Cell adhesion and communication最新文献_第7页

Binding of the alpha 2 integrin I domain to extracellular matrix ligands: structural and mechanistic differences between collagen and laminin binding. α 2整合素I结构域与细胞外基质配体的结合:胶原和层粘连蛋白结合的结构和机制差异。

Cell adhesion and communication Pub Date : 1998-06-01 DOI: 10.3109/15419069809040297

S K Dickeson, J J Walsh, S A Santoro

{"title":"Binding of the alpha 2 integrin I domain to extracellular matrix ligands: structural and mechanistic differences between collagen and laminin binding.","authors":"S K Dickeson, J J Walsh, S A Santoro","doi":"10.3109/15419069809040297","DOIUrl":"https://doi.org/10.3109/15419069809040297","url":null,"abstract":"The alpha 2 beta 1 integrin functions as a cell surface receptor for collagen on some cells and as both a collagen and laminin receptor on a more restricted subset of cell types including endothelial and epithelial cells. The alpha 2 integrin subunit I domain binds collagen in a divalent cation-dependent manner. In contrast, I domain binding to laminin occurs via both divalent cation-dependent and -independent mechanisms. Saturable binding was observed in the presence of either Mn2+ or EDTA, although the extent of binding in Mn2+ was twice that observed in EDTA. Half-maximal binding occurred at about 22 nM I domain in either case. Whereas laminin binding was significantly enhanced by Mn2+, with half-maximal binding occurring at 1.9 mM Mn2+, Mg2+ was much less effective. Deletion of the N-terminal 35 residues of the I domain, including the DXSXS portion of the MIDAS motif, caused a significant diminution of laminin binding activity. Laminin binding by the I domain was significantly inhibited by the alpha 2 beta 1 function-blocking antibody 6F1 in the presence of either EDTA or Mn2+. The non-function-blocking antibody 12F1 had no effect. In contrast to the binding of the alpha 2 integrin I domain to collagen, the laminin binding activity of the I domain was not enhanced by the addition of the first EF hand motif of the integrin.","PeriodicalId":79325,"journal":{"name":"Cell adhesion and communication","volume":"5 4","pages":"273-81"},"PeriodicalIF":0.0,"publicationDate":"1998-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/15419069809040297","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"20676079","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

A mutation in alpha-catenin disrupts adhesion in clone A cells without perturbing its actin and beta-catenin binding activity. α -连环蛋白的突变会破坏克隆A细胞的粘附，但不会干扰其肌动蛋白和β -连环蛋白的结合活性。

Cell adhesion and communication Pub Date : 1998-06-01 DOI: 10.3109/15419069809040298

S Roe, E R Koslov, D L Rimm

{"title":"A mutation in alpha-catenin disrupts adhesion in clone A cells without perturbing its actin and beta-catenin binding activity.","authors":"S Roe, E R Koslov, D L Rimm","doi":"10.3109/15419069809040298","DOIUrl":"https://doi.org/10.3109/15419069809040298","url":null,"abstract":"Cadherin mediated cell-cell adhesion requires cytoplasmic connections to the cytoskeleton mediated by alpha-catenin. Original descriptions of the catenins, as well as our own in vitro studies, have suggested that this connection was mediated by the interaction of alpha-catenin to actin. Loss of adhesion in the human colon carcinoma cell line \"Clone A\" is the result of an internal deletion mutation of 158 residues near the N-terminus of the protein resulting in an 80 kD mutated protein. Transfection of these cells with the full length protein restores the normal adhesive phenotype. We have characterized this mutant protein in efforts to understand the normal function of alpha-catenin and, in particular, the region deleted in the Clone A mutant. Co-precipitation experiments using whole cell lysates indicate that the mutant form of alpha-catenin binds beta-catenin and plakoglobin, and can form a structural complex with E-cadherin via these interactions. Actin co-sedimentation assays show that the recombinant mutant binds and bundles F-actin and binds both actin and beta-catenin simultaneously, as seen with wild type alpha-catenin. These results suggest that the stabilization of the E-cadherin-catenin complex may be mediated by factors beyond its direct interaction with actin. We conclude that a region near the N-terminus of alpha-catenin mediates additional interactions between the adhesive complex and the cytoskeleton that are critical for functional adhesion.","PeriodicalId":79325,"journal":{"name":"Cell adhesion and communication","volume":"5 4","pages":"283-96"},"PeriodicalIF":0.0,"publicationDate":"1998-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/15419069809040298","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"20676080","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: 18

