Cell adhesion and communication最新文献_第4页

Bau, a splice form of Neurabin-I that interacts with the tumor suppressor Bin1, inhibits malignant cell transformation. Bau是neurabin - 1的一种剪接形式，与肿瘤抑制因子Bin1相互作用，抑制恶性细胞转化。

Cell adhesion and communication Pub Date : 1999-01-01 DOI: 10.3109/15419069909034394

J Duhadaway, F Rowe, K Elliott, N C Mao, G C Prendergast

{"title":"Bau, a splice form of Neurabin-I that interacts with the tumor suppressor Bin1, inhibits malignant cell transformation.","authors":"J Duhadaway, F Rowe, K Elliott, N C Mao, G C Prendergast","doi":"10.3109/15419069909034394","DOIUrl":"https://doi.org/10.3109/15419069909034394","url":null,"abstract":"Bin1 is a nucleocytoplasmic adaptor protein and tumor suppressor. A novel protein termed Bau was identified through its ability to interact with a region of Bin1 required to inhibit malignant cell transformation by certain oncogenes. Bau is a splice form of Neurabin-I, one of two related F-actin-binding proteins that are proposed to link cadherin-based cell-cell adhesion sites with the growth regulatory kinase p70S6K. Bau lacks actin- and p70S6K-binding domains found in Neurabin-I but includes coiled-coil domains that are part of its central domain as well as additional sequences not found in Neurabin-I. Interaction with Bin1 requires the presence of the U3 region which is alternately spliced in muscle cells. Bau localizes to the nucleus and cytosol. Like Bin1, Bau can suppress oncogene-mediated transformation and inhibit tumor cell growth. We suggest that Bau may link Bin1 to the Neurabin-I/p70S6K system in muscle and other cells, perhaps providing a mechanism to influence adhesion-dependent signals which affect cell fate.","PeriodicalId":79325,"journal":{"name":"Cell adhesion and communication","volume":"7 2","pages":"99-110"},"PeriodicalIF":0.0,"publicationDate":"1999-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/15419069909034394","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"21293187","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}

引用次数: 5

Involvement of desmoplakin phosphorylation in the regulation of desmosomes by protein kinase C, in HeLa cells. 在HeLa细胞中，蛋白激酶C参与桥粒磷酸化的调节。

Cell adhesion and communication Pub Date : 1999-01-01 DOI: 10.3109/15419069909034396

L S Amar, A H Shabana, M Oboeuf, N Martin, N Forest

{"title":"Involvement of desmoplakin phosphorylation in the regulation of desmosomes by protein kinase C, in HeLa cells.","authors":"L S Amar, A H Shabana, M Oboeuf, N Martin, N Forest","doi":"10.3109/15419069909034396","DOIUrl":"https://doi.org/10.3109/15419069909034396","url":null,"abstract":"In the present study, we have examined how modulation of protein kinase C (PKC) activity affected desmosome organization in HeLa cells. Immunofluorescence and electron microscopy showed that PKC activation upon short exposure to 12-O-tetradecanoylphorbol 13-acetate (TPA) resulted in a reduction of intercellular contacts, splitting of desmosomes and dislocation of desmosomal components from the cell periphery towards the cytoplasm. As determined by immunoblot analysis of Triton X-100-soluble and -insoluble pools of proteins, these morphological changes were not correlated with modifications in the extractability of both desmoglein and plakoglobin, but involved almost complete solubilization of the desmosomal plaque protein, desmoplakin. Immunoprecipitation experiments and immunoblotting with anti-phosphoserine, antiphosphothreonine and anti-phosphotyrosine antibodies revealed that desmoplakin was mainly phosphorylated on serine and tyrosine residues in both treated and untreated cells. While phosphotyrosine content was not affected by PKC activation, phosphorylation on serine residues was increased by about two-fold. This enhanced serine phosphorylation coincided with the increase in the protein solubility, suggesting that phosphorylation of desmoplakin may be a mechanism by which PKC mediates desmosome disassembly. Consistent with the loss of PKC activity, we also showed that down-modulation of the kinase (in response to prolonged TPA treatment) or its specific inhibition (by GF 109203X) had opposite effects and increased desmosome formation. Taken together, these results clearly demonstrate an important role for PKC in the regulation ofdesmosomal junctions in HeLa cells, and identify serine phosphorylation of desmoplakin as a crucial event in this pathway.","PeriodicalId":79325,"journal":{"name":"Cell adhesion and communication","volume":"7 2","pages":"125-38"},"PeriodicalIF":0.0,"publicationDate":"1999-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/15419069909034396","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"21293189","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}

