Integrins: A family of transmembrane glycoproteins (MEMBRANE GLYCOPROTEINS) consisting of noncovalent heterodimers. They interact with a wide variety of ligands including EXTRACELLULAR MATRIX PROTEINS; COMPLEMENT, and other cells, while their intracellular domains interact with the CYTOSKELETON. The integrins consist of at least three identified families: the cytoadhesin receptors(RECEPTORS, CYTOADHESIN), the leukocyte adhesion receptors (RECEPTORS, LEUKOCYTE ADHESION), and the VERY LATE ANTIGEN RECEPTORS. Each family contains a common beta-subunit (INTEGRIN BETA CHAINS) combined with one or more distinct alpha-subunits (INTEGRIN ALPHA CHAINS). These receptors participate in cell-matrix and cell-cell adhesion in many physiologically important processes, including embryological development; HEMOSTASIS; THROMBOSIS; WOUND HEALING; immune and nonimmune defense mechanisms; and oncogenic transformation.Antigens, CD29: Integrin beta-1 chains which are expressed as heterodimers that are noncovalently associated with specific alpha-chains of the CD49 family (CD49a-f). CD29 is expressed on resting and activated leukocytes and is a marker for all of the very late activation antigens on cells. (from: Barclay et al., The Leukocyte Antigen FactsBook, 1993, p164)Cell Adhesion: Adherence of cells to surfaces or to other cells.Integrin alphaV: An alpha integrin with a molecular weight of 160-kDa that is found in a variety of cell types. It undergoes posttranslational cleavage into a heavy and a light chain that are connected by disulfide bonds. Integrin alphaV can combine with several different beta subunits to form heterodimers that generally bind to RGD sequence-containing extracellular matrix proteins.Antigens, CD18: Cell-surface glycoprotein beta-chains that are non-covalently linked to specific alpha-chains of the CD11 family of leukocyte-adhesion molecules (RECEPTORS, LEUKOCYTE-ADHESION). A defect in the gene encoding CD18 causes LEUKOCYTE-ADHESION DEFICIENCY SYNDROME.Integrin beta Chains: Integrin beta chains combine with integrin alpha chains to form heterodimeric cell surface receptors. Integrins have traditionally been classified into functional groups based on the identity of one of three beta chains present in the heterodimer. The beta chain is necessary and sufficient for integrin-dependent signaling. Its short cytoplasmic tail contains sequences critical for inside-out signaling.Receptors, Vitronectin: Receptors such as INTEGRIN ALPHAVBETA3 that bind VITRONECTIN with high affinity and play a role in cell migration. They also bind FIBRINOGEN; VON WILLEBRAND FACTOR; osteopontin; and THROMBOSPONDINS.Integrin beta3: An integrin beta subunit of approximately 85-kDa in size which has been found in INTEGRIN ALPHAIIB-containing and INTEGRIN ALPHAV-containing heterodimers. Integrin beta3 occurs as three alternatively spliced isoforms, designated beta3A-C.Integrin alpha4: An integrin alpha subunit that is unique in that it does not contain an I domain, and its proteolytic cleavage site is near the middle of the extracellular portion of the polypeptide rather than close to the membrane as in other integrin alpha subunits.Integrin alphaVbeta3: An integrin that binds to a variety of plasma and extracellular matrix proteins containing the conserved RGD amino acid sequence and modulates cell adhesion. Integrin alphavbeta3 is highly expressed in OSTEOCLASTS where it may play role in BONE RESORPTION. It is also abundant in vascular smooth muscle and endothelial cells, and in some tumor cells, where it is involved in angiogenesis and cell migration. Although often referred to as the vitronectin receptor there is more than one receptor for vitronectin (RECEPTORS, VITRONECTIN).Fibronectins: Glycoproteins found on the surfaces of cells, particularly in fibrillar structures. The proteins are lost or reduced when these cells undergo viral or chemical transformation. They are highly susceptible to proteolysis and are substrates for activated blood coagulation factor VIII. The forms present in plasma are called cold-insoluble globulins.Integrin alpha3beta1: Cell surface receptor for LAMININ, epiligrin, FIBRONECTINS, entactin, and COLLAGEN. Integrin alpha3beta1 is the major integrin present in EPITHELIAL CELLS, where it plays a role in the assembly of BASEMENT MEMBRANE as well as in cell migration, and may regulate the functions of other integrins. Two alternatively spliced isoforms of the alpha subunit (INTEGRIN ALPHA3), are differentially expressed in different cell types.Integrin alpha6beta1: A cell surface receptor mediating cell adhesion to the EXTRACELLULAR MATRIX and to other cells via binding to LAMININ. It is involved in cell migration, embryonic development, leukocyte activation and tumor cell invasiveness. Integrin alpha6beta1 is the major laminin receptor on PLATELETS; LEUKOCYTES; and many EPITHELIAL CELLS, and ligand binding may activate a number of signal transduction pathways. Alternative splicing of the cytoplasmic domain of the alpha6 subunit (INTEGRIN ALPHA6) results in the formation of A and B isoforms of the heterodimer, which are expressed in a tissue-specific manner.Integrin alpha4beta1: Integrin alpha4beta1 is a FIBRONECTIN and VCAM-1 receptor present on LYMPHOCYTES; MONOCYTES; EOSINOPHILS; NK CELLS and thymocytes. It is involved in both cell-cell and cell- EXTRACELLULAR MATRIX adhesion and plays a role in INFLAMMATION, hematopoietic cell homing and immune function, and has been implicated in skeletal MYOGENESIS; NEURAL CREST migration and proliferation, lymphocyte maturation and morphogenesis of the PLACENTA and HEART.Receptors, Fibronectin: Specific cell surface receptors which bind to FIBRONECTINS. Studies have shown that these receptors function in certain types of adhesive contact as well as playing a major role in matrix assembly. These receptors include the traditional fibronectin receptor, also called INTEGRIN ALPHA5BETA1 and several other integrins.Integrin alpha5beta1: An integrin found in FIBROBLASTS; PLATELETS; MONOCYTES, and LYMPHOCYTES. Integrin alpha5beta1 is the classical receptor for FIBRONECTIN, but it also functions as a receptor for LAMININ and several other EXTRACELLULAR MATRIX PROTEINS.Integrin alpha Chains: The alpha subunits of integrin heterodimers (INTEGRINS), which mediate ligand specificity. There are approximately 18 different alpha chains, exhibiting great sequence diversity; several chains are also spliced into alternative isoforms. They possess a long extracellular portion (1200 amino acids) containing a MIDAS (metal ion-dependent adhesion site) motif, and seven 60-amino acid tandem repeats, the last 4 of which form EF HAND MOTIFS. The intracellular portion is short with the exception of INTEGRIN ALPHA4.Integrin alpha5: This integrin alpha subunit combines with INTEGRIN BETA1 to form a receptor (INTEGRIN ALPHA5BETA1) that binds FIBRONECTIN and LAMININ. It undergoes posttranslational cleavage into a heavy and a light chain that are connected by disulfide bonds.Vitronectin: A blood plasma glycoprotein that mediates cell adhesion and interacts with proteins of the complement, coagulation, and fibrinolytic cascade. (From Segen, Dictionary of Modern Medicine, 1992)Cell Movement: The movement of cells from one location to another. Distinguish from CYTOKINESIS which is the process of dividing the CYTOPLASM of a cell.Integrin alpha3: An integrin alpha subunit that occurs as alternatively spliced isoforms. The isoforms are differentially expressed in specific cell types and at specific developmental stages. Integrin alpha3 combines with INTEGRIN BETA1 to form INTEGRIN ALPHA3BETA1 which is a heterodimer found primarily in epithelial cells.Laminin: Large, noncollagenous glycoprotein with antigenic properties. It is localized in the basement membrane lamina lucida and functions to bind epithelial cells to the basement membrane. Evidence suggests that the protein plays a role in tumor invasion.Extracellular Matrix: A meshwork-like substance found within the extracellular space and in association with the basement membrane of the cell surface. It promotes cellular proliferation and provides a supporting structure to which cells or cell lysates in culture dishes adhere.Integrin alpha1beta1: Integrin alpha1beta1 functions as a receptor for LAMININ and COLLAGEN. It is widely expressed during development, but in the adult is the predominant laminin receptor (RECEPTORS, LAMININ) in mature SMOOTH MUSCLE CELLS, where it is important for maintenance of the differentiated phenotype of these cells. Integrin alpha1beta1 is also found in LYMPHOCYTES and microvascular endothelial cells, and may play a role in angiogenesis. In SCHWANN CELLS and neural crest cells, it is involved in cell migration. Integrin alpha1beta1 is also known as VLA-1 and CD49a-CD29.Integrin alpha6: An integrin alpha subunit that primarily associates with INTEGRIN BETA1 or INTEGRIN BETA4 to form laminin-binding heterodimers. Integrin alpha6 has two alternatively spliced isoforms: integrin alpha6A and integrin alpha6B, which differ in their cytoplasmic domains and are regulated in a tissue-specific and developmental stage-specific manner.Talin: A 235-kDa cytoplasmic protein that is also found in platelets. It has been localized to regions of cell-substrate adhesion. It binds to INTEGRINS; VINCULIN; and ACTINS and appears to participate in generating a transmembrane connection between the extracellular matrix and the cytoskeleton.Oligopeptides: Peptides composed of between two and twelve amino acids.Cell Adhesion Molecules: Surface ligands, usually glycoproteins, that mediate cell-to-cell adhesion. Their functions include the assembly and interconnection of various vertebrate systems, as well as maintenance of tissue integration, wound healing, morphogenic movements, cellular migrations, and metastasis.Receptors, Collagen: Collagen receptors are cell surface receptors that