Localisation of a novel adhesion blocking epitope on the human beta 1 integrin chain. 一个新的粘附阻断表位在人β 1整合素链上的定位。

Cell adhesion and communication Pub Date : 1998-06-01 DOI: 10.3109/15419069809040296

H Ni, J A Wilkins

{"title":"Localisation of a novel adhesion blocking epitope on the human beta 1 integrin chain.","authors":"H Ni, J A Wilkins","doi":"10.3109/15419069809040296","DOIUrl":"https://doi.org/10.3109/15419069809040296","url":null,"abstract":"Members of the beta 1 integrin family mediate cellular adherence to a wide range of extracellular and cell surface associated ligands. Conformational changes have been shown to be associated with integrin activation and ligand binding. Some studies suggest that there may be a restricted region of the beta 1 integrin that serves as the target for regulatory antibodies which can inhibit or stimulate integrin function. Here we identify an inhibitory epitope that is located at a distinct sight from that suggested for other inhibitory antibodies. Three different adhesion blocking antibodies, JB1A, C30B, and D11B bind to a peptide corresponding to residues 82-87 of the mature beta 1 chain. Mn++ inhibited the binding of JB1A to purified beta 1 integrin. In contrast the binding of several other antibodies to beta 1 were not influenced by these conditions. JB1A binding to purified peptide was also inhibited by Mn++ suggesting that it related to interference with the antibody function rather than a cation dependent change in the epitope. Our data 1) directly demonstrates the peptide sequence recognised by three adhesion blocking antibodies to the human beta 1 integrin chain 2) identifies a novel epitope located at residues 82-87, distinct from that of previously described regulatory epitopes 3) characterises a Mn++ sensitive antibody integrin interaction. Collectively, these results indicate the existence of multiple regulatory sites on the beta 1 integrin molecule.","PeriodicalId":79325,"journal":{"name":"Cell adhesion and communication","volume":"5 4","pages":"257-71"},"PeriodicalIF":0.0,"publicationDate":"1998-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/15419069809040296","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"20676078","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: 30

Expression profile of vascular cell adhesion molecule-1 (CD106) in inflammatory foci using rhenium-188 labelled monoclonal antibody in mice. 利用铼-188标记单克隆抗体研究小鼠炎症灶中血管细胞粘附分子-1 (CD106)的表达谱。

Cell adhesion and communication Pub Date : 1998-06-01 DOI: 10.3109/15419069809040301

