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PubMed1990

Solid-phase monoclonal antibodies. A novel method of directing the function of biologically active molecules by presenting a specific orientation.

Monoclonal antibodies were produced against fibronectin and vitronectin, using the extracellular matrix from cultured bovine corneal endothelial cells as immunogen. Some antibodies inhibited the adhesion of BHK-21 cells to these molecules, in a standard assay with fibronectin or vitronectin coated on a plastic surface. By first coating the plastic surface with the monoclonal antibodies and subsequently binding vitronectin, the inhibitory effect was markedly increased. Divalent fibronectin required the presence of antibody in the medium as well as coated on the surface for maximal inhibition of cell adhesion. The inhibitory effect of surface-coated antibodies was stable in the presence of cells up to at least 24 h in vitro. Using this antibody coating method the surface could either be made compatible for cell adhesion (using non-inhibitory antibodies) or refractory. Assays performed by this method have considerable potential for quantifying particular functions of extracellular matrix molecules.

Animals↗
PubMed1988

Cell-substratum interactions: serum spreading factor.

We have prepared a fraction of commercial fetal calf serum whose major component comprises proteins of apparent molecular mass 65-80 kDa. These preparations elicit cell spreading responses in serum-free medium at concentrations similar to those reported for human vitronectin. In addition, we have identified (by a protein blotting technique) the 65-80 kDa component as the active species in our preparations. Cell spreading responses in the presence of our 'bovine vitronectin' preparations are similar to cell spreading on fetal calf serum. (In contrast, cell spreading on bovine fibronectin showed very different kinetics). Our results suggest that bovine vitronectin may be an important component of fetal calf serum involved in conditioning cell culture substrata.

Animals↗
PubMed2004

c-Src-dependent cross-talk between CEACAM6 and alphavbeta3 integrin enhances pancreatic adenocarcinoma cell adhesion to extracellular matrix components.

Carcinoembryonic antigen-related cell adhesion molecule 6 (CEACAM6) is an immunoglobulin superfamily member with a diversity of extracellular ligands that is implicated in the initiation and progression of a variety of malignancies. We sought to characterize the effects of CEACAM6 crosslinking on pancreatic adenocarcinoma cellular interaction with the extracellular matrix (ECM) components fibronectin and vitronectin. Antibody-mediated CEACAM6 crosslinking was performed and the ability of BxPC3 cells, which inherently overexpress CEACAM6, to adhere to fibronectin and vitronectin was quantified. The roles of the archetypal fibronectin (alpha5beta1 integrin) and vitronectin (alphavbeta3 integrin) receptors were determined. The effects of c-Src inhibition were investigated using the Src family kinase inhibitor 4-amino-5-(4-chlorophenyl)-7-(t-butyl)pyrazolo[3,4-d]pyrimidine (PP2) and c-Src specific RNA interference. CEACAM6 crosslinking initiates c-Src-dependent cross-talk between CEACAM6 and alphavbeta3 integrin, leading to increased ECM component adhesion. CEACAM6-mediated signaling events may contribute to the invasive and metastatic potential of pancreatic adenocarcinoma cells by promoting their interaction with ECM components.

Adenocarcinoma↗
PubMed2005

ADAM15 decreases integrin alphavbeta3/vitronectin-mediated ovarian cancer cell adhesion and motility in an RGD-dependent fashion.

We have recently described that integrin alphavbeta3 upon interaction with its major extracellular matrix ligand vitronectin induces adhesion, motility, and proliferation of human ovarian cancer cells. Due to the important function of alphavbeta3 in cancer cell biology, it has been the effort of many scientific approaches to specifically target alphavbeta3-mediated cell adhesion and tumorbiological effects arising thereof by synthetic integrin antagonists. More recently, proteins of the ADAM family have been recognized as naturally occurring integrin ligands. Among those, human ADAM15 which encompasses the integrin binding RGD motif was shown to interact with integrin alphavbeta3. Thus, we investigated in human ovarian OV-MZ-6 cancer cells, expressing both ADAM15 and alphavbeta3, whether ADAM15 might affect alphavbeta3-mediated tumorbiological effects. We stably (over)expressed ADAM15 or its extracellular domain in OV-MZ-6 cells as well as respective ADAM15 mutants containing the tripeptide SGA instead of RGD. Cells (over)expressing ADAM15-RGD exhibited a significantly reduced alphavbeta3-mediated adhesion to vitronectin. Also, a significant time-dependent decline in numbers of cells cultivated on vitronectin was noticed. This effect was found to be rather due to impaired alphavbeta3-mediated cell adhesion than decreased cell proliferation rates, since de novo DNA synthesis was not significantly altered by elevated ADAM15 expression. Moreover, a substantially decreased random cellular motility was noticed as a function of ADAM15 encompassing an intact RGD motif. In conclusion, our results point to a physiological role of ADAM15 as a natural binding partner of integrin alphavbeta3 thereby loosening tumor cell adhesion to the underlying matrix and regulating tumor cell migration and invasion.