modulate signal transduction between cells and the EXTRACELLULAR MATRIX. They are found in many cell types and are involved in the maintenance and regulation of cell shape and behavior, including PLATELET ACTIVATION and aggregation, through many different signaling pathways and differences in their affinities for collagen isoforms. Collagen receptors include discoidin domain receptors, INTEGRINS, and glycoprotein VI.Lymphocyte Function-Associated Antigen-1: An integrin heterodimer widely expressed on cells of hematopoietic origin. CD11A ANTIGEN comprises the alpha chain and the CD18 antigen (ANTIGENS, CD18) the beta chain. Lymphocyte function-associated antigen-1 is a major receptor of T-CELLS; B-CELLS; and GRANULOCYTES. It mediates the leukocyte adhesion reactions underlying cytolytic conjugate formation, helper T-cell interactions, and antibody-dependent killing by NATURAL KILLER CELLS and granulocytes. Intracellular adhesion molecule-1 has been defined as a ligand for lymphocyte function-associated antigen-1.Macrophage-1 Antigen: An adhesion-promoting leukocyte surface membrane heterodimer. The alpha subunit consists of the CD11b ANTIGEN and the beta subunit the CD18 ANTIGEN. The antigen, which is an integrin, functions both as a receptor for complement 3 and in cell-cell and cell-substrate adhesive interactions.Integrin alpha2beta1: An integrin found on fibroblasts, platelets, endothelial and epithelial cells, and lymphocytes where it functions as a receptor for COLLAGEN and LAMININ. Although originally referred to as the collagen receptor, it is one of several receptors for collagen. Ligand binding to integrin alpha2beta1 triggers a cascade of intracellular signaling, including activation of p38 MAP kinase.Antigens, CD: Differentiation antigens residing on mammalian leukocytes. CD stands for cluster of differentiation, which refers to groups of monoclonal antibodies that show similar reactivity with certain subpopulations of antigens of a particular lineage or differentiation stage. The subpopulations of antigens are also known by the same CD designation.Signal Transduction: The intracellular transfer of information (biological activation/inhibition) through a signal pathway. In each signal transduction system, an activation/inhibition signal from a biologically active molecule (hormone, neurotransmitter) is mediated via the coupling of a receptor/enzyme to a second messenger system or to an ion channel. Signal transduction plays an important role in activating cellular functions, cell differentiation, and cell proliferation. Examples of signal transduction systems are the GAMMA-AMINOBUTYRIC ACID-postsynaptic receptor-calcium ion channel system, the receptor-mediated T-cell activation pathway, and the receptor-mediated activation of phospholipases. Those coupled to membrane depolarization or intracellular release of calcium include the receptor-mediated activation of cytotoxic functions in granulocytes and the synaptic potentiation of protein kinase activation. Some signal transduction pathways may be part of larger signal transduction pathways; for example, protein kinase activation is part of the platelet activation signal pathway.Cells, Cultured: Cells propagated in vitro in special media conducive to their growth. Cultured cells are used to study developmental, morphologic, metabolic, physiologic, and genetic processes, among others.Integrin alpha2: An integrin alpha subunit that primarily combines with INTEGRIN BETA1 to form the INTEGRIN ALPHA2BETA1 heterodimer. It contains a domain which has homology to collagen-binding domains found in von Willebrand factor.Antigens, CD11: A group of three different alpha chains (CD11a, CD11b, CD11c) that are associated with an invariant CD18 beta chain (ANTIGENS, CD18). The three resulting leukocyte-adhesion molecules (RECEPTORS, LEUKOCYTE ADHESION) are LYMPHOCYTE FUNCTION-ASSOCIATED ANTIGEN-1; MACROPHAGE-1 ANTIGEN; and ANTIGEN, P150,95.Receptors, Lymphocyte Homing: Cell surface glycoproteins on lymphocytes and other leukocytes that mediate adhesion to specialized blood vessels called high endothelial venules. Several different classes of lymphocyte homing receptors have been identified, and they appear to target different surface molecules (addressins) on high endothelial venules in different tissues. The adhesion plays a crucial role in the trafficking of lymphocytes.Extracellular Matrix Proteins: Macromolecular organic compounds that contain carbon, hydrogen, oxygen, nitrogen, and usually, sulfur. These macromolecules (proteins) form an intricate meshwork in which cells are embedded to construct tissues. Variations in the relative types of macromolecules and their organization determine the type of extracellular matrix, each adapted to the functional requirements of the tissue. The two main classes of macromolecules that form the extracellular matrix are: glycosaminoglycans, usually linked to proteins (proteoglycans), and fibrous proteins (e.g., COLLAGEN; ELASTIN; FIBRONECTINS; and LAMININ).Focal Adhesion Protein-Tyrosine Kinases: A family of non-receptor, PROLINE-rich protein-tyrosine kinases.Antigens, CD151: Tetraspanin proteins found associated with LAMININ-binding INTEGRINS. The CD151 antigens may play a role in the regulation of CELL MOTILITY.Integrin alpha6beta4: This intrgrin is a key component of HEMIDESMOSOMES and is required for their formation and maintenance in epithelial cells. Integrin alpha6beta4 is also found on thymocytes, fibroblasts, and Schwann cells, where it functions as a laminin receptor (RECEPTORS, LAMININ) and is involved in wound healing, cell migration, and tumor invasiveness.Protein Binding: The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.Antibodies, Monoclonal: Antibodies produced by a single clone of cells.Receptors, Cytoadhesin: A group of INTEGRINS that includes the platelet outer membrane glycoprotein GPIIb-IIIa (PLATELET GLYCOPROTEIN GPIIB-IIIA COMPLEX) and the vitronectin receptor (RECEPTORS, VITRONECTIN). They play a major role in cell adhesion and serve as receptors for fibronectin, von Willebrand factor, and vitronectin.Focal Adhesion Kinase 1: A non-receptor protein tyrosine kinase that is localized to FOCAL ADHESIONS and is a central component of integrin-mediated SIGNAL TRANSDUCTION PATHWAYS. Focal adhesion kinase 1 interacts with PAXILLIN and undergoes PHOSPHORYLATION in response to adhesion of cell surface integrins to the EXTRACELLULAR MATRIX. Phosphorylated p125FAK protein binds to a variety of SH2 DOMAIN and SH3 DOMAIN containing proteins and helps regulate CELL ADHESION and CELL MIGRATION.Focal Adhesions: An anchoring junction of the cell to a non-cellular substrate. It is composed of a specialized area of the plasma membrane where bundles of the ACTIN CYTOSKELETON terminate and attach to the transmembrane linkers, INTEGRINS, which in turn attach through their extracellular domains to EXTRACELLULAR MATRIX PROTEINS.Ligands: A molecule that binds to another molecule, used especially to refer to a small molecule that binds specifically to a larger molecule, e.g., an antigen binding to an antibody, a hormone or neurotransmitter binding to a receptor, or a substrate or allosteric effector binding to an enzyme. Ligands are also molecules that donate or accept a pair of electrons to form a coordinate covalent bond with the central metal atom of a coordination complex. (From Dorland, 27th ed)Antigens, CD11a: An alpha-integrin subunit found on lymphocytes, granulocytes, macrophages and monocytes. It combines with the integrin beta2 subunit (CD18 ANTIGEN) to form LYMPHOCYTE FUNCTION-ASSOCIATED ANTIGEN-1.Integrin beta4: Also known as CD104 antigen, this protein is distinguished from other beta integrins by its relatively long cytoplasmic domain (approximately 1000 amino acids vs. approximately 50). Five alternatively spliced isoforms have been described.Receptors, Very Late Antigen: Members of the integrin family appearing late after T-cell activation. They are a family of proteins initially identified at the surface of stimulated T-cells, but now identified on a variety of cell types. At least six VLA antigens have been identified as heterodimeric adhesion receptors consisting of a single common beta-subunit and different alpha-subunits.Cytoskeleton: The network of filaments, tubules, and interconnecting filamentous bridges which give shape, structure, and organization to the cytoplasm.Collagen: A polypeptide substance comprising about one third of the total protein in mammalian organisms. It is the main constituent of SKIN; CONNECTIVE TISSUE; and the organic substance of bones (BONE AND BONES) and teeth (TOOTH).Receptors, Laminin: Glycoprotein molecules on the surface of cells that react with or bind to laminin whose function allows the binding of epithelial cells to the basement membrane. The molecular weight of this high-affinity receptor is 67 kD.Cell Line: Established cell cultures that have the potential to propagate indefinitely.Paxillin: Paxillin is a signal transducing adaptor protein that localizes to FOCAL ADHESIONS via its four LIM domains. It undergoes PHOSPHORYLATION in response to integrin-mediated CELL ADHESION, and interacts with a variety of proteins including VINCULIN; FOCAL ADHESION KINASE; PROTO-ONCOGENE PROTEIN PP60(C-SRC); and PROTO-ONCOGENE PROTEIN C-CRK.Amino Acid Sequence: The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.Integrin alphaXbeta2: A major adhesion-associated heterodimer molecule expressed by MONOCYTES; GRANULOCYTES; NK CELLS; and some LYMPHOCYTES. The alpha subunit is the CD11C ANTIGEN, a surface antigen expressed on some myeloid cells. The beta subunit is the CD18 ANTIGEN.Molecular Sequence Data: Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.Receptors, Leukocyte-Adhesion: Family of proteins associated with the capacity of LEUKOCYTES to adhere to each other and to certain substrata, e.g., the