引用次数: 26

ICAM-3 (CD50) is expressed by human mast cells: induction of homotypic mast cell aggregation via ICAM-3. ICAM-3 (CD50)在人肥大细胞中表达:通过ICAM-3诱导同型肥大细胞聚集。

Cell adhesion and communication Pub Date : 1999-01-01 DOI: 10.3109/15419069909010802

M Babina, K Mammeri, B M Henz

{"title":"ICAM-3 (CD50) is expressed by human mast cells: induction of homotypic mast cell aggregation via ICAM-3.","authors":"M Babina, K Mammeri, B M Henz","doi":"10.3109/15419069909010802","DOIUrl":"https://doi.org/10.3109/15419069909010802","url":null,"abstract":"Intercellular adhesion molecule-3 (ICAM-3, CD50), an adhesion receptor of the immunoglobulin superfamily, is suggested to play a key role in adhesive cellular interactions during the initial phase of an immune response. We here provide evidence that ICAM-3 is abundantly expressed by cells of the human mast cell line HMC-1 and, to a lower degree, by purified skin mast cells, as demonstrated by flow-cytometry, ELISA and RT-PCR. ICAM-3 immunoprecipitated from surface biotinylated HMC-1 cells migrates as a broad band of Mr 124,000 by Western blot analysis. We also demonstrate that monoclonal antibodies directed against ICAM-3 are capable of inducing rapid HMC-1 cell aggregation, the extent of which strongly depends on the epitope recognized by the mAb applied. Interestingly, although inhibitable by two of six mAbs against LFA-1, HMC-1 aggregation induced via ICAM-3 appears to be mediated by an adhesive pathway independent of LFA-1. Dermal mast cells are also aggregated with anti-ICAM-3 mAbs, a phenomenon which has not been described before for isolated tissue mast cells. However, this process displays slower kinetics, as compared to HMC-1 cells. That anti-ICAM-3 mAbs are able to mediate biological effects is further illustrated by their capability to increase stimulation-dependent release of the pro-inflammatory cytokines interleukin-6 (IL-6) and IL-8 from HMC-1 cells. Taken together, these results indicate that ICAM-3 is not only expressed by immature and mature human mast cells, but also possesses functional relevance and may therefore play a significant role in mast cell associated processes.","PeriodicalId":79325,"journal":{"name":"Cell adhesion and communication","volume":"7 3","pages":"195-209"},"PeriodicalIF":0.0,"publicationDate":"1999-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/15419069909010802","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"21482171","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}

引用次数: 7

Transforming growth factor-beta 1 increases the adhesion of MDA-MB-231 mammary adenocarcinoma cells to the microvascular subendothelium. 转化生长因子- β 1增加MDA-MB-231乳腺腺癌细胞对微血管内皮下层的粘附。

Cell adhesion and communication Pub Date : 1999-01-01 DOI: 10.3109/15419069909034392