K J Kairemo, S Strömberg, T K Nikula, S L Karonen

{"title":"Expression profile of vascular cell adhesion molecule-1 (CD106) in inflammatory foci using rhenium-188 labelled monoclonal antibody in mice.","authors":"K J Kairemo, S Strömberg, T K Nikula, S L Karonen","doi":"10.3109/15419069809040301","DOIUrl":"https://doi.org/10.3109/15419069809040301","url":null,"abstract":"Rhenium (Re)-188 is a generator (W-188/Re-188) produced high energy beta-emitter suitable for radionuclide therapy (T1/2 is 16.9 hrs and Emax 2.1 MeV (range 11 mm)). We have labelled monoclonal antibody (MAb) raised against vascular cell adhesion molecule-1 (VCAM-1) with Re-188 using glucoheptonate chelation technique and SnCl2 as reducing agent. The labelling efficiency, free perrhenate and reduced Re were controlled with thin layer chromatography and the purification of Re-188-MoAbs was performed using gel filtration. Our results indicate that Re-188-labelled antibodies remain in vitro stable and the labelling purity is > 90%. We also have applied these Re-188-MoAbs for detection of inflammatory disease in a mouse. The effective half-lives of organs of interest after an injection of Re-188-anti-VCAM1 were as follows: blood 5.2 hr, kidney 4.7 hr, and liver 9.6 hr. Re-188-anti-VCAM-1 was found to accumulate mainly in kidney and liver. One hour after the injection, the kidney contained in average as high as 12.5% and the liver 2.8 ID/g tissue. After 6 hr, the kidney contained 5.5% ID/g and the liver 2.6% ID/g. At 24 hr, the kidney uptake was 0.5% ID/g and the liver uptake 0.8% ID/g, respectively. The inflamed foci, subcutaneous lesions in the footpad skin, were visualized using gamma camera. From the distribution data the uptakes in the inflamed foci as follows: at 1 hr 2.18 (inflammation) and 1.72% ID/g (control), at 6 hr 1.42 (inflammation) and 0.85% ID/g (control), and at 24 hr 0.17 (inflammation) and 0.084% ID/g (control), respectively. Anti-VCAM-1 MAb showed better targeting as compared to control MoAbs in inflammation (caused by E.coli lipoplysaccaride). In conclusion, Re-188 is suitable for MAb labelling, and MAb against VCAM-1 may be used for detection of local inflammatory disease.","PeriodicalId":79325,"journal":{"name":"Cell adhesion and communication","volume":"5 4","pages":"325-33"},"PeriodicalIF":0.0,"publicationDate":"1998-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/15419069809040301","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"20675374","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: 3

Protein phosphatase 1 delta is associated with focal adhesions. 蛋白磷酸酶1 δ与局灶性粘连有关。

Cell adhesion and communication Pub Date : 1998-06-01 DOI: 10.3109/15419069809040299

E Villa-Moruzzi, M Tognarini, G Cecchini, P C Marchisio

{"title":"Protein phosphatase 1 delta is associated with focal adhesions.","authors":"E Villa-Moruzzi, M Tognarini, G Cecchini, P C Marchisio","doi":"10.3109/15419069809040299","DOIUrl":"10.3109/15419069809040299","url":null,"abstract":"In all mammalian cells protein phosphatase-1 (PP1) exists in three isoforms, defined as alpha, gamma 1 and delta. Immunofluorescence studies with isoform-specific antibodies indicated that delta, but not alpha or gamma 1, is enriched at focal adhesions in HeLa cells, fibroblasts, endothelial cells and keratinocytes. This was confirmed also by interference reflection microscopy, which indicated that PP1 delta was in areas of tight adhesion of the membrane to the extracellular matrix at sites where the microfilament cytoskeleton is organized. In all the cell types so far considered the PP1 delta in focal adhesions represented only a small aliquot of the total PP1 delta, which was predominantly localized to the nucleus. The association of PP1 delta to focal adhesions was confirmed by the co-immunoprecipitation of PP1 delta with the focal adhesion kinase pp125FAK and with the alpha v integrin. Comparison between the amount of PP1 delta associated with focal adhesion proteins and that of PP1 delta recovered in an anti-PP1 delta immunoprecipitate confirmed that only a minor amount of the enzyme was associated with the focal adhesions. Since some focal adhesion proteins are phosphorylated on Ser/Thr, it is likely that PP1 delta may be involved in the regulation of focal adhesion functions and particularly in the signaling pathway generated by cell-substratum adhesion.","PeriodicalId":79325,"journal":{"name":"Cell adhesion and communication","volume":"5 4","pages":"297-305"},"PeriodicalIF":0.0,"publicationDate":"1998-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"20676081","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: 0