C3bi component of complement. Members of this family are the LYMPHOCYTE FUNCTION-ASSOCIATED ANTIGEN-1; (LFA-1), the MACROPHAGE-1 ANTIGEN; (Mac-1), and the INTEGRIN ALPHAXBETA2 or p150,95 leukocyte adhesion protein. They all share a common beta-subunit which is the CD18 antigen. All three of the above antigens are absent in inherited LEUKOCYTE-ADHESION DEFICIENCY SYNDROME, which is characterized by recurrent bacterial infections, impaired pus formation, and wound healing as well as abnormalities in a wide spectrum of adherence-dependent functions of granulocytes, monocytes, and lymphoid cells.CHO Cells: CELL LINE derived from the ovary of the Chinese hamster, Cricetulus griseus (CRICETULUS). The species is a favorite for cytogenetic studies because of its small chromosome number. The cell line has provided model systems for the study of genetic alterations in cultured mammalian cells.Platelet Glycoprotein GPIIb-IIIa Complex: Platelet membrane glycoprotein complex important for platelet adhesion and aggregation. It is an integrin complex containing INTEGRIN ALPHAIIB and INTEGRIN BETA3 which recognizes the arginine-glycine-aspartic acid (RGD) sequence present on several adhesive proteins. As such, it is a receptor for FIBRINOGEN; VON WILLEBRAND FACTOR; FIBRONECTIN; VITRONECTIN; and THROMBOSPONDINS. A deficiency of GPIIb-IIIa results in GLANZMANN THROMBASTHENIA.Platelet Membrane Glycoproteins: Surface glycoproteins on platelets which have a key role in hemostasis and thrombosis such as platelet adhesion and aggregation. Many of these are receptors.Leukocyte-Adhesion Deficiency Syndrome: Rare, autosomal recessive disorder caused by deficiency of the beta 2 integrin receptors (RECEPTORS, LEUKOCYTE-ADHESION) comprising the CD11/CD18 family of glycoproteins. The syndrome is characterized by abnormal adhesion-dependent functions, especially defective tissue emigration of neutrophils, leading to recurrent infection.Neutrophils: Granular leukocytes having a nucleus with three to five lobes connected by slender threads of chromatin, and cytoplasm containing fine inconspicuous granules and stainable by neutral dyes.Vascular Cell Adhesion Molecule-1: Cytokine-induced cell adhesion molecule present on activated endothelial cells, tissue macrophages, dendritic cells, bone marrow fibroblasts, myoblasts, and myotubes. It is important for the recruitment of leukocytes to sites of inflammation. (From Pigott & Power, The Adhesion Molecule FactsBook, 1993, p154)Antigens, CD9: A subtype of tetraspanin proteins that play a role in cell adhesion, cell motility, and tumor metastasis. CD9 antigens take part in the process of platelet activation and aggregation, the formation of paranodal junctions in neuronal tissue, and the fusion of sperm with egg.Disintegrins: A family of polypeptides purified from snake venoms, which contain the arginine-glycine-aspartic acid (RGD) sequence. The RGD tripeptide binds to integrin receptors and thus competitively inhibits normal integrin-ligand interactions. Disintegrins thus block adhesive functions and act as platelet aggregation inhibitors.Endothelium, Vascular: Single pavement layer of cells which line the luminal surface of the entire vascular system and regulate the transport of macromolecules and blood components.Actins: Filamentous proteins that are the main constituent of the thin filaments of muscle fibers. The filaments (known also as filamentous or F-actin) can be dissociated into their globular subunits; each subunit is composed of a single polypeptide 375 amino acids long. This is known as globular or G-actin. In conjunction with MYOSINS, actin is responsible for the contraction and relaxation of muscle.Flow Cytometry: Technique using an instrument system for making, processing, and displaying one or more measurements on individual cells obtained from a cell suspension. Cells are usually stained with one or more fluorescent dyes specific to cell components of interest, e.g., DNA, and fluorescence of each cell is measured as it rapidly transverses the excitation beam (laser or mercury arc lamp). Fluorescence provides a quantitative measure of various biochemical and biophysical properties of the cell, as well as a basis for cell sorting. Other measurable optical parameters include light absorption and light scattering, the latter being applicable to the measurement of cell size, shape, density, granularity, and stain uptake.Cricetinae: A subfamily in the family MURIDAE, comprising the hamsters. Four of the more common genera are Cricetus, CRICETULUS; MESOCRICETUS; and PHODOPUS.Intercellular Adhesion Molecule-1: A cell-surface ligand involved in leukocyte adhesion and inflammation. Its production is induced by gamma-interferon and it is required for neutrophil migration into inflamed tissue.Protein Structure, Tertiary: The level of protein structure in which combinations of secondary protein structures (alpha helices, beta sheets, loop regions, and motifs) pack together to form folded shapes called domains. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure. Small proteins usually consist of only one domain but larger proteins may contain a number of domains connected by segments of polypeptide chain which lack regular secondary structure.Vinculin: A cytoskeletal protein associated with cell-cell and cell-matrix interactions. The amino acid sequence of human vinculin has been determined. The protein consists of 1066 amino acid residues and its gene has been assigned to chromosome 10.Tumor Cells, Cultured: Cells grown in vitro from neoplastic tissue. If they can be established as a TUMOR CELL LINE, they can be propagated in cell culture indefinitely.Protein-Tyrosine Kinases: Protein kinases that catalyze the PHOSPHORYLATION of TYROSINE residues in proteins with ATP or other nucleotides as phosphate donors.Cell-Matrix Junctions: Specialized areas at the CELL MEMBRANE where a cell attaches to the EXTRACELLULAR MATRIX or other substratum.Antibodies: Immunoglobulin molecules having a specific amino acid sequence by virtue of which they interact only with the ANTIGEN (or a very similar shape) that induced their synthesis in cells of the lymphoid series (especially PLASMA CELLS).Leukocytes: White blood cells. These include granular leukocytes (BASOPHILS; EOSINOPHILS; and NEUTROPHILS) as well as non-granular leukocytes (LYMPHOCYTES and MONOCYTES).Basement Membrane: A darkly stained mat-like EXTRACELLULAR MATRIX (ECM) that separates cell layers, such as EPITHELIUM from ENDOTHELIUM or a layer of CONNECTIVE TISSUE. The ECM layer that supports an overlying EPITHELIUM or ENDOTHELIUM is called basal lamina. Basement membrane (BM) can be formed by the fusion of either two adjacent basal laminae or a basal lamina with an adjacent reticular lamina of connective tissue. BM, composed mainly of TYPE IV COLLAGEN; glycoprotein LAMININ; and PROTEOGLYCAN, provides barriers as well as channels between interacting cell layers.Fluorescent Antibody Technique: Test for tissue antigen using either a direct method, by conjugation of antibody with fluorescent dye (FLUORESCENT ANTIBODY TECHNIQUE, DIRECT) or an indirect method, by formation of antigen-antibody complex which is then labeled with fluorescein-conjugated anti-immunoglobulin antibody (FLUORESCENT ANTIBODY TECHNIQUE, INDIRECT). The tissue is then examined by fluorescence microscopy.Fibroblasts: Connective tissue cells which secrete an extracellular matrix rich in collagen and other macromolecules.Mice, Knockout: Strains of mice in which certain GENES of their GENOMES have been disrupted, or "knocked-out". To produce knockouts, using RECOMBINANT DNA technology, the normal DNA sequence of the gene being studied is altered to prevent synthesis of a normal gene product. Cloned cells in which this DNA alteration is successful are then injected into mouse EMBRYOS to produce chimeric mice. The chimeric mice are then bred to yield a strain in which all the cells of the mouse contain the disrupted gene. Knockout mice are used as EXPERIMENTAL ANIMAL MODELS for diseases (DISEASE MODELS, ANIMAL) and to clarify the functions of the genes.Fibrinogen: Plasma glycoprotein clotted by thrombin, composed of a dimer of three non-identical pairs of polypeptide chains (alpha, beta, gamma) held together by disulfide bonds. Fibrinogen clotting is a sol-gel change involving complex molecular arrangements: whereas fibrinogen is cleaved by thrombin to form polypeptides A and B, the proteolytic action of other enzymes yields different fibrinogen degradation products.Transfection: The uptake of naked or purified DNA by CELLS, usually meaning the process as it occurs in eukaryotic cells. It is analogous to bacterial transformation (TRANSFORMATION, BACTERIAL) and both are routinely employed in GENE TRANSFER TECHNIQUES.Cytoskeletal Proteins: Major constituent of the cytoskeleton found in the cytoplasm of eukaryotic cells. They form a flexible framework for the cell, provide attachment points for organelles and formed bodies, and make communication between parts of the cell possible.rap1 GTP-Binding Proteins: A genetically related subfamily of RAP GTP-BINDING PROTEINS that share homology with RAS PROTEINS. They bind to Ras effectors but do not activate them, therefore they may antagonize the effects of RAS PROTEINS. This enzyme was formerly listed as EC 3.6.1.47.Binding Sites: The parts of a macromolecule that directly participate in its specific combination with another molecule.Phosphorylation: The introduction of a phosphoryl group into a compound through the formation of an ester bond between the compound and a phosphorus moiety.Chemotaxis, Leukocyte: The movement of leukocytes in response to a chemical concentration gradient or to products formed in an immunologic reaction.Selectins: Transmembrane proteins consisting of a lectin-like domain, an epidermal growth factor-like domain, and a variable number of domains that