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Query: UMLS:C0001511 (Adhesion)
 5,955 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

In a previous study we showed that tumorigenic and invasive human uroepithelial cell lines are characterized by the presence of sialosyl Le(a) (sLe(a)) ganglioside. Our data suggested that expression of this glycolipid correlated with acquisition of the malignant phenotype by human urothelial cells. To evaluate the postulated adhesion function of sLe(a) antigen, we studied the adherence of 6 human urothelial cell lines with different expressions of this carbohydrate structure to E-selectin-expressing CHO cells. The only cell line that bound specifically to E-selectin was Hu 1703He, which expressed the highest level of sLe(a) antigen. The involvement of carbohydrate-E-selectin interaction in the adhesion of Hu 1703He cells was indicated by the following facts: (i) anti-E-selectin monoclonal antibody (MAb) completely abolished binding to E-selectin-expressing CHO cells; (ii) removal of sialic acid from Hu 1703He cells highly decreased the adhesion. Adhesion correlated with the presence of several sLe(a)-carrying glycoproteins, which was shown by immunoblotting of Hu 1703He cell lysate with anti-sLe(a) MAb 19-9. The binding of antibody was abolished when cell lysate was treated with O-sialoglycoprotein endopeptidase, suggesting that sLe(a) is present on O-linked oligosaccharides. However, incubation of Hu 1703He cells with O-sialoglycoprotease had no effect on adhesion to E-selectin or on binding of 19-9 MAb to the cell surface. Our data suggest that (i) protein-bound sLe(a) oligosaccharides represent only a minor portion of whole sLe(a) antigen produced by uroepithelial cells; (ii) effective binding to E-selectin occurs when sLe(a) oligosaccharide present on cell-surface glycosphingolipids is expressed in high density since the cell lines with moderate expression of sLe(a) ganglioside did not bind to E-selectin-transfected CHO cells.
Int J Cancer 1996 Oct 09
PMID:Adhesion of human uroepithelial cells to E-selectin: possible involvement of sialosyl LewisA-ganglioside. 890 Apr 35

That adhesion molecules play a major role in the regulation of normal hematopoiesis is suggested by the abundance of these molecules present on early bone marrow progenitor cells and their differential pattern of expression at discrete stages of differentiation along the various cell lineages. In particular, precursor cell matrix/endothelial interactions determine retainment or release of hematopoietic cells from the bone marrow microenvironment. Consequently, changes in the affinity or quantitative expression of adhesion molecules on either the bone marrow stroma or the blood cell precursor component-during normal development or due to activation or a malignant process-will affect cell attachment. Adhesion molecules, therefore, are modulator molecules which alter the biological behavior of normal or leukemic hematopoietic cells, primarily in terms of migration and localization properties, although they also participate in many other cell functions such as cytotoxicity, antigen presentation and binding of viruses or cancer cells. Several membrane-bound adhesion molecules and, in some instances, their soluble counterparts which may be biologically active, have been described in acute myeloid leukemia. The potential diagnostic or physiological significance of leukocyte antigens with adhesive properties will be addressed in this comment.
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PMID:Adhesion molecules in acute myeloid leukemia. 894 91

Metastatic spread of some solid tumours is thought to depend upon the adhesion of tumour cells to the vascular endothelium followed by extravasation into surrounding tissues. We investigated the role of beta 1 integrins in the adhesion of the breast adenocarcinoma cell line MDA-MB-231 and the melanoma cell line RPMI-7951 to quiescent human umbilical vein endothelial cells (HUVEC) in vitro. In the course of adhesion assays, tumour cells were observed to adhere to quiescent HUVEC monolayers, particularly at endothelial cell-cell junctions. Immunohistochemistry revealed concentration of beta 1 integrin expression at these sites. Adhesion was reduced by pretreatment of either tumour cells or HUVEC with antibodies against beta 1 integrins. Simultaneous treatment of HUVECs and tumour cells with these antibodies produced an additive blocking effect, consistent with a heterotypic adhesion mechanism. Our data suggest that tumour cell and endothelial beta 1 integrins may play a crucial role in the arrest and migration of tumour cells through the vascular endothelium in the absence of endothelial 'activation'.
Br J Cancer 1996 Dec
PMID:beta-1 Integrins mediate tumour cell adhesion to quiescent endothelial cells in vitro. 895 90

All trans-retinoic acid (ATRA) induces complete remission in acute-promyelocytic-leukemia (APL) patients. This study investigated the adhesive properties of APL cells for the endothelium and the extracellular matrix, their motility and the effect of ATRA on these functions. Blasts from 7 APL patients adhered to resting and IL-1-activated endothelium, to the same degree as normal PMN. Adhesion was partially mediated by ICAM-1 and, for IL-1-activated endothelium, by VCAM-1 and E-selectin. These cells showed less adhesiveness for the matrix than PMN, although they maintained the same substrate preference: they adhered to fibronectin and thrombospondin, but not to laminin and type-IV collagen. Exposure to ATRA in vitro (1 microM for 48 to 96 hr) increased the adhesiveness of APL cells; this effect was particularly evident in the case of sub-endothelial matrix and fibronectin. A similar increment in adhesiveness was observed when comparing cells from 2 patients before and after treatment with ATRA. APL cells migrated in response to fMLP and motility was increased by ATRA. In conclusion, APL cells were less adhesive to the matrix than PMN, but treatment with ATRA considerably enhanced their adhesive properties. This could be important in determining the efflux of leukemic cells from the bone marrow and their tissue infiltration during ATRA therapy.
Int J Cancer 1997 Jan 06
PMID:Effect of all trans-retinoic acid (ATRA) on the adhesive and motility properties of acute promyelocytic leukemia cells. 898 93

