and VCAM-1. Microtubule inhibition during TNF stimulation partially inhibited E-selectin, VCAM-1 and ICAM-1 mRNA upregulation. VCAM-1 and ICAM-1 cell surface expression were similarly partially inhibited, however, E-selectin levels were unaffected, presumably due to the dual, opposing effect of inhibiting protein expression and inhibiting internalization. Microfilament inhibition during protein induction specifically inhibited the maximal expression of VCAM-1 protein and mRNA, without affecting E-selectin or ICAM-1. These data support the notion that E-selectin, VCAM-1, and ICAM-1 expression are differentially regulated on HUVECs and suggest that TNF neutralizing therapies may be effective because of their ability to reduce the levels of pre-existing adhesion proteins.</p>","PeriodicalId":79325,"journal":{"name":"Cell adhesion and communication","volume":"5 6","pages":"491-503"},"PeriodicalIF":0.0,"publicationDate":"1998-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/15419069809005606","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"20703472","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":"Cell interactions with collagen matrices in vivo and in vitro depend on phosphatidylinositol 3-kinase and free cytoplasmic calcium.","authors":"K Ahlén,&nbsp;A Berg,&nbsp;F Stiger,&nbsp;A Tengholm,&nbsp;A Siegbahn,&nbsp;E Gylfe,&nbsp;R K Reed,&nbsp;K Rubin","doi":"10.3109/15419069809005604","DOIUrl":"https://doi.org/10.3109/15419069809005604","url":null,"abstract":"<p><p>We have investigated the role of phosphatidylinositol 3-kinase (PI3-kinase) in cellular interactions with collagenous matrices. Platelet-derived growth factor-BB (PDGF-BB) elicited a mobilization of intracellular Ca2+ in pig aortic endothelial (PAE) cells transfected with wild type PDGF beta-receptor. This response was greatly reduced in PAE cells transfected with PDGF beta-receptors mutated at positions Y740 and Y751 to prevent PI3-kinase binding. The experimental drug 1D-myo-inositol 1,2,6-trisphosphate (alpha-trinositol) induced a rapid increase and subsequent oscillations of the cytoplasmic Ca2+ concentration in cultured fibroblasts. This response was not due to an effect of alpha-trinositol on inositol 1,4,5-trisphosphate (IP3) receptors. alpha-Trinositol did not influence PDGF-BB elicited chemotaxis through collagen-coated membranes of PAE cells transfected with the wild-type PDGF beta-receptor, but restored PDGF-BB elicited chemotaxis of PAE cells transfected with the PI3-kinase binding-site mutated PDGF beta-receptor. Collagen gel contraction has been suggested to serve as a model for cellular control of interstitial fluid pressure (PIF) in dermis. The PI3-kinase inhibitors wortmannin (50 nM) and LY294002 (5 microM) inhibited the stimulation of fibroblast-mediated collagen gel contraction by 0.4 nM PDGF-BB. Injection of wortmannin in rat paw skin induced a lowering of PIF, and this effect was abolished in animals pre-treated with alpha-trinositol. Pretreatment of rats with alpha-trinositol abolished the decrease in PIF induced by injecting monoclonal anti-rat alpha 2 beta 1 integrin IgG in rat paw skin. Taken together our data indicate that cell-collagen interactions in vivo and in vitro depend on PI3-kinase, and that this dependence can be bypassed by a drug eliciting intracellular Ca2+ mobilization.</p>","PeriodicalId":79325,"journal":{"name":"Cell adhesion and communication","volume":"5 6","pages":"461-73"},"PeriodicalIF":0.0,"publicationDate":"1998-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/15419069809005604","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"20703470","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":"Gap junctional communication between murine macrophages and intestinal epithelial cell lines.","authors":"C A Martin,&nbsp;F R Homaidan,&nbsp;T Palaia,&nbsp;R Burakoff,&nbsp;M E el-Sabban","doi":"10.3109/15419069809005602","DOIUrl":"https://doi.org/10.3109/15419069809005602","url":null,"abstract":"<p><p>In intestinal inflammation, inflammatory cells infiltrate the submucosa and are found juxtaposed to intestinal epithelial cell (IEC) basolateral membranes and may directly regulate IEC function. In this study we determined whether macrophage (M phi), P388D1 and J774A.1, are coupled by gap junctions to IEC lines, Mode-K and IEC6. Using flow cytometric analysis, we show bi-directional transfer of the fluorescent dye, calcein (700 Da) between IEC and M phi resulting in a 3.5-20-fold increase in recipient cell fluorescence. Homocellular and heterocellular dye transfer between M phi and/or IEC was detected in cocultures of P388D1, J774A.1, Mode-K, IEC6 and CMT93. However, transfer between P388D1 and Mode-K was asymmetrical in that transfer from P388D1 to Mode-K was always more efficient than transfer from Mode-K to P388D1. Dye transfer was strictly dependent on IEC-M phi adhesion which in turn was dependent on the polarity of IEC adhesion molecule expression. Both calcein dye transfer and adhesion were inhibited by the addition of heptanol to cocultures. Furthermore we demonstrate both IEC homocellular, and M phi-IEC heterocellular propagation of calcium waves in response to mechanical stimulation, typical of gap junctional communication. Finally, areas of close membrane apposition were seen in electron micrographs of IEC-M phi cocultures, suggestive of gap junction formation. These data indicate that IEC and M phi are coupled by gap junctions suggesting that gap junctional communication may provide a means by which inflammatory cells might regulate IEC function.