are homologous to complement regulatory proteins. They are important cell adhesion molecules which help LEUKOCYTES attach to VASCULAR ENDOTHELIUM.Neutrophil Activation: The process in which the neutrophil is stimulated by diverse substances, resulting in degranulation and/or generation of reactive oxygen products, and culminating in the destruction of invading pathogens. The stimulatory substances, including opsonized particles, immune complexes, and chemotactic factors, bind to specific cell-surface receptors on the neutrophil.Cell Membrane: The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.Membrane Glycoproteins: Glycoproteins found on the membrane or surface of cells.Stress, Mechanical: A purely physical condition which exists within any material because of strain or deformation by external forces or by non-uniform thermal expansion; expressed quantitatively in units of force per unit area.Microscopy, Fluorescence: Microscopy of specimens stained with fluorescent dye (usually fluorescein isothiocyanate) or of naturally fluorescent materials, which emit light when exposed to ultraviolet or blue light. Immunofluorescence microscopy utilizes antibodies that are labeled with fluorescent dye.Endothelial Cells: Highly specialized EPITHELIAL CELLS that line the HEART; BLOOD VESSELS; and lymph vessels, forming the ENDOTHELIUM. They are polygonal in shape and joined together by TIGHT JUNCTIONS. The tight junctions allow for variable permeability to specific macromolecules that are transported across the endothelial layer.Precipitin Tests: Serologic tests in which a positive reaction manifested by visible CHEMICAL PRECIPITATION occurs when a soluble ANTIGEN reacts with its precipitins, i.e., ANTIBODIES that can form a precipitate.Recombinant Proteins: Proteins prepared by recombinant DNA technology.Cell Differentiation: Progressive restriction of the developmental potential and increasing specialization of function that leads to the formation of specialized cells, tissues, and organs.Tenascin: Hexameric extracellular matrix glycoprotein transiently expressed in many developing organs and often re-expressed in tumors. It is present in the central and peripheral nervous systems as well as in smooth muscle and tendons. (From Kreis & Vale, Guidebook to the Extracellular Matrix and Adhesion Proteins, 1993, p93)Cell Line, Tumor: A cell line derived from cultured tumor cells.src-Family Kinases: A PROTEIN-TYROSINE KINASE family that was originally identified by homology to the Rous sarcoma virus ONCOGENE PROTEIN PP60(V-SRC). They interact with a variety of cell-surface receptors and participate in intracellular signal transduction pathways. Oncogenic forms of src-family kinases can occur through altered regulation or expression of the endogenous protein and by virally encoded src (v-src) genes.Receptors, Urokinase Plasminogen Activator: An extracellular receptor specific for UROKINASE-TYPE PLASMINOGEN ACTIVATOR. It is attached to the cell membrane via a GLYCOSYLPHOSPHATIDYLINOSITOL LINKAGE and plays a role in the co-localization of urokinase-type plasminogen activator with PLASMINOGEN.Mechanotransduction, Cellular: The process by which cells convert mechanical stimuli into a chemical response. It can occur in both cells specialized for sensing mechanical cues such as MECHANORECEPTORS, and in parenchymal cells whose primary function is not mechanosensory.Models, Biological: Theoretical representations that simulate the behavior or activity of biological processes or diseases. For disease models in living animals, DISEASE MODELS, ANIMAL is available. Biological models include the use of mathematical equations, computers, and other electronic equipment.Keratinocytes: Epidermal cells which synthesize keratin and undergo characteristic changes as they move upward from the basal layers of the epidermis to the cornified (horny) layer of the skin. Successive stages of differentiation of the keratinocytes forming the epidermal layers are basal cell, spinous or prickle cell, and the granular cell.Recombinant Fusion Proteins: Recombinant proteins produced by the GENETIC TRANSLATION of fused genes formed by the combination of NUCLEIC ACID REGULATORY SEQUENCES of one or more genes with the protein coding sequences of one or more genes.Antibodies, Blocking: Antibodies that inhibit the reaction between ANTIGEN and other antibodies or sensitized T-LYMPHOCYTES (e.g., antibodies of the IMMUNOGLOBULIN G class that compete with IGE antibodies for antigen, thereby blocking an allergic response). Blocking antibodies that bind tumors and prevent destruction of tumor cells by CYTOTOXIC T-LYMPHOCYTES have also been called enhancing antibodies. (Rosen et al., Dictionary of Immunology, 1989)Cell Communication: Any of several ways in which living cells of an organism communicate with one another, whether by direct contact between cells or by means of chemical signals carried by neurotransmitter substances, hormones, and cyclic AMP.Cell Aggregation: The phenomenon by which dissociated cells intermixed in vitro tend to group themselves with cells of their own type.Collagen Type IV: A non-fibrillar collagen found in the structure of BASEMENT MEMBRANE. Collagen type IV molecules assemble to form a sheet-like network which is involved in maintaining the structural integrity of basement membranes. The predominant form of the protein is comprised of two alpha1(IV) subunits and one alpha2(IV) subunit, however, at least six different alpha subunits can be incorporated into the heterotrimer.Epithelial Cells: Cells that line the inner and outer surfaces of the body by forming cellular layers (EPITHELIUM) or masses. Epithelial cells lining the SKIN; the MOUTH; the NOSE; and the ANAL CANAL derive from ectoderm; those lining the RESPIRATORY SYSTEM and the DIGESTIVE SYSTEM derive from endoderm; others (CARDIOVASCULAR SYSTEM and LYMPHATIC SYSTEM) derive from mesoderm. Epithelial cells can be classified mainly by cell shape and function into squamous, glandular and transitional epithelial cells.Cytoplasm: The part of a cell that contains the CYTOSOL and small structures excluding the CELL NUCLEUS; MITOCHONDRIA; and large VACUOLES. (Glick, Glossary of Biochemistry and Molecular Biology, 1990)Up-Regulation: A positive regulatory effect on physiological processes at the molecular, cellular, or systemic level. At the molecular level, the major regulatory sites include membrane receptors, genes (GENE EXPRESSION REGULATION), mRNAs (RNA, MESSENGER), and proteins.Mice, Inbred C57BLK562 Cells: An ERYTHROLEUKEMIA cell line derived from a CHRONIC MYELOID LEUKEMIA patient in BLAST CRISIS.Receptor Aggregation: Chemically stimulated aggregation of cell surface receptors, which potentiates the action of the effector cell.Peptides: Members of the class of compounds composed of AMINO ACIDS joined together by peptide bonds between adjacent amino acids into linear, branched or cyclical structures. OLIGOPEPTIDES are composed of approximately 2-12 amino acids. Polypeptides are composed of approximately 13 or more amino acids. PROTEINS are linear polypeptides that are normally synthesized on RIBOSOMES.Immunohistochemistry: Histochemical localization of immunoreactive substances using labeled antibodies as reagents.Platelet Membrane Glycoprotein IIb: Platelet membrane glycoprotein IIb is an integrin alpha subunit that heterodimerizes with INTEGRIN BETA3 to form PLATELET GLYCOPROTEIN GPIIB-IIIA COMPLEX. It is synthesized as a single polypeptide chain which is then postranslationally cleaved and processed into two disulfide-linked subunits of approximately 18 and 110 kDa in size.Osteopontin: A negatively-charged extracellular matrix protein that plays a role in the regulation of BONE metabolism and a variety of other biological functions. Cell signaling by osteopontin may occur through a cell adhesion sequence that recognizes INTEGRIN ALPHA-V BETA-3.Antigens, CD98: A heterodimeric protein that is a cell surface antigen associated with lymphocyte activation. The initial characterization of this protein revealed one identifiable heavy chain (ANTIGENS, CD98 HEAVY CHAIN) and an indeterminate smaller light chain. It is now known that a variety of light chain subunits (ANTIGENS, CD98 LIGHT CHAINS) can dimerize with the heavy chain. Depending upon its light chain composition a diverse array of functions can be found for this protein. Functions include: type L amino acid transport, type y+L amino acid transport and regulation of cellular fusion.Receptors, Virus: Specific molecular components of the cell capable of recognizing and interacting with a virus, and which, after binding it, are capable of generating some signal that initiates the chain of events leading to the biological response.Blood Platelets: Non-nucleated disk-shaped cells formed in the megakaryocyte and found in the blood of all mammals. They are mainly involved in blood coagulation.Antigens, CD47: A ubiquitously expressed membrane glycoprotein. It interacts with a variety of INTEGRINS and mediates responses to EXTRACELLULAR MATRIX PROTEINS.L-Selectin: Cell adhesion molecule and CD antigen that serves as a homing receptor for lymphocytes to lymph node high endothelial venules.Cytochalasin D: A fungal metabolite that blocks cytoplasmic cleavage by blocking formation of contractile microfilament structures resulting in multinucleated cell formation, reversible inhibition of cell movement, and the induction of cellular extrusion. Additional reported effects include the inhibition of actin polymerization, DNA synthesis, sperm motility, glucose transport, thyroid secretion, and growth hormone release.Membrane Proteins: Proteins which are found in membranes including cellular and intracellular membranes. They consist of two types, peripheral and integral proteins. They include most membrane-associated enzymes, antigenic proteins, transport proteins, and drug, hormone, and