ADAM Proteins↗
PubMed1996

Attachment and differentiation in vitro of trophoblast from normal and preeclamptic human placentas.

OBJECTIVE: Trophoblast from preeclamptic patients shows impairment of various functions, including restricted invasive behavior of extravillous trophoblast. In this light the effect of different matrix components on attachment and differentiation of primary trophoblast cultures derived from normal and preeclamptic pregnancies was investigated. STUDY DESIGN: Trophoblast was isolated from placentas of normotensive (n = 5) and preeclamptic patients (n = 5) and cultured up to 7 days on LabTek slides precoated with fibronectin, laminin, or vitronectin. Attachment was evaluated 24 hours after plating, the degree of syncytialization was evaluated, and slides were immunocytochemically stained for cytokeratin, vimentin, human chorionic gonadotropin, and human placental lactogen. RESULTS: Trophoblast from placentas of preeclamptic patients showed a significantly lower attachment on fibronectin and vitronectin compared with controls. Diminished multinuclear cell formation was found on uncoated and laminin-coated slides in preeclamptic cases. No difference was found in the percentage of human chorionic gonadotropin- and human placental lactogen-positive cells between groups. CONCLUSIONS: Lower trophoblast attachment on fibronectin and vitronectin was observed in preeclamptic pregnancies, which may reflect differences in expression of matrix receptors. Lower syncytialization of trophoblast in this group indicates an intrinsic defect in differentiation, but otherwise no differences were found in differentiation between normotensive and preeclamptic patients.

Adult↗
PubMed1995

Extracellular matrix on intraocular lenses.

We examined the distribution of extracellular matrix components in the proteinaceous matrix on explanted IOLs using immunohistochemistry to clarify the nature of proteinaceous deposits on the surfaces of IOLs. We examined 15 polymethylmethacrylate (PMMA) IOLs and one silicone IOL explanted from patients. The IOLs were immunostained for cellular fibronectin, types I and IV collagen, and vitronectin. Various amounts of fibronectin, types I and IV collagen, and vitronectin were detected in the extracellular matrix on all IOLs with cellular deposits. Types I and IV collagen and cellular fibronectin were present in the extracellular matrix and were probably the products of cells adhering to the IOLs. Vitronectin in the fibrous extracellular matrix appeared to represent an adsorption material derived from the aqueous humor. These proteinaceous deposits associated with cellular deposits indicate unsuccessful formation of granulation tissue and could influence IOL biocompatibility.

Adult↗
PubMedDate not supplied

Cell adhesion glycoproteins in the human lamina cribrosa.

PURPOSE: The distribution of the cell adhesion glycoproteins, laminin, fibronectin, tenascin, vitronectin, thrombospondin, and entactin/nidogen, was examined in the human lamina cribrosa. METHODS: Frozen sections of the optic nerve head from 7 normal human elderly donors were stained by immunohistochemistry. RESULTS: All six glycoproteins were detected in this tissue. While laminin and entactin/nidogen were observed linearly, reflecting the localization of basement membranes, fibronectin was identified diffusely. Marked tenascin immunoreactivity was apparent in the lamina cribrosa, but little or no tenascin staining was detected in the sclera. Vitronectin showed a fine fibrillar staining pattern in the lamina cribrosa, and, to a lesser extent, in the sclera and pial septa. Thrombospondin staining was apparent only in the sclera and the lamina cribrosa, which traversed the optic nerve. CONCLUSIONS: These results indicate that extracellular matrix components in the lamina cribrosa differ from those in the sclera or pial septa. This study is the first report that the human lamina cribrosa includes vitronectin and thrombospondin.