Calcium-induced intercellular adhesion of keratinocytes does not involve accumulation of beta 1 integrins at cell-cell contacts and does not involve changes in the levels or phosphorylation of catenins. 钙诱导的角质形成细胞的细胞间粘附不涉及细胞间接触处β 1整合素的积累，也不涉及连环蛋白水平或磷酸化的变化。

Cell adhesion and communication Pub Date : 1998-03-01 DOI: 10.3109/15419069809040287

V M Braga, N Hajibagheri, F M Watt

{"title":"Calcium-induced intercellular adhesion of keratinocytes does not involve accumulation of beta 1 integrins at cell-cell contacts and does not involve changes in the levels or phosphorylation of catenins.","authors":"V M Braga, N Hajibagheri, F M Watt","doi":"10.3109/15419069809040287","DOIUrl":"https://doi.org/10.3109/15419069809040287","url":null,"abstract":"On initiation of terminal differentiation human epidermal keratinocytes detach from the underlying basement membrane as a result of inactivation and subsequent loss of integrins from the cell surface. Assembly of keratinocytes into multilayered sheets requires functional E- and P-cadherin and when stratification is inhibited in low calcium medium differentiating keratinocytes continue to express functional integrins. Using immunofluorescence microscopy, we found that on addition of calcium ions to keratinocyte monolayers there was colocalisation of the beta 1 integrins and E-cadherin along the lateral membranes except for a zone close to the substratum which exclusively contained integrins. Quantitative immunoelectron microscopy showed that on induction of stable cell-cell contacts the density of beta 1 integrins was the same on the apical and lateral membranes, suggesting that the accumulation of integrins on the lateral membranes observed by immunofluorescence microscopy is due to the increased area of contact between adjacent cells and not to an increase in receptor density. There were no changes in the levels of catenins and their degree of phosphorylation after induction of cell-cell contacts. These observations provide new sights into the mechanism of calcium-dependent intercellular adhesion of keratinocytes.","PeriodicalId":79325,"journal":{"name":"Cell adhesion and communication","volume":"5 2","pages":"137-49"},"PeriodicalIF":0.0,"publicationDate":"1998-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/15419069809040287","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"20556554","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: 21

The apical lamina and its role in cell adhesion in sea urchin embryos. 海胆胚顶层及其在细胞粘附中的作用。

Cell adhesion and communication Pub Date : 1998-03-01 DOI: 10.3109/15419069809040284

R D Burke, M Lail, Y Nakajima

{"title":"The apical lamina and its role in cell adhesion in sea urchin embryos.","authors":"R D Burke, M Lail, Y Nakajima","doi":"10.3109/15419069809040284","DOIUrl":"https://doi.org/10.3109/15419069809040284","url":null,"abstract":"The hyaline layer (HL) is an extracellular matrix surrounding sea urchin embryos which has been implicated in a cell adhesion and morphogenesis. The apical lamina (AL) is a fibrous meshwork that remains after removal of hyalin from the HL and the fibropellins (FP) are glycoproteins thought to be the principal components of the AL. Using anti-FP antibodies (AL-1 and AL-2) we report immunoprecipitations and affinity purifications yield a high molecular weight complex comprised of the FP glycoproteins. The three components form a complex, stabilized by disulphide cross-linking and have stochiometric ratios of 2 FPIa molecules to 1 each of FPIb and FPIII. Pulse chase experiments indicate all 3 FP's are synthesized throughout development with peaks in synthesis during cleavage and a sustained peak beginning at hatching. Using immunogold and immunoperoxidase localization, the FP localize to a fibrillar complex forming the innermost layer of the HL. In cell adhesion experiments, cells adhere to affinity purified FP in a temperature, time and concentration dependent manner. Cell adhesion to Fp is about 70% of that seen when hyalin is used as a substrate. Pretreating with AL-1 and AL-2 reduces in vitro cell adhesion by about 65%. We conclude FP's form a fibrillar complex, which is synthesized throughout early development and functions, with other components of the HL, as a substrate for cell adhesion.","PeriodicalId":79325,"journal":{"name":"Cell adhesion and communication","volume":"5 2","pages":"97-108"},"PeriodicalIF":0.0,"publicationDate":"1998-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/15419069809040284","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"20556612","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: 24