L D Loganadane, J Vassy, C Legrand, F Fauvel-Lafeve

{"title":"Transforming growth factor-beta 1 increases the adhesion of MDA-MB-231 mammary adenocarcinoma cells to the microvascular subendothelium.","authors":"L D Loganadane, J Vassy, C Legrand, F Fauvel-Lafeve","doi":"10.3109/15419069909034392","DOIUrl":"https://doi.org/10.3109/15419069909034392","url":null,"abstract":"The increase of tumor cell adhesion to the subendothelium in the presence of TGF-beta 1 is thought to be mediated by two major events: an enrichment of extracellular matrix proteins secreted by endothelial cells and an increase of the integrins on the surface of tumor cells. In this study, we analyzed the effect of TGF-beta 1 on the adhesion of a mammary adenocarcinoma cell line (MDA-MB-231) to the matrix of human microvascular endothelial cells (HMEC-1). The adhesion of TGF-beta 1-treated tumor cells to a non-treated matrix or to purified matrix proteins was enhanced, while no increase was observed when non-treated tumor cells were let to adhere to a matrix secreted by HMEC-1 in the presence of the cytokine. Thus, the increase of cell adhesion was due to the effect of TGF-beta 1 on tumor cells and not to the matrix enrichment induced by this cytokine. The hyper-adhesion was inhibited by the RGD peptide and EDTA indicating that integrins were involved. Integrin subunits concentrations (alpha 5, alpha v and beta 1) on the surface of TGF-beta 1-treated tumor cells were not modified, while confocal microscopy showed a reorganization of beta 1 integrin subunits on the cell surface and in the cytoplasm resulting in actin fibers reorganization in the cytoskeleton. This indicates that the enhanced adhesion of TGF-beta 1-treated MDA-MB-231 cells to the subendothelium is due to a qualitative change of integrins.","PeriodicalId":79325,"journal":{"name":"Cell adhesion and communication","volume":"7 1","pages":"57-71"},"PeriodicalIF":0.0,"publicationDate":"1999-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/15419069909034392","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"21099282","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}

引用次数: 7

Keratinocyte growth factor (KGF) promotes keratinocyte cell attachment and migration on collagen and fibronectin. 角化细胞生长因子(KGF)促进角化细胞在胶原和纤维连接蛋白上的附着和迁移。

Cell adhesion and communication Pub Date : 1999-01-01 DOI: 10.3109/15419069909010803

E E Putnins, J D Firth, A Lohachitranont, V J Uitto, H Larjava

{"title":"Keratinocyte growth factor (KGF) promotes keratinocyte cell attachment and migration on collagen and fibronectin.","authors":"E E Putnins, J D Firth, A Lohachitranont, V J Uitto, H Larjava","doi":"10.3109/15419069909010803","DOIUrl":"https://doi.org/10.3109/15419069909010803","url":null,"abstract":"Keratinocyte growth factor (KGF) induction of keratinocyte attachment and migration on provisional and basement membrane proteins was examined. KGF-treated keratinocytes showed increased attachment to collagen types I and IV and fibronectin, but, not to laminin-1, vitronectin, or tenascin. This increase was time- and dose-dependent. Increase in attachment occurred with 2 10 microg/ml of ECM proteins. This KGF-stimulated cell attachment was beta1 integrin-dependent but was not associated with stimulation of the cell surface expression nor affinity (activity) of the collagen integrin receptor (alpha2beta1) nor the fibronectin integrin receptors (alpha5beta1 or alphav). At the basal layer of KGF-treated cells significant accumulation of beta1 integrins was found at the leading edges, and actin stress fibers colocalized with beta1. KGF also induced migratory phenotype and stimulated keratinocyte migration on both fibronectin and collagen types I and IV but not on laminin-1, vitronectin nor tenascin. The results suggest that in addition to its proliferation promoting activity. KGF is able to modulate keratinocyte adhesion and migration on collagen and fibronectin. Our data suggest that KGF induced integrin avidity (clustering), a signaling event, which is not dependent on the alteration of cell surface integrin numbers.","PeriodicalId":79325,"journal":{"name":"Cell adhesion and communication","volume":"7 3","pages":"211-21"},"PeriodicalIF":0.0,"publicationDate":"1999-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/15419069909010803","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"21485254","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}

引用次数: 55

Mutational analysis of MAdCAM-1/alpha4beta7 interactions reveals significant binding determinants in both the first and second immunuglobulin domains. MAdCAM-1/alpha4beta7相互作用的突变分析揭示了第一和第二免疫球蛋白结构域的重要结合决定因素。

Cell adhesion and communication Pub Date : 1999-01-01 DOI: 10.3109/15419069909010800