lectin receptors.Wound Healing: Restoration of integrity to traumatized tissue.Monocytes: Large, phagocytic mononuclear leukocytes produced in the vertebrate BONE MARROW and released into the BLOOD; contain a large, oval or somewhat indented nucleus surrounded by voluminous cytoplasm and numerous organelles.Skin: The outer covering of the body that protects it from the environment. It is composed of the DERMIS and the EPIDERMIS.Umbilical Veins: Venous vessels in the umbilical cord. They carry oxygenated, nutrient-rich blood from the mother to the FETUS via the PLACENTA. In humans, there is normally one umbilical vein.Receptors, Cell Surface: Cell surface proteins that bind signalling molecules external to the cell with high affinity and convert this extracellular event into one or more intracellular signals that alter the behavior of the target cell (From Alberts, Molecular Biology of the Cell, 2nd ed, pp693-5). Cell surface receptors, unlike enzymes, do not chemically alter their ligands.Peptide Fragments: Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.Cell Division: The fission of a CELL. It includes CYTOKINESIS, when the CYTOPLASM of a cell is divided, and CELL NUCLEUS DIVISION.Enzyme Activation: Conversion of an inactive form of an enzyme to one possessing metabolic activity. It includes 1, activation by ions (activators); 2, activation by cofactors (coenzymes); and 3, conversion of an enzyme precursor (proenzyme or zymogen) to an active enzyme.N-Formylmethionine Leucyl-Phenylalanine: A formylated tripeptide originally isolated from bacterial filtrates that is positively chemotactic to polymorphonuclear leucocytes, and causes them to release lysosomal enzymes and become metabolically activated.Collagen Type I: The most common form of fibrillar collagen. It is a major constituent of bone (BONE AND BONES) and SKIN and consists of a heterotrimer of two alpha1(I) and one alpha2(I) chains.Tyrosine: A non-essential amino acid. In animals it is synthesized from PHENYLALANINE. It is also the precursor of EPINEPHRINE; THYROID HORMONES; and melanin.rhoA GTP-Binding Protein: A RHO GTP-BINDING PROTEIN involved in regulating signal transduction pathways that control assembly of focal adhesions and actin stress fibers. This enzyme was formerly listed as EC 3.6.1.47.Cadherins: Calcium-dependent cell adhesion proteins. They are important in the formation of ADHERENS JUNCTIONS between cells. Cadherins are classified by their distinct immunological and tissue specificities, either by letters (E- for epithelial, N- for neural, and P- for placental cadherins) or by numbers (cadherin-12 or N-cadherin 2 for brain-cadherin). Cadherins promote cell adhesion via a homophilic mechanism as in the construction of tissues and of the whole animal body.Syndecan-4: A ubiquitously expressed syndecan that is found in all stages of embryonic development and in most adult tissues. Syndecan-4 is found localized to focal adhesion sites in fibronectin-adherent cells and may play a role the process of CELL MIGRATION and CELL PROLIFERATION.Cricetulus: A genus of the family Muridae consisting of eleven species. C. migratorius, the grey or Armenian hamster, and C. griseus, the Chinese hamster, are the two species used in biomedical research.Neovascularization, Physiologic: The development of new BLOOD VESSELS during the restoration of BLOOD CIRCULATION during the healing process.Microscopy, Confocal: A light microscopic technique in which only a small spot is illuminated and observed at a time. An image is constructed through point-by-point scanning of the field in this manner. Light sources may be conventional or laser, and fluorescence or transmitted observations are possible.Antigens, CD11b: A CD antigen that contains a conserved I domain which is involved in ligand binding. When combined with CD18 the two subunits form MACROPHAGE-1 ANTIGEN.Gene Expression Regulation: Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control (induction or repression) of gene action at the level of transcription or translation.Jurkat Cells: A CELL LINE derived from human T-CELL LEUKEMIA and used to determine the mechanism of differential susceptibility to anti-cancer drugs and radiation.Actinin: A protein factor that regulates the length of R-actin. It is chemically similar, but immunochemically distinguishable from actin.Filamins: A family of crosslinking filament proteins encoded by distinct FLN genes. Filamins are involved in cell adhesion, spreading, and migration, acting as scaffolds for over 90 binding partners including channels, receptors, intracellular signaling molecules and transcription factors. Due to the range of molecular interactions, mutations in FLN genes result in anomalies with moderate to lethal consequences.Mutation: Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.Cell Polarity: Orientation of intracellular structures especially with respect to the apical and basolateral domains of the plasma membrane. Polarized cells must direct proteins from the Golgi apparatus to the appropriate domain since tight junctions prevent proteins from diffusing between the two domains.Focal Adhesion Kinase 2: A non-receptor protein-tyrosine kinase that is expressed primarily in the BRAIN; OSTEOBLASTS; and LYMPHOID CELLS. In the CENTRAL NERVOUS SYSTEM focal adhesion kinase 2 modulates ION CHANNEL function and MITOGEN-ACTIVATED PROTEIN KINASES activity.Coxsackie and Adenovirus Receptor-Like Membrane Protein: An Ig superfamily transmembrane protein that localizes to junctional complexes that occur between ENDOTHELIAL CELLS and EPTHELIAL CELLS. The protein may play a role in cell-cell adhesion and is the primary site for the attachment of ADENOVIRUSES during infection.Amino Acid Motifs: Commonly observed structural components of proteins formed by simple combinations of adjacent secondary structures. A commonly observed structure may be composed of a CONSERVED SEQUENCE which can be represented by a CONSENSUS SEQUENCE.T-Lymphocytes: Lymphocytes responsible for cell-mediated immunity. Two types have been identified - cytotoxic (T-LYMPHOCYTES, CYTOTOXIC) and helper T-lymphocytes (T-LYMPHOCYTES, HELPER-INDUCER). They are formed when lymphocytes circulate through the THYMUS GLAND and differentiate to thymocytes. When exposed to an antigen, they divide rapidly and produce large numbers of new T cells sensitized to that antigen.Microscopy, Video: Microscopy in which television cameras are used to brighten magnified images that are otherwise too dark to be seen with the naked eye. It is used frequently in TELEPATHOLOGY.Cell Culture Techniques: Methods for maintaining or growing CELLS in vitro.PhosphoproteinsLeukocyte Rolling: Movement of tethered, spherical LEUKOCYTES along the endothelial surface of the microvasculature. The tethering and rolling involves interaction with SELECTINS and other adhesion molecules in both the ENDOTHELIUM and leukocyte. The rolling leukocyte then becomes activated by CHEMOKINES, flattens out, and firmly adheres to the endothelial surface in preparation for transmigration through the interendothelial cell junction. (From Abbas, Cellular and Molecular Immunology, 3rd ed)Cell Size: The quantity of volume or surface area of CELLS.RNA, Messenger: RNA sequences that serve as templates for protein synthesis. Bacterial mRNAs are generally primary transcripts in that they do not require post-transcriptional processing. Eukaryotic mRNA is synthesized in the nucleus and must be exported to the cytoplasm for translation. Most eukaryotic mRNAs have a sequence of polyadenylic acid at the 3' end, referred to as the poly(A) tail. The function of this tail is not known for certain, but it may play a role in the export of mature mRNA from the nucleus as well as in helping stabilize some mRNA molecules by retarding their degradation in the cytoplasm.Gene Expression: The phenotypic manifestation of a gene or genes by the processes of GENETIC TRANSCRIPTION and GENETIC TRANSLATION.Actin Cytoskeleton: Fibers composed of MICROFILAMENT PROTEINS, which are predominately ACTIN. They are the smallest of the cytoskeletal filaments.Blotting, Western: Identification of proteins or peptides that have been electrophoretically separated by blot transferring from the electrophoresis gel to strips of nitrocellulose paper, followed by labeling with antibody probes.Snake Venoms: Solutions or mixtures of toxic and nontoxic substances elaborated by snake (Ophidia) salivary glands for the purpose of killing prey or disabling predators and delivered by grooved or hollow fangs. They usually contain enzymes, toxins, and other factors.rho GTP-Binding Proteins: A large family of MONOMERIC GTP-BINDING PROTEINS that are involved in regulation of actin organization, gene expression and cell cycle progression. This enzyme was formerly listed as EC 3.6.1.47.Morphogenesis: The development of anatomical structures to create the form of a single- or multi-cell organism. Morphogenesis provides form changes of a part, parts, or the whole organism.Antigens, CD98 Heavy Chain: A transmembrane glycoprotein subunit that can dimerize with a variety of light chain subunits (ANTIGENS, CD98 LIGHT CHAINS). This protein subunit serves a diverse array of functions including amino acid transport and cell fusion. Its function is altered depending which of the light chain subunits it interacts with.Mucoproteins: Conjugated proteins in which mucopolysaccharides are combined with proteins. The mucopolysaccharide moiety is the predominant group with the protein making up only a small percentage of the total weight.Viper Venoms: Venoms from SNAKES of the viperid family. They tend to be less toxic than elapid or hydrophid venoms and act mainly on the vascular system, interfering with coagulation and capillary membrane integrity and are highly cytotoxic. They contain large amounts of several enzymes, other factors, and some toxins.