Adhesion of cultured human kidney mesangial cells to native entactin: role of integrin receptors. 培养的人肾系膜细胞与天然紧动蛋白的粘附:整合素受体的作用。

Cell adhesion and communication Pub Date : 1998-03-01 DOI: 10.3109/15419069809040294

X Y Yi, E A Wayner, Y Kim, A J Fish

{"title":"Adhesion of cultured human kidney mesangial cells to native entactin: role of integrin receptors.","authors":"X Y Yi, E A Wayner, Y Kim, A J Fish","doi":"10.3109/15419069809040294","DOIUrl":"https://doi.org/10.3109/15419069809040294","url":null,"abstract":"Entactin is an extracellular matrix glycoprotein which binds to laminin and is found in most renal basement membranes and in the glomerular mesangial matrix. In the present study, we have characterized specific integrin receptors on cultured human mesangial cells (CHMC) responsible for adhesion to native entactin. The integrin receptors alpha 2 beta 1, alpha 3 beta 1, alpha 5 beta 1, alpha v beta 3, alpha v beta 5, and alpha 6 complexed with either beta 1 or beta 4 could be immune precipitated from detergent extracts of metabolically labeled CHMC. Adhesion assays with inhibitory anti integrin monoclonal antibodies (mab) demonstrated that CHMC use both alpha v beta 3 and a beta 1-containing integrin to bind surfaces coated with native entactin. Optimal binding of CHMC to native entactin required the participation of cations. Using wild type and mutant recombinant entactin fragments, the binding site for the alpha v beta 3 receptor was localized to the RGD sequence on the rod or E domain of entactin. CHMC adhesion to mutant full length recombinant entactin ligands lacking the E domain RGD sequence confirmed the presence of ligand binding site(s) for beta 1 integrin receptor(s). Differences in CHMC binding characteristics to recombinant and full length entactin compared to native bovine basement membrane entactin were observed. This suggests that tertiary molecular structure may contribute to entactin ligand binding properties. Primary amino acid residue sequences and tertiary structure of entactin may play roles in forming functional cell attachment sites in native basement membrane entactin.","PeriodicalId":79325,"journal":{"name":"Cell adhesion and communication","volume":"5 3","pages":"237-48"},"PeriodicalIF":0.0,"publicationDate":"1998-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/15419069809040294","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"20603566","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: 25

Adhesion and cytosolic dye transfer between macrophages and intestinal epithelial cells. 巨噬细胞与肠上皮细胞间的黏附和胞质染料转移。

Cell adhesion and communication Pub Date : 1998-03-01 DOI: 10.3109/15419069809040283