Adhesion of cancer cells to vascular endothelium is an important step in haematogenous metastasis of cancer. A human hepatocellular carcinoma cell line, HepG2, strongly adheres to human umbilical vein endothelial cells (HUVECs) through the interaction of E-selectin and its carbohydrate ligand sialyl Lewis X. In this study, we investigated alteration in integrin expression on HepG2 cells, which follows the selectin-mediated initial adhesion of HepG2 cells to HUVECs. Expression of alpha2beta1 integrin was markedly increased when the HepG2 cells adhered to HUVECs. Among the tested cytokines that are known to be produced by endothelial cells, recombinant hepatocyte growth factor (rHGF) could replace the effect of HUVECs, and a similar increase in integrin expression was observed by the addition of 20 ng ml-1 rHGF to HepG2. The increment of alpha2beta1 integrin expression was significantly inhibited by anti-HGF neutralizing antibody treatment. HepG2 cells expressed alpha2, alpha6, beta1, and beta4 integrin subunits, but expression of integrins other than alpha2beta1 was not affected by the rHGF treatment. The rHGF treatment of HepG2 cells resulted in augmented adhesion to immobilized collagen. This augmentation in adhesion to collagen was completely blocked by the addition of anti-alpha2- or anti-beta1-integrin antibody. In double-chamber chemoinvasion experiments, transmigration of the HepG2 cells through extracellular matrix (ECM) gel was significantly accelerated by co-cultivation with HUVECs. A similar level of enhancement in transmigration activity of the cancer cells was observed by the addition of rHGF. Our interpretation of the results described above is that the cancer cells received stimulation from cytokines, such as HGF, presented by vascular endothelial cells, following the initial adhesion of cancer cells via selectins. This resulted in the secondary increment in the expression of cell adhesion molecules, such as the alpha2beta1 integrin, and led to the augmented adhesive activities of cancer cells towards extracellular matrices at vascular walls. We suggest that this sequence of events is involved in the facilitated migration of some cancer cells to extravascular tissues.
Br J Cancer 1997
PMID:Involvement of hepatocyte growth factor in increased integrin expression on HepG2 cells triggered by adhesion to endothelial cells. 900 May 97

The integrins are receptors that regulate interaction between epithelial cells and the extracellular matrix. Previous studies have shown that a reduction in the expression of the alpha2beta1, alpha3beta1, alpha6beta1, alpha(v)beta1 and alpha(v)beta5 integrins in primary breast cancer is associated with positive nodal status. In order to assess the functional significance of altered integrin expression, primary breast cancer cells were derived from individual patients with known tumour characteristics using immunomagnetic separation. Purified human fibronectin, vitronectin, laminin and type IV collagen were used to represent the principal extracellular matrix proteins in an in vitro adhesion assay. Primary breast cancer cells from lymph node-positive patients were significantly less adhesive to each of the matrix proteins studied (P<0.001, Mann-Whitney U-test). Matrix adhesion of primary breast cancer cells from node-negative patients was inhibited by appropriate integrin monoclonal antibodies (P<0.001, paired Wilcoxon test). Adhesion to fibronectin, vitronectin and laminin, but not type IV collagen, was influenced by the inhibitor arginine-glycine-aspartate, suggesting that breast cancer cell recognition of collagen IV is mediated through alternative epitopes. Weak matrix adhesion correlated with loss of integrin expression in tissue sections from corresponding patients assessed using immunohistochemistry. This study demonstrates a link between altered integrin expression and function in primary breast cancers predisposed to metastasize.
Br J Cancer 1997
PMID:Altered cell-matrix contact: a prerequisite for breast cancer metastasis? 904 16