</p>","PeriodicalId":79325,"journal":{"name":"Cell adhesion and communication","volume":"5 6","pages":"437-49"},"PeriodicalIF":0.0,"publicationDate":"1998-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/15419069809005602","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"20703513","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":"Transglutaminase-mediated oligomerization of galectin-3 modulates human melanoma cell interactions with laminin.","authors":"F A van den Brûle,&nbsp;F T Liu,&nbsp;V Castronovo","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Tumor cell adhesion and migration to laminin are important events during invasion and metastatic spread. Galectin-3, a multifunctional member of the galectin family, binds specifically the poly-N-acetyllactosamine residues of laminin and has been implicated in tumor invasion and metastasis. Galectin-3 is multimerized by transglutaminase, an enzyme that catalyzes cross-linking between glutamine and other aminoacid residues. In this study, we examined the consequences of transglutaminase-mediated galectin-3 oligomerization on the interactions between cancer cells and laminin. We first demonstrated that human galectin-3 is cross-linked by guinea pig liver transglutaminase, forms oligomers, and incorporates the marker 5-(biotinamido) pentylamine. Expression of transglutaminase activity in the A375 and A2058 human melanoma cell extracts was revealed by its ability to induce galectin-3 oligomerization and 5-(biotinamido) pentylamine incorporation. Transglutaminase-treated galectin-3 did not affect adhesion or migration of the melanoma cells to laminin but consistently induced a significant increase of the percentage of cell spreading compared to the control (23.5 +/- 2.3%, vs. 10.6 +/- 1.9% at 180 min, p < 0.05), or to untreated galectin-3 or transglutaminase alone. Our study is the first demonstration that human galectin-3 is oligomerized by transglutaminase with, as a consequence, a specific effect of melanoma cell spreading on laminin. This phenomenon could be of significance in the modulation of cancer cell interactions with laminin during tumor invasion and metastasis.</p>","PeriodicalId":79325,"journal":{"name":"Cell adhesion and communication","volume":"5 6","pages":"425-35"},"PeriodicalIF":0.0,"publicationDate":"1998-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"20703512","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":"Studying receptor-mediated cell adhesion at the single molecule level.","authors":"A Pierres,&nbsp;A M Benoliel,&nbsp;P Bongrand","doi":"10.3109/15419069809010783","DOIUrl":"https://doi.org/10.3109/15419069809010783","url":null,"abstract":"<p><p>Cell adhesion is essentially mediated by specific interactions between membrane receptors and ligands. It is now apparent that the mere knowledge of the on- and off-rate of association of soluble forms of these receptors and ligands is not sufficient to yield accurate prediction of cell adhesive behavior. During the last few years, a variety of complementary techniques relying on the use of hydrodynamic flow, atomic force microscopy, surface forces apparatus or soft vesicles yielded accurate information on i) the dependence of the lifetime of individual bonds on applied forces and ii) the distance dependence of the association rate of bound receptors and ligands. The purpose of this review is, first to recall the physical significance of these parameters, and second to describe newly obtained results. It is emphasized that molecular size and flexibility may be a major determinant of the efficiency of receptor mediated adhesion, and this cannot be studied by conventional methods dealing with soluble molecules.</p>","PeriodicalId":79325,"journal":{"name":"Cell adhesion and communication","volume":"5 5","pages":"375-95"},"PeriodicalIF":0.0,"publicationDate":"1998-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/15419069809010783","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"20701646","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":"Eosinophil accumulation in rat uterus following estradiol administration is modulated by laminin and its integrin receptors.","authors":"M L Katayama,&nbsp;M H Federico,&nbsp;R R Brentani,&nbsp;M M Brentani","doi":"10.3109/15419069809010785","DOIUrl":"https://doi.org/10.3109/15419069809010785","url":null,"abstract":"<p><p>Eosinophils accumulate into the uterus of ovariectomized rats, after treatment with estradiol (E2). We have investigated whether this feature is related to interactions of eosinophils with uterine extracellular matrix proteins: laminin (LM) and fibronectin (FN). Eosinophils isolated from the peritoneal cavity of ovariectomized rats displayed estrogen receptors measured at both binding activity and mRNA levels. An increased number of laminin binding sites, calculated by Scatchard analysis using iodinated LM was determined in E2-treated eosinophils (70,100 +/- 28,000 sites/cell vs 21,000 +/- 5,000 sites/cell in controls). Eo binding to 125I-LM- was inhibited by the E8-LM fragment. Estradiol up-regulated the expression in eosinophils of alpha 6 and beta 2 integrin subunits evaluated by flow-cytometry as well as by alpha 6 mRNA expression. After E2 treatment, eosinophils showed higher adhesiveness to LM-coated dishes (10 +/- 2 vs 56 +/- 3%) which was inhibited by monoclonal antibodies against alpha 6, beta 1 and beta 2 integrins and by the steroid antagonist tamoxifen. These monoclonal antibodies also blocked the attachment of stimulated eosinophils to uterine cryostat sections obtained from spayed rats previously treated with estradiol. We did not detect any apparent influence of E2 on basal eosinophil adherence or binding to FN although alpha 4 and alpha 5 integrin subunits were expressed in eosinophils. Expression of laminin and merosin in the uterus was determined immunohistochemically. Our results suggest that integrin-laminin interactions may contribute to the preferential eosinophil recruitment in vivo.