N Green, J Rosebrook, N Cochran, K Tan, J H Wang, T A Springer, M J Briskin

{"title":"Mutational analysis of MAdCAM-1/alpha4beta7 interactions reveals significant binding determinants in both the first and second immunuglobulin domains.","authors":"N Green, J Rosebrook, N Cochran, K Tan, J H Wang, T A Springer, M J Briskin","doi":"10.3109/15419069909010800","DOIUrl":"https://doi.org/10.3109/15419069909010800","url":null,"abstract":"The selective emigration of blood born leukocytes into tissues is mediated, in part by interactions of Ig-like cell adhesion molecules (IgCAMs) expressed on vascular endothelium and their cognate ligands, the leukocyte integrins. Within mucosal lymphoid tissues and gastrointestinal sites the mucosal vascular addressin. MAdCAM-1 is the predominant IgCAM, mediating specific lymphocyte homing via interactions with its ligand on lymphocytes, the integrin alpha4beta7. Previous studies have shown that an essential binding motif resides in the first Ig domain of all IgCAMs, containing an acidic residue (D or E) preceded by an aliphatic residue (L or I) that resides in strand C or the CD loop. However, domain swap experiments with MAdCAM-1 and VCAM-1 have shown a requirement for both Ig domains 1 and 2 for efficient integrin binding. We describe the use of chimeric MAdCAM-1/VCAM-1 receptors and point mutations in MAdCAM-1 to define other sites that are required for binding to the integrin alpha4beta7. We find that, in addition to critical CD loop residues, other regions in both domain one and two contribute to MAdCAM-1/alpha4beta7 interactions, including a buried arginine residue in the F strand of domain one and several acidic residues in a highly extended DE ribbon in domain 2. These mutations, when placed in the recently solved crystal structure of human MAdCAM-1 give insight into the integrin binding preference of this unique receptor.","PeriodicalId":79325,"journal":{"name":"Cell adhesion and communication","volume":"7 3","pages":"167-81"},"PeriodicalIF":0.0,"publicationDate":"1999-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/15419069909010800","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"21482169","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}

引用次数: 14

Cellular localization of alpha3beta1 integrin isoforms in association with myofibrillogenesis during cardiac myocyte development in culture. 在培养心肌细胞发育过程中，与肌原纤维形成相关的alpha3beta1整合素亚型的细胞定位。

Cell adhesion and communication Pub Date : 1999-01-01 DOI: 10.3109/15419069909034393

Y Y Kim, C S Lim, Y H Song, J Ahnn, D Park, W K Song

{"title":"Cellular localization of alpha3beta1 integrin isoforms in association with myofibrillogenesis during cardiac myocyte development in culture.","authors":"Y Y Kim, C S Lim, Y H Song, J Ahnn, D Park, W K Song","doi":"10.3109/15419069909034393","DOIUrl":"https://doi.org/10.3109/15419069909034393","url":null,"abstract":"The cellular localization of alpha3beta1 integrin isoforms was examined in cultured neonatal myocytes at selected times during development using double immunofluorescence assays. The distribution of alpha3A subunits began as diffuse and patternless, but as the cells matured, the distribution assumed a sarcomeric banding pattern, and alpha3A appeared to be localized in costameres - sarcolemmal regions adjacent to the Z-disks. Alpha-actinin, a component of the Z-disk, was localized in the same intracellular regions. Temporal analysis of the incorporation of the alpha3A subunit and other myofibrillar proteins into sarcomeres revealed that alpha3A was integrated into sarcomeres following incorporation of alpha-actinin and myosin heavy chain (MHC) but prior to that of desmin. This suggests that alpha3A integrins are incorporated into a pre-existing myofibrillar structure, and it is unlikely that alpha3A integrins participate in the initial assembly of myofibrillar proteins. The alpha3B, beta1A and beta1D subunits were also localized in costameres, where they formed alpha3Abeta1A, alpha3Abeta1D and alpha3Bbeta1A heterodimers. The alpha3Bbeta1D heterodimer, however, was not found in cardiac myocytes. The antisera raised against the cytoplasmic domains of alpha3A, alpha3B, beta1A and beta1D caused disruption of sarcomere structure. Thus, the myofibril-extracellular matrix linkages mediated by isoforms of alpha3beta1 integrin may play a crucial role in the stabilization of myofibril assembly and in the maintenance of sarcomere structure. Co-immunoprecipitation experiments revealed that beta1A, but not beta1D, interacts with the Nck signaling protein, suggesting that Nck participates in downstream signaling triggered by beta1A and that the beta1A-mediated signaling pathway is distinct from that of beta1D.","PeriodicalId":79325,"journal":{"name":"Cell adhesion and communication","volume":"7 2","pages":"85-97"},"PeriodicalIF":0.0,"publicationDate":"1999-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/15419069909034393","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"21293186","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}