Primary haemostasis: sticky fingers cement the relationship. (1/5403)

Platelet aggregation to form a haemostatic plug, or thrombus, plays a key role in preventing bleeding from a wound. Recent studies have provided new insights into how platelet receptors are deployed during the interactions with the vascular subendothelial matrix that lead to haemostatic plug formation.  (+info)

The LIM-only protein PINCH directly interacts with integrin-linked kinase and is recruited to integrin-rich sites in spreading cells. (2/5403)

PINCH is a widely expressed and evolutionarily conserved protein comprising primarily five LIM domains, which are cysteine-rich consensus sequences implicated in mediating protein-protein interactions. We report here that PINCH is a binding protein for integrin-linked kinase (ILK), an intracellular serine/threonine protein kinase that plays important roles in the cell adhesion, growth factor, and Wnt signaling pathways. The interaction between ILK and PINCH has been consistently observed under a variety of experimental conditions. They have interacted in yeast two-hybrid assays, in solution, and in solid-phase-based binding assays. Furthermore, ILK, but not vinculin or focal adhesion kinase, has been coisolated with PINCH from mammalian cells by immunoaffinity chromatography, indicating that PINCH and ILK associate with each other in vivo. The PINCH-ILK interaction is mediated by the N-terminal-most LIM domain (LIM1, residues 1 to 70) of PINCH and multiple ankyrin (ANK) repeats located within the N-terminal domain (residues 1 to 163) of ILK. Additionally, biochemical studies indicate that ILK, through the interaction with PINCH, is capable of forming a ternary complex with Nck-2, an SH2/SH3-containing adapter protein implicated in growth factor receptor kinase and small GTPase signaling pathways. Finally, we have found that PINCH is concentrated in peripheral ruffles of cells spreading on fibronectin and have detected clusters of PINCH that are colocalized with the alpha5beta1 integrins. These results demonstrate a specific protein recognition mechanism utilizing a specific LIM domain and multiple ANK repeats and suggest that PINCH functions as an adapter protein connecting ILK and the integrins with components of growth factor receptor kinase and small GTPase signaling pathways.  (+info)