Aged↗
PubMed2002

Snake venom disintegrin, saxatilin, inhibits platelet aggregation, human umbilical vein endothelial cell proliferation, and smooth muscle cell migration.

A novel disintegrin, saxatilin, was purified from Korean snake (Gloydius saxatilis) venom by means of chromatographic fractionations. We have also isolated the cDNA encoding the disintegrin using cDNA library of the snake venom gland and analyzed its complete nucleotide sequence. Saxatilin is a single-chain polypeptide composed of 73 amino acids including 12 cysteines as well as the tripeptide sequence Arg-Gly-Asp (RGD), a proposed recognition site of adhesive proteins. Molecular mass of saxatilin was determined to be 7712 Da by matrix-assisted laser desorption ionization mass spectrometry. Saxatilin inhibits glycoprotein (GP) IIb-IIIa binding to immobilized fibrinogen with IC(50) of 2.0 nM and ADP-induced platelet aggregation with IC(50) of 127 nM, respectively. The snake venom disintegrin also significantly suppresses basic fibroblast growth factor-induced human umbilical vein endothelial cell (HUVEC) proliferation, but has little effect on normal growth of the cell. Interaction of human umbilical vein cell to immobilized vitronectin is also inhibited by binding of saxatilin to alpha(v)beta(3) integrin. Adhesion of smooth muscle cells (SMCs) to vitronectin as well as vitronectin-induced migration of the cells was strongly inhibited by saxatilin. Several lines of experimental evidence suggest potential use of saxatilin for development of therapeutic agents.

Animals↗
PubMed1997

Expression of the membrane attack complex of complement and its inhibitors during human liver allograft transplantation.

BACKGROUND/AIMS: In order to test the possible role of activated complement in human liver allograft rejection, we evaluated the expression of the membrane attack complex of complement, its soluble inhibitors clusterin and vitronectin and its membrane inhibitor protectin during the evolution of liver transplants. METHODS: An indirect immunoperoxidase technique was applied to biopsy specimens obtained from liver allografts in 16 patients without complications, nine with acute rejection, four with chronic rejection and five with biliary complications. RESULTS: Two types of membrane attack complex deposition were observed: (a) extracellular deposits in portal tracts and perisinusoidal matrix, associated with clusterin and vitronectin, similar to those found in the normal liver; and (b) intra-portal vascular deposits, devoid of clusterin and vitronectin. Vascular membrane attack complex deposition was detected in four clinically stable patients, three patients with chronic rejection and two patients with biliary complications. In clinically stable patients, vascular membrane attack complex deposition was restricted to large portal vessels and was detected in a minority of portal tracts. In patients with chronic rejection or biliary complications, vascular membrane attack complex deposition was detected along both large and small portal vessels and was present in the majority of portal tracts. Protectin induction on hepatocytes was detected in 33 cases. CONCLUSIONS: Our results suggest that membrane attack complex deposition is unlikely to play a major role in the pathogenesis of acute liver allograft rejection but may contribute to the vascular and biliary lesions observed in chronic rejection.

Adult↗
PubMed2000

Binding of 125I-insulin-like growth factor-II to cells cultured in fetal bovine serum: a complication.

Insulin-like growth factor II is an important fetal mitogen in mice and humans and its biological activity is regulated in a complex manner. The peptide interacts with three membrane-bound receptors, with a superfamily of insulin-like growth factor binding proteins and with the proteoglycan, glypican-3. Recently, the blood protein, vitronectin, has been identified as a novel insulin-like growth factor II-binding protein. Many studies have used cell lines maintained in fetal bovine serum to identify cell surface insulin-like growth factor II binding sites. We now describe a complication associated with the interpretation of such in vitro studies. Fetal bovine serum-derived vitronectin adheres very tightly to tissue culture dishes. When cells that have been maintained in fetal bovine serum are incubated with 125I-insulin-like growth factor II, a substantial fraction of the 125I-insulin-like growth factor II apparently associated with the cell surfaces may represent radioliogand bound by the fetal bovine serum-derived vitronectin. This may result in over-estimation of cell surface insulin-like growth factor II binding sites.

Animals↗
PubMed1991

Functional interaction of plasminogen activator inhibitor type 1 (PAI-1) and heparin.