引用次数: 16

Role of carbohydrate structures in CEA-mediated intercellular adhesion. 碳水化合物结构在cea介导的细胞间粘附中的作用。

Cell adhesion and communication Pub Date : 1999-01-01 DOI: 10.3109/15419069909010805

J Charbonneau, C P Stanners

{"title":"Role of carbohydrate structures in CEA-mediated intercellular adhesion.","authors":"J Charbonneau, C P Stanners","doi":"10.3109/15419069909010805","DOIUrl":"https://doi.org/10.3109/15419069909010805","url":null,"abstract":"Human carcinoembryonic antigen (CEA) is a member of a family of cell surface glycoproteins representing a subset of the immunoglobulin superfamily and is a major tumor marker. CEA has been demonstrated to function in vitro, at least, as a homotypic intercellular adhesion molecule. CEA can also inhibit the differentiation of several different cell types and contribute to tumorigenesis, an activity that requires CEA-CEA interactions. Post-translational modifications that could modulate CEA-CEA binding are therefore of interest. CEA is heavily glycosylated with 28 consensus sites for the addition of asparagine-linked carbohydrate structures, leading to a molecule with a bottle brush-like structure. In order to modulate the glycosylation of CEA, we transfected the functional cDNA of CEA into Chinese hamster ovary (CHO) mutant cells, Lec1, Lec2, and Lec8, which are deficient in enzymes responsible for various steps in the glycosylation processing pathway. Aggregation assays of cells in suspension were performed with stable CEA transfectants of these cell lines and showed that all of the aberrant CEA glycoforms could still mediate adhesion. In addition, the specificity of adhesion of these glycoforms was unchanged, as shown by homotypic and heterotypic adhesion assays between the transfectants. Lec1 and Lec2 transfectants did, however, show an increased speed and final extent of aggregation, which is consistent with models in which sugar structures interfere with binding through protein domains. Lec8 transfectants, on the other hand, with more truncated sugar structures than Lec2, showed less aggregation than wild type (WT) transfectants. We therefore conclude that carbohydrates do not determine the adhesion property of CEA or its specificity, in spite of the unusually high degree of glycosylation; they do, however, modulate the strength of adhesion.","PeriodicalId":79325,"journal":{"name":"Cell adhesion and communication","volume":"7 3","pages":"233-44"},"PeriodicalIF":0.0,"publicationDate":"1999-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/15419069909010805","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"21485256","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}

引用次数: 15

Different integrins mediate cell spreading, haptotaxis and lateral migration of HaCaT keratinocytes on fibronectin. 不同的整合素介导HaCaT角化细胞在纤维连接蛋白上的细胞扩散、趋向性和横向迁移。

Cell adhesion and communication Pub Date : 1999-01-01 DOI: 10.3109/15419069909010806