Blocking very late antigen-4 integrin decreases leukocyte entry and fatty streak formation in mice fed an atherogenic diet. (3/5403)

Atherosclerotic lesion development is characterized by the recruitment of leukocytes, principally monocytes, to the vessel wall. Considerable interest has been focused on the adhesion molecule(s) involved in leukocyte/endothelial interactions. The goal of the present study was to determine the role of the very late antigen-4 (VLA-4) integrin/ligand interaction in fatty streak development using murine models. Because alpha4 null mice are not viable, a peptidomimetic was used to block VLA-4-mediated leukocyte binding. The ability of a synthetic peptidomimetic of connecting segment-1 (CS-1 peptide) to block the recruitment of leukocytes and the accumulation of lipid in the aortic sinus of either wild-type mice (strain C57BL/6J) or mice with a low-density lipoprotein null mutation (LDLR-/-) maintained on an atherogenic diet was assessed. The active (Ac) CS-1 peptide or scrambled (Sc) CS-1 peptide was delivered subcutaneously into mice using a mini osmotic pump. Mice were exposed to the peptide for 24 to 36 hours before the onset of the atherogenic diet. In C57BL/6J mice, leukocyte entry into the aortic sinus, as assessed by en face preparations, was inhibited by the active peptide (Ac=28+/-4, Sc=54+/-6 monocytes/valve; P=0.004). Additionally, frozen sections stained with Oil Red O were analyzed to assess lipid accumulation in the aortic sinus. C57BL/6J mice that received the (Ac) compound demonstrated significantly reduced lesion areas as compared with mice that received the (Sc) peptide (Ac=4887+/-4438 microm2, Sc=15 009 +/-5619 microm2; P<0.0001). In a separate study, LDLR-/- mice were implanted with pumps containing either the (Ac) or (Sc) peptide before initiation of the atherogenic diet. Because LDLR-/- mice fed a chow diet displayed small lesions at 14 weeks, the effects of the peptide seen in these animals represented a change in early lipid accumulation rather than initiation. By using whole-mount preparations, the (Ac) but not the (Sc) peptide significantly reduced the area of lipid accumulation in the aortic sinus, resulting in an approximate 66% decrease. Plasma analysis from all studies revealed concentrations of peptide to be present at levels previously determined by in vitro analysis to block adhesion. (Ac) CS-1 peptide, which blocks VLA-4 on the leukocyte surface, is effective in reducing leukocyte recruitment and lipid accumulation in the aortic sinus. The present study provides in vivo evidence that the VLA-4 integrin plays an important role in the initiation of the atherosclerotic lesion and lipid accumulation, and it suggests a potential therapeutic strategy for this disease.  (+info)

Integrin subunit gene expression is regionally differentiated in adult brain. (4/5403)

Integrins are a diverse family of heterodimeric (alphabeta) adhesion receptors recently shown to be concentrated within synapses and involved in the consolidation of long-term potentiation. Whether neuronal types or anatomical systems in the adult rat brain are coded by integrin type was studied in the present experiments by mapping the relative densities of mRNAs for nine alpha and four beta subunits. Expression patterns were markedly different and in some regions complementary. General results and areas of notable labeling were as follows: alpha1-limited neuronal expression, neocortical layer V, hippocampal CA3; alpha3 and alpha5-diffuse neuronal and glial labeling, Purkinje cells, hippocampal stratum pyramidale, locus coeruleus (alpha3); alpha4- discrete limbic regions, olfactory cortical layer II, hippocampal CA2; alpha6-most prominently neuronal, neocortical subplate, endopiriform, subiculum; alpha7-discrete, all neocortical layers, hippocampal granule cells and CA3, cerebellar granule and Purkinje cells, all efferent cranial nerve nuclei; alpha8-discrete neuronal, deep cortex, hippocampal CA1, basolateral amygdala, striatum; alphaV-all cortical layers, striatum, Purkinje cells; beta4-dentate gyrus granule cells; beta5-broadly distributed, neocortex, medial amygdala, cerebellar granule and Purkinje cells, efferent cranial nerve nuclei; alpha2, beta2, and beta3-mRNAs not detected. These results establish that brain subfields express different balances of integrin subunits and thus different integrin receptors. Such variations will determine which matrix proteins are recognized by neurons and the types of intraneuronal signaling generated by matrix binding. They also could generate important differences in synaptic plasticity across brain systems.  (+info)