Peritoneal dissemination frequently occurs after surgery in patients with gastric cancer. The presence of peritoneal metastasis after surgery affects prognosis. Very little is known about the biochemical processes involved in the initial attachment of gastric cancer cells to peritoneal mesothelial cells. We conducted in vitro and in vivo studies to assess the role of adhesion molecules and TGF-beta1 in this process, using 4 cell lines derived from human gastric cancers. NUGC-4 cells, which disseminate early after inoculation into the abdominal cavity of nude mice, predominantly express CD44H and beta1 integrin. We found that NUGC-4 cells adhered to monolayers of mesothelial cells more firmly than to other cell lines. Adhesion of NUGC-4 cells to mesothelial cells was partially inhibited by antibodies against CD44H or the beta1 subunit of integrin and was completely blocked by a combination of these 2 antibodies. Treatment with ligands for CD44H and beta1 integrin also inhibited adhesion. In the NUGC-4 cell culture medium, larger amounts of TGF-beta1 were detected in relation to the increase in cancer cells than in the other cell lines. TGF-beta1 increased the expression of CD44H in NUGC-4 cells and in mesothelial cells and augmented adhesion and implantation of NUGC-4 cells to mesothelial cells accompanied by accumulation of extracellular matrix (ECM) components. Treatment with antibodies against both CD44H and beta1 integrin inhibited the dissemination of NUGC-4 cells in the peritoneal cavity of nude mice and prolonged their survival time. Our findings suggest that CD44H and integrins mediate the initial attachment of gastric cancer cells to mesothelial cells and that TGF-beta1 participates in the promotion of the disease. Increased expression of CD44H and of the amount of ligands for CD44H and integrins induced by TGF-beta1 promotes early development of peritoneal dissemination.
Int J Cancer 1997 Mar 04
PMID:Adhesion molecules and TGF-beta1 are involved in the peritoneal dissemination of NUGC-4 human gastric cancer cells. 905 64

Adhesion molecules mediate cell-cell and cell-matrix interactions and are essential for numerous physiological and pathological processes. Recent evidence from many laboratories suggests that adhesion molecules play an important role in tumor progression and may promote tumor growth and organ-specific metastasis. Certain adhesion molecules may also function as tumor suppressors. In this review, we describe current concepts concerning the role of the adhesion molecules in the pathogenesis of cancer and the development of therapeutic approaches which make use of this information. Hence, by preventing tumor cells from interacting with each other or with their microenvironment, tumor growth and metastasis can be suppressed. The feasibility of using anti-adhesion strategies to treat cancer has been demonstrated in many animal models. Thus, monoclonal antibodies (MAbs) against adhesion molecules, synthetic peptidic and nonpeptidic analogues of the recognition sequences on their receptors, soluble adhesion molecules and antisense oligonucleotides can inhibit tumor growth and gene therapy can restore the functions of altered tumor-suppressive adhesion molecules.
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PMID:Adhesion molecules as targets for cancer therapy. 915 Nov 36

Adhesion of metastatic cancer cells at secondary sites is known to be regulated by several families of adhesion proteins, including selectins and integrins. Colon carcinoma cells have been shown to tether to and roll on both stimulated endothelial cells and purified E-selectin. We have demonstrated that HT-29 human colon carcinoma cells adhere specifically to an E-selectin-IgG chimera. Upon adhesion to E-selectin, the amount of tyrosine phosphorylation of several proteins in HT-29 cell lysates increases compared with cells in bovine serum albumin-coated wells on phosphotyrosine Western blots; this increase is statistically significant. This effect is specific for adhesion to E-selectin, since addition of an E-selectin blocking monoclonal antibody (MAb), E3, to the wells causes a statistically significant decrease in tyrosine phosphorylation relative to E-selectin alone on phosphotyrosine Western blots. One protein that is affected this way has been identified as c-src. Kinase assays show a dose-dependent and statistically significant decrease in c-src activity upon adhesion to E-selectin, which correlates with an increase in phosphorylation of Tyr 527, the negative regulatory tyrosine. CnBr digestion of 32P-labeled c-src shows an increase in phosphorylation of tyrosine 527 after adhesion to E-selectin. Our results may identify a signaling pathway involving the E-selectin ligand on HT-29 cells and c-src.
Int J Cancer 1997 May 16
PMID:Adhesion of HT-29 colon carcinoma cells to E-selectin results in increased tyrosine phosphorylation and decreased activity of c-src. 917 21

Mesothelial cells (MC) form a polarized monolayer lining serosal cavities. During serositis, the MC lining undergoes hyperplasia, and MC are shed into effusions. During these processes, contact with basement membrane and, ultimately, neighboring cells is at least temporarily lost, suggesting regulated alterations in cell/matrix and cell/cell adhesion. Such interactions are primarily mediated by integrins. Malignant mesothelioma has a growth pattern characterized by lateral, limited invasive but contiguous spread. During serositis, activated MC, both sessile and detached, expressed an extended spectrum of beta1, beta3 and beta4 integrins compared with resting MC, as shown by immunohistology. Malignant mesothelioma had an integrin repertoire and a subcellular distribution resembling that of activated sessile rather than floating MC. In vitro, MC exposed a more comprehensive pattern of integrins than that of the newly established mesothelioma cell lines ME-HD-1 and ME-HD-2, as shown by flow cytometry. MC consistently adhered better than mesothelioma cells to laminin, tenascin, fibronectin and collagen type IV. Adhesion of MC and mesothelioma cells to these matrix proteins was, at least in part, mediated via beta1 integrins. The different integrin profiles and adhesion properties of cultured MC and mesothelioma cells may reflect a limited functional differentiation of the latter.
Int J Cancer 1997 Jul 03
PMID:Pleural mesothelioma mimics the integrin profile of activated, sessile rather than detached mesothelial cells. 921 27


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