L Koivisto, K Larjava, L Häkkinen, V J Uitto, J Heino, H Larjava

{"title":"Different integrins mediate cell spreading, haptotaxis and lateral migration of HaCaT keratinocytes on fibronectin.","authors":"L Koivisto, K Larjava, L Häkkinen, V J Uitto, J Heino, H Larjava","doi":"10.3109/15419069909010806","DOIUrl":"https://doi.org/10.3109/15419069909010806","url":null,"abstract":"Collaborative role of various fibronectin-binding integrins (alpha5beta1, alphavbeta1 and alphavbeta6) as mediators of cell adhesion and migration on fibronectin was studied using cultured HaCaT keratinocytes. This cell line spontaneously expressed all three fibronectin-binding integrins. In addition, the expression of alphavbeta6 integrin was strongly and specifically upregulated by transforming growth factor-beta1 (TGFbeta1) whereas the amount of other integrins remained practically unchanged on the cell surface. Adhesion, spreading and motility of HaCaT keratinocytes on fibronectin were promoted by TGFbeta1. Based on antibody blocking experiments, both untreated and TGFbeta1-treated HaCaT cells used alphavbeta6 integrin as their main fibronectin receptor for cell spreading. In contrast to TGFbeta1-treated cells, the untreated cells also needed alpha5beta1 integrin for maximal cell spreading on fibronectin. Combinations of antibodies blocking both of these receptors totally prevented spreading of both untreated and TGFbeta1-treated cells. Haptotactic motility of individual HaCaT cells through fibronectin-coated membranes was again mainly dependent on alphavbeta6 integrin, while alphavbeta1 and alpha5beta1 integrins played a lesser role both in untreated and TGFbeta1-treated HaCaT cells. However, unlike haptotaxis, lateral migration of HaCaT cell sheet was mainly mediated by beta1 integrins, and alphavbeta6 integrin showed a minor role. The migration process appeared to involve a number of beta1 integrins that could adaptively replace each other when blocking antibodies were present. Thus, keratinocytes appear to use different fibronectin receptors for different functions, such as cell spreading, haptotaxis and lateral migration. The cells can also adapt to a situation where one receptor is unfunctional by switching to another receptor of the same ligand.","PeriodicalId":79325,"journal":{"name":"Cell adhesion and communication","volume":"7 3","pages":"245-57"},"PeriodicalIF":0.0,"publicationDate":"1999-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/15419069909010806","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"21485257","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}

引用次数: 77

Low affinity binding of an LFA-3/IgG1 fusion protein to CD2+ T cells is independent of cell activation. LFA-3/IgG1融合蛋白与CD2+ T细胞的低亲和力结合不依赖于细胞活化。

Cell adhesion and communication Pub Date : 1999-01-01 DOI: 10.3109/15419069909010808

G R Majeau, A Whitty, K Yim, W Meier, P S Hochman

{"title":"Low affinity binding of an LFA-3/IgG1 fusion protein to CD2+ T cells is independent of cell activation.","authors":"G R Majeau, A Whitty, K Yim, W Meier, P S Hochman","doi":"10.3109/15419069909010808","DOIUrl":"https://doi.org/10.3109/15419069909010808","url":null,"abstract":"Quantitative analysis of binding of the bivalent recombinant soluble fusion protein, LFA-3/IgG1, shows that the fusion protein binds to human CD2+ PBLs primarily through low affinity (KD approximately 140 microM) but also through high avidity (90 nM) interactions. The concentration dependence for LFA-3/IgG1 PBL binding took the form of two overlapping bell-shaped curves separated by a clear and reproducible minimum. This was accounted for in part by minor heterogeneity in the LFA-3/IgG1 preparations, and potentially by the ability of the ligand to bind to both CD2 and Fc receptors (FcR), best evidenced by the distinct binding properties of the fusion protein to NK and T cells. The low affinity LFA-3/ IgG1 binding to T cells is consistent with binding to CD2 only, and is in agreement with the low affinity reported for interactions between soluble forms of LFA-3 and CD2 by surface plasmon resonance technology. Moreover, as the low affinity determinations are similar for CD2 on resting and activated T cells, although the CD2 molecule has been reported to be altered to reveal new epitopes upon T cell activation, the binding data argue against multiple cell activation-dependent affinity states of CD2 for LFA-3 binding. This is distinct from that observed with other adhesion partners, and suggests that the different adhesion pathways utilize distinct mechanisms to mediate cell adhesion.","PeriodicalId":79325,"journal":{"name":"Cell adhesion and communication","volume":"7 3","pages":"267-79"},"PeriodicalIF":0.0,"publicationDate":"1999-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/15419069909010808","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"21485259","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}

引用次数: 31