</p>","PeriodicalId":79325,"journal":{"name":"Cell adhesion and communication","volume":"5 5","pages":"409-24"},"PeriodicalIF":0.0,"publicationDate":"1998-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/15419069809010785","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"20701648","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":"Dual control by divalent cations and mitogenic cytokines of alpha 4 beta 1 and alpha 5 beta 1 integrin avidity expressed by human hemopoietic cells.","authors":"Y Takamatsu,&nbsp;P J Simmons,&nbsp;J P Lévesque","doi":"10.3109/15419069809010781","DOIUrl":"https://doi.org/10.3109/15419069809010781","url":null,"abstract":"<p><p>Beta-1 integrins have essential functions in hemopoietic and immune systems by controlling phenomenons such as cell homing and cell activation. The function alpha 4 beta 1 and alpha 5 beta 1 integrins is regulated by divalent cations and, as demonstrated more recently, by mitogenic cytokines which activate them by \"inside-out\" mechanisms. Using the adhesive interaction of a cytokine-dependent human hemopoietic cell line to immobilized fibronectin, we have analyzed the requirements in divalent cations Mn2+, Mg2+ and Ca2+ for alpha 4 beta 1 and alpha 5 beta 1 activation by \"inside-out\" mechanisms triggered by cytokines such as granulocyte-macrophage colony stimulating factor or KIT ligand, or by external conformational constraints with the function-activating anti-beta 1 integrin monoclonal antibody 8A2. The intrinsic difference between these two modes of beta 1 integrin activation was revealed by their different requirements in divalent cations. We found that in the absence of any divalent cations, alpha 4 beta 1 and alpha 5 beta 1 were non-functional even after further stimulation by cytokines or 8A2. However, whilst either Ca2+, Mg2+ or Mn2+ were able to restore adhesive functions of alpha 4 beta 1 and alpha 5 beta 1 when activated by 8A2, only Mg2+ and Mn2+ were able to support activation of alpha 4 beta 1 and alpha 5 beta 1 by cytokines. Furthermore, high concentrations of Ca2+ exceeding 20 mM dramatically inhibited cell adhesion to fibronectin induced by Mn2+ and cytokines but not by 8A2. On the contrary, in the presence of both Ca2+ and Mg2+, Mn2+ had an additive effect on the activation of alpha 4 beta 1 and alpha 5 beta 1 by mitogenic cytokines. The presence of the absence of these divalent cations did not inhibit early tyrosine phosphorylation induced by the binding of KIT ligand to its tyrosine-kinase receptor KIT. Therefore, we propose that in hemopoietic cells, Ca2+, Mg2+ and Mn2+ may modulate in vivo alpha 4 beta 1 and alpha 5 beta 1 regulation by mitogenic cytokines, a phenomenon involved in the regulation of hemopoietic progenitor cell homing within the bone marrow.</p>","PeriodicalId":79325,"journal":{"name":"Cell adhesion and communication","volume":"5 5","pages":"349-66"},"PeriodicalIF":0.0,"publicationDate":"1998-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/15419069809010781","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"20701644","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 membrane proximal region of the integrin beta cytoplasmic domain can mediate oligomerization.","authors":"P E Zage,&nbsp;E E Marcantonio","doi":"10.3109/15419069809010780","DOIUrl":"https://doi.org/10.3109/15419069809010780","url":null,"abstract":"<p><p>Integrin-ligand binding generates many intracellular signals, including signals to initiate focal contact formation and to regulate cellular decisions concerning growth and differentiation. Oligomerization of the beta subunit cytoplasmic domain appears to be required for many of these events. In order to study these processes, we have generated a novel chimeric protein, consisting of the chicken integrin beta 1 cytoplasmic domain connected to the central rod domain of a neuronal intermediate filament, alpha-internexin. This chimeric protein, when expressed transiently in 293T cells, oligomerizes in a beta cytoplasmic domain-dependent manner. This oligomerization requires the membrane proximal amino acids LLMII of the beta 1 cytoplasmic domain, as demonstrated by deletion analysis. Therefore, the integrin beta cytoplasmic domain in this system contains an oligomerization function, which may provide some insight as to the function of intact integrins in vivo.</p>","PeriodicalId":79325,"journal":{"name":"Cell adhesion and communication","volume":"5 5","pages":"335-47"},"PeriodicalIF":0.0,"publicationDate":"1998-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/15419069809010780","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"20702350","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}