Plasminogen activator inhibitor type 1 (PAI-1), the fast-acting inhibitor of tissue-type plasminogen activator (t-PA) and urokinase (u-PA), is a member of the serpin superfamily of proteins. Both in plasma and in the growth substratum of cultured endothelial cells, PAI-1 is associated with its binding protein vitronectin, resulting in a stabilization of active PAI-1. Recently, it has been demonstrated that the PAI-1-binding site on vitronectin is adjacent to a heparin-binding site (Preissner et al., 1990). Furthermore, it can be deduced that the amino acid residues, proposed to mediate heparin binding in the serpins antithrombin III and heparin cofactor II, are conserved in PAI-1. Consequently, here we have investigated whether PAI-1 also interacts with heparin. At pH 7.4, PAI-1 quantitatively binds to heparin-Sepharose and can be eluted with increasing [NaCl]. Binding of PAI-1 to heparin-Sepharose can be efficiently competed with heparin in solution (IC50, 7 microM). In the presence of heparin, the protease specificity of PAI-1 toward thrombin is substantially increased. This is shown by (i) quenching of thrombin activity of PAI-1 in the presence of heparin and (ii) induction of the formation of SDS-stable complexes between thrombin and PAI-1 by heparin. In a dose response curve, both effects reached a maximum at approximately 1 unit/mL and then diminished again upon further increasing the heparin concentration, strongly suggesting a template mechanism as an explanation for the observed effect. In contrast to vitronectin, heparin does not stabilize the active conformation of PAI-1.(ABSTRACT TRUNCATED AT 250 WORDS)

Affinity Labels↗
PubMed2001

Integrin activation is required for VEGF and FGF receptor protein presence on human microvascular endothelial cells.

Endothelial cell proliferation and migration is initiated by growth factors including FGF and VEGF that bind to specific transmembrane receptor tyrosine kinases. Mechanisms that regulate in vivo expression of fibroblast growth factor receptors (FGFR) and vascular endothelial growth factor receptors (VEGFR) are not well understood. Since it is well known that different matrices influence the proliferation and migration of endothelial cells in culture, we hypothesized that changes in the extracellular matrix environment can regulate growth factor receptors on endothelial cells. We cultured human microvascular endothelial cells on different matrices (vitronectin, laminin, fibronectin, fibrin, and collagen IV) and examined for the presence of growth factor receptors (FGFR-1, FGFR-2, VEGFR-1, and VEGFR-2). We show that vitronectin increased the presence of all four growth factor receptors and most notably, VEGFR-1. In contrast, fibrin decreased all four receptors, especially FGFR-1 and FGFR-2. Inhibiting phosphotyrosine signaling abolished immunostaining for all four receptors, regardless of the matrix, but was not dependent on activating the Fyn-Shc pathway. Cells plated on vitronectin in the presence of blocking antibodies to integrins alphavbeta3 and alphavbeta5 similarly decreased presence of these growth factor receptors. Our data suggests a possible mechanism of how matrix-integrin interactions regulate endothelial cell responsiveness to growth factors and anchorage-dependent cell growth.

Adaptor Proteins, Signal Transducing↗
PubMed2002

Matrix metalloproteinases and cellular fibrinolytic activity.