C A Martin, M E el-Sabban, L Zhao, R Burakoff, F R Homaidan

{"title":"Adhesion and cytosolic dye transfer between macrophages and intestinal epithelial cells.","authors":"C A Martin, M E el-Sabban, L Zhao, R Burakoff, F R Homaidan","doi":"10.3109/15419069809040283","DOIUrl":"https://doi.org/10.3109/15419069809040283","url":null,"abstract":"Activated macrophages (M phi) found in the intestinal lesions of patients with inflammatory bowel disease (IBD) secrete many inflammatory mediators which can regulate intestinal epithelial cell (IEC) function. However, little is known about direct M phi-IEC interactions. Two potential mechanisms by which cells may interact are through specific receptor-ligand binding of adhesion molecules, such as integrins or cadherins, and by exchange of cytoplasmic substances through transmembraneous channels called gap junctions. We investigated whether M phi could adhere to epithelial cells in culture and form transmembrane communication channels as defined by dye transfer. Primary cultures of murine M phi and a M phi cell line, P388D1, adhered to Mode-K and IEC6, but not CMT-93 IEC. Antibody blocking studies determined that P388D1-Mode-K binding was partially dependent on beta 2 integrin (CD18) function, Mode-K constitutively expressed CD106 (VCAM-1) and cell associated fibronectin, while P388D1 expressed low levels of CD49d/CD29 (VLA4) but blocking antibodies to these surface molecules did not inhibit P388D1-Mode-K adherence. Transfer of calcein dye from M phi to IEC was quantitated by flow cytometry and was dependent on M phi-IEC adhesion. Dye transfer was concentration dependent in that the fluorescence intensity of Mode-K was proportional to the number of adherent P388D1 cells as well as the dye load of the M phi. These results indicate that M phi interact with IEC by adhesion and possibly through gap junctions and may thus regulate IEC function by direct cell-cell communication.","PeriodicalId":79325,"journal":{"name":"Cell adhesion and communication","volume":"5 2","pages":"83-95"},"PeriodicalIF":0.0,"publicationDate":"1998-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/15419069809040283","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"20556611","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: 30

Down-regulation of laminin-binding integrins by 1 alpha,25-dihydroxyvitamin D3 in human melanoma cells in vitro. 1 α，25-二羟基维生素D3在体外下调人黑色素瘤细胞中层粘连蛋白结合整合素的作用。

Cell adhesion and communication Pub Date : 1998-03-01 DOI: 10.3109/15419069809040285

C M Hansen, M W Madsen, B Arensbak, T Skak-Nielsen, S Latini, L Binderup

{"title":"Down-regulation of laminin-binding integrins by 1 alpha,25-dihydroxyvitamin D3 in human melanoma cells in vitro.","authors":"C M Hansen, M W Madsen, B Arensbak, T Skak-Nielsen, S Latini, L Binderup","doi":"10.3109/15419069809040285","DOIUrl":"https://doi.org/10.3109/15419069809040285","url":null,"abstract":"In the present investigation the effect of 1 alpha,25(OH)2D3 on the expression of the integrin laminin receptor on the melanoma cell line SK-MEL-28 has been examined. The SK-MEL-28 cells were shown to contain high-affinity receptors for 1 alpha,25(OH)2D3 and cell proliferation was found to be inhibited in a dose-dependent manner in response to the hormone. Using monoclonal antibodies against the alpha 6-sub-unit of the integrin laminin receptor, immunocytochemistry demonstrated that exposure of cells to 1 alpha,25(OH)2D3 for 5 days caused a reduced staining intensity. This observation was further confirmed by dot blot analysis, where a dose-dependent decline of alpha 6 expression was obtained after treatment of the cells with 1 alpha,25(OH)2D3 for 6 days. FACS-analysis was performed in order to quantify this decline, and it was found that the level of alpha 6-subunits on the cell surface was reduced by more than 40%. Additional investigations including Northern blot analyses of poly(A)+RNA extracts also showed a dose-dependent reduction of alpha 6 mRNA. Interestingly, the decrease of alpha 6 expression on the surface of SK-MEL-28 melanoma cells was accompanied by a reduced ability of the cells to adhere to an artificial basement membrane. In conclusion, the present investigation shows that besides having an antiproliferative effect on the SK-MEL-28 melanoma cells, 1 alpha,25(OH)2D3 is also able to inhibit the surface expression of the alpha 6-subunit of the integrin laminin receptor. Moreover, the results strongly indicate that 1 alpha,25(OH)2D3 exerts its regulatory effect on the alpha 6-subunit at the transcriptional level rather than at the protein level.","PeriodicalId":79325,"journal":{"name":"Cell adhesion and communication","volume":"5 2","pages":"109-20"},"PeriodicalIF":0.0,"publicationDate":"1998-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/15419069809040285","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"20556613","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