Several molecular interactions between the matrix metalloproteinase (MMP) and the plasminogen/plasmin (fibrinolytic) system may affect cellular fibrinolysis. MMP-3 (stromelysin-1) specifically hydrolyzes urokinase (u-PA), yielding a 17 kD NH2-terminal fragment containing the functionally intact receptor (u-PAR)-binding sequence and a 32 kD COOH-terminal fragment containing the intact serine proteinase domain. MMP-3 generates an angiostatin-like fragment (containing kringles 1-4 with the cellular binding domains) from plasminogen. Treatment with MMP-3 of monocytoid THP-1 cells saturated with bound plasminogen, resulted in a dose-dependent reduction of the amount of u-PA-activatible plasminogen. Treatment with MMP-3 of cell-bound u-PA, in contrast, did not alter cell-associated u-PA activity. These data thus indicate that MMP-3 may downregulate cell-associated plasmin activity by decreasing the amount of activatible plasminogen, without affecting cell-bound u-PA activity. MMP-3 also specifically interacts with the main inhibitors of the fibrinolytic system. Thus, MMP-3 specifically hydrolyzes human alpha2-antiplasmin (alpha2-AP), the main physiological plasmin inhibitor. alpha2-AP cleaved by MMP-3 no longer forms a stable complex with plasmin and no longer interacts with plasminogen. Cleavage and inactivation of alpha2-AP by MMP-3 may constitute a mechanism favoring local plasmin-mediated proteolysis. Furthermore, MMP-3 specifically hydrolyzes and inactivates human plasminogen activator inhibitor-1 (PAI-1). Stable PAI-1 bound to vitronectin is cleaved and inactivated by MMP-3 in a comparable manner as free PAI-1; the cleaved protein, however, does not bind to vitronectin. Cleavage and inactivation of PAI-1 by MMP-3 may thus constitute a mechanism decreasing the antiproteolytic activity of PAI-1 and impairing the potential inhibitory effect of vitronectin-bound PAI-1 on cell adhesion and/or migration. These molecular interactions of MMP-3 with enzymes, substrates and inhibitors of the fibrinolytic system may thus play a role in the regulation of (cellular) fibrinolysis. Furthermore, the temporal and topographic expression pattern of MMP components, as well as studies in gene-deficient mice, suggest a functional role in neointima formation after vascular injury.

Animals↗
PubMed2001

Importance of the amino-acid composition of the shutter region of plasminogen activator inhibitor-1 for its transitions to latent and substrate forms.

The serpins are of general protein chemical interest due to their ability to undergo a large conformational change consisting of the insertion of the reactive centre loop (RCL), which becomes strand 4, into the central beta sheet A. To make space for the incoming RCL, the 'shutter region' opens by the beta strands 3A and 5A sliding apart over the underlying alpha helix B. Loop insertion occurs during the formation of complexes of serpins with their target serine proteinases and during latency transition. This type of loop insertion is unique to plasminogen activator inhibitor-1 (PAI-1). We report here that amino-acid substitutions in a buried cluster of three residues forming a hydrogen bonding network in the shutter region drastically accelerate PAI-1 latency transition; that the rate was in all cases normalized by the PAI-1 binding protein vitronectin; and that substitution of an adjacent beta strand 5A Lys residue, believed to anchor beta strand 5A to other secondary structural elements, had differential effects on the rates of latency transition in the absence and the presence of vitronectin, respectively. An overlapping, but not identical set of substitutions resulted in an increased tendency to substrate behaviour of PAI-1 at reaction with its target proteinases. These findings show that vitronectin regulates the movements of the RCL through conformational changes of the shutter region and beta strand 5A, are in agreement with RCL insertion proceeding by different routes during latency transition and complex formation, and contribute to the biochemical basis for the potential use of PAI-1 as a therapeutic target in cancer and cardiovascular diseases.

Amino Acid Substitution↗
PubMed2003

Concurrent signaling from Galphaq- and Galphai-coupled pathways is essential for agonist-induced alphavbeta3 activation on human platelets.

The integrin alphavbeta3 mediates platelet adhesion to the matrix protein osteopontin and likely is the predominant integrin mediating platelet adhesion to the matrix protein vitronectin. To address the mechanism that regulates alphavbeta3 activity in platelets, we measured the effect of the P2Y1 antagonist adenosine 3'-phosphate-5'-phosphate (A3P5P) and the P2Y12 antagonist AR-C66096 on ADP-stimulated platelet adhesion to osteopontin and vitronectin. Each antagonist completely inhibited platelet adhesion, implying that concurrent stimulation of P2Y1 and P2Y12 was required to activate alphavbeta3. The reducing agent dithiothreitol and Mn2+ also induced platelet adhesion to osteopontin, but did so without stimulating platelet activation. Thus, these data suggest that ADP stimulation regulates alphavbeta3 activity by perturbing the conformation of its extracellular domain. The actin polymerization inhibitors cytochalasin D and latrunculin A also induced platelet adhesion to osteopontin and vitronectin. Thus, alphavbeta3 activity in resting platelets appears to be constrained by the platelet cytoskeleton. Moreover, the effect of these agents was inhibited by A3P5P and AR-C66096 at micromolar and subnanomolar concentrations, respectively, suggesting that subthreshold platelet stimulation by ADP was required. Our data suggest that signals from both Galphaq- and Galphai-coupled receptors converge to release cytoskeletal constraints on alphavbeta3. We propose that the release of cytoskeletal constraints and a concurrent increase in affinity for ligands is responsible for alphavbeta3-mediated platelet adhesion.

Actins↗
PubMed1987

Human endothelial cells synthesize and express an Arg-Gly-Asp-directed adhesion receptor involved in attachment to fibrinogen and von Willebrand factor.

Human umbilical vein endothelial cells express a heterodimeric adhesion receptor complex consisting of noncovalently associated alpha and beta subunits that under reducing conditions have molecular masses of 135 kDa and 115 kDa, respectively. This complex can be isolated in pure form from an affinity matrix consisting of an Arg-Gly-Asp-containing heptapeptide and is specifically immunoprecipitated with monoclonal antibodies (mAbs) directed against the vitronectin receptor of human melanoma cells. These data suggest that this complex is one member of a large family of cell adhesion receptors. One of the mAbs, LM609, inhibits the attachment of human endothelial cells to fibrinogen, von Willebrand factor, and vitronectin yet has no effect on the attachment of these cells to fibronectin, collagen, or laminin. In addition, mAb LM609 inhibits attachment of endothelial cells to an immobilized synthetic peptide containing the Arg-Gly-Asp sequence. This adhesion receptor appears structurally similar to the IIb/IIIa glycoprotein complex expressed on platelets yet is antigenically distinct, since mAb LM609 fails to recognize IIb/IIIa glycoproteins. This receptor organizes in clusters on endothelial cells during their attachment to von Willebrand factor, vitronectin, or the Arg-Gly-Asp-containing heptapeptide. The data presented in this report suggest that Arg-Gly-Asp recognition may play a significant role in biological events associated with vascular proliferation.

Antibodies, Monoclonal↗
PubMed1992

Role of the alpha v beta 3 integrin in human melanoma cell invasion.

The human melanoma cell line A375M expresses the vitronectin receptor (alpha v beta 3 integrin) on its cell surface. Treatment of A375M cells with either polyclonal or monoclonal anti-alpha v beta 3 antibodies resulted in stimulation of invasion through basement membrane matrices in vitro. Similar treatment of these cells with a monoclonal anti-alpha v antibody, which does not inhibit the adhesive function of the alpha v beta 3 antigen, also stimulated invasion; however, anti-beta 3 antibody treatment had no effect. Furthermore, pretreatment of the cells with vitronectin or addition of vitronectin to the basement membrane matrix also resulted in stimulation of invasion. Similar treatments with fibronectin receptor antibody or fibronectin had no effect on invasion. Analysis of type IV collagenase expression in cells treated with anti-alpha v beta 3 antibody showed higher levels of both the secreted 72-kDa enzyme and its mRNA. Signal transduction through the alpha v beta 3 integrin could underlie the elevated expression of metalloproteinase and the enhanced invasion of A375M cells through basement membrane matrices.

Cell Adhesion↗
PubMed2000

Regulation of integrin alpha vbeta 3-mediated endothelial cell migration and angiogenesis by integrin alpha5beta1 and protein kinase A.

Recent studies indicate that angiogenesis depends, in part, on ligation of integrin alpha(5)beta(1) by fibronectin. Evidence is now provided that integrin alpha(5)beta(1) regulates the function of integrin alpha(v)beta(3) on endothelial cells during their migration in vitro or angiogenesis in vivo. Secretion of fibronectin by endothelial cells leads to the ligation of integrin alpha(5)beta(1), which potentiates alpha(v)beta(3)-mediated migration on vitronectin without influencing alpha(v)beta(3)-mediated cell adhesion. Endothelial cell attachment to vitronectin suppresses protein kinase A (PKA) activity, while addition of soluble anti-alpha(5)beta(1) restores this activity. Moreover, agents that activate intracellular PKA, such as forskolin, dibutyryl cAMP or alpha(5)beta(1) antagonists, suppress endothelial cell migration on vitronectin in vitro or angiogenesis in vivo. In contrast, inhibitors of PKA reverse the anti-migratory or anti-angiogenic effects mediated by alpha(5)beta(1) antagonists. Therefore, alpha(v)beta(3)-mediated endothelial cell migration and angiogenesis can be regulated by PKA activity, which depends on the ligation state of integrin alpha(5)beta(1).

Cell Adhesion↗