The integrin alpha v beta 6 binds and activates latent TGF beta 1: a mechanism for regulating pulmonary inflammation and fibrosis. (5/5403)

Transforming growth factor beta (TGF beta) family members are secreted in inactive complexes with a latency-associated peptide (LAP), a protein derived from the N-terminal region of the TGF beta gene product. Extracellular activation of these complexes is a critical but incompletely understood step in regulation of TGF beta function in vivo. We show that TGF beta 1 LAP is a ligand for the integrin alpha v beta 6 and that alpha v beta 6-expressing cells induce spatially restricted activation of TGF beta 1. This finding explains why mice lacking this integrin develop exaggerated inflammation and, as we show, are protected from pulmonary fibrosis. These data identify a novel mechanism for locally regulating TGF beta 1 function in vivo by regulating expression of the alpha v beta 6 integrin.  (+info)

Cell adhesion regulates the interaction between the docking protein p130(Cas) and the 14-3-3 proteins. (6/5403)

Integrin ligand binding induces a signaling complex formation via the direct association of the docking protein p130(Cas) (Cas) with diverse molecules. We report here that the 14-3-3zeta protein interacts with Cas in the yeast two-hybrid assay. We also found that the two proteins associate in mammalian cells and that this interaction takes place in a phosphoserine-dependent manner, because treatment of Cas with a serine phosphatase greatly reduced its ability to bind 14-3-3zeta. Furthermore, the Cas-14-3-3zeta interaction was found to be regulated by integrin-mediated cell adhesion. Thus, when cells are detached from the extracellular matrix, the binding of Cas to 14-3-3zeta is greatly diminished, whereas replating the cells onto fibronectin rapidly induces the association. Consistent with these results, we found that the subcellular localization of Cas and 14-3-3 is also regulated by integrin ligand binding and that the two proteins display a significant co-localization during cell attachment to the extracellular matrix. In conclusion, our results demonstrate that 14-3-3 proteins participate in integrin-activated signaling pathways through their interaction with Cas, which, in turn, may contribute to important biological responses regulated by cell adhesion to the extracellular matrix.  (+info)

Tyrosine phosphorylation of SLP-76 is downstream of Syk following stimulation of the collagen receptor in platelets. (7/5403)

Collagen-related peptide (CRP), a collagen homologue, induces platelet activation through a tyrosine kinase-dependent pathway, leading to sequential tyrosine phosphorylation of Fc receptor (FcR) gamma-chain, Syk, and phospholipase C-gamma2. Here we report that CRP and the platelet low affinity immune receptor FcgammaRIIA stimulate tyrosine phosphorylation of the T cell adapter SLP-76, whereas the G protein-coupled receptor agonist thrombin induces only minor tyrosine phosphorylation. This suggests that SLP-76 has a specific role downstream of receptors that signal via an immunoreceptor tyrosine-based activation motif. Immunoprecipitation studies demonstrate association of SLP-76 with SLAP-130, Vav, Fyn, Lyn, and the FcR gamma-chain in CRP-stimulated platelets. Several of these proteins, including SLP-76, undergo tyrosine phosphorylation in in vitro kinase assays performed on SLP-76 immunoprecipitates. Tyrosine phosphorylation of all of these proteins in the in vitro kinase assay was abrogated by the Src family kinase inhibitor PP1, suggesting that it is mediated by either Fyn or Lyn. The physiological significance of this is uncertain, however, since tyrosine phosphorylation of SLP-76 in vivo is not altered in either Fyn- or Lyn-deficient platelets. CRP stimulation of Syk-deficient platelets demonstrated that in vivo tyrosine phosphorylation of SLP-76 is downstream of Syk. The absence of Syk in the SLP-76 immunoprecipitates raises the possibility that another protein is responsible for bringing SLP-76 to Syk. Candidates for this include those proteins that co-immunoprecipitate with SLP-76, including the FcR gamma-chain. Tyrosine phosphorylation of PLC-gamma2 and Ca2+ mobilization is markedly attenuated in SLP-76-deficient platelets following CRP stimulation, suggesting that the adapter plays a critical role in the regulation of the phospholipase. The increase in tyrosine phosphorylation of SLAP-130 in response to CRP is also inhibited in SLP-76-deficient platelets, placing it downstream of SLP-76. This work identifies SLP-76 as an important adapter molecule that is regulated by Syk and lies upstream of SLAP-130 and PLC-gamma2 in CRP-stimulated platelets.  (+info)

Expression pattern of integrin adhesion molecules in endometriosis and human endometrium. (8/5403)

Integrins are cell adhesion molecules that undergo cell-specific dynamic changes during the normal menstrual cycle in the human endometrium. Here, using immunohistochemistry, we have investigated the expression pattern of the integrins alphav, alpha2beta1, alpha3beta1, alpha3, alpha6, beta1, beta2 and beta3 in the human ectopic endometrium of 30 patients and in nine cases in the corresponding eutopic endometrium. The biopsies were obtained during the early or late follicular phase (25 cases), during the corpus luteum phase (four cases) and in one case after 6 months' treatment with a gonadotrophin releasing hormone (GnRH) agonist. The integrin expression was independent of the ovarian steroid situation at the time of biopsy. The integrin alpha6 was expressed in all endometriotic and endometrium samples. The integrin alpha3 was absent in all endometrium tissues of patients with endometriosis. However, the corresponding endometriotic lesions re-expressed this adhesion molecule in 15 cases. No change in integrin beta3 expression pattern could be demonstrated in either endometriotic lesions or endometrium samples, regardless of the menstrual cycle phase. A correlation between serum oestradiol and progesterone concentrations and the expression of the investigated integrins was not observed, thus indicating that these two hormones play a minor role in the regulation of the cell adhesion molecules examined. Our investigation suggests that endometriosis is a dedifferentiated disease as it expressed different integrins in comparison with the eutopic endometrium, and independently of the hormonal situation. The ability of endometriotic tissues to express integrins may explain the high recurrence rates in patients with endometriosis, as these samples retain their adhesion potency after retrograde menstruation and are thus able to establish cell-cell and cell-matrix interactions with the surrounding peritoneum.  (+info)

ITAGV encodes integrin alpha chain V. Integrins are heterodimeric integral membrane proteins composed of an alpha chain and a beta chain. The I-domain containing integrin alpha V undergoes post-translational cleavage to yield disulfide-linked heavy and light chains, that combine with multiple integrin beta chains to form different integrins. Among the known associating beta chains (beta chains 1,3,5,6, and 8; ITGB1, ITGB3, ITGB5, ITGB6, and ITGB8), each can interact with extracellular matrix ligands; the alpha V beta 3 integrin, perhaps the most studied of these, is referred to as the Vitronectin receptor (VNR). In addition to adhesion, many integrins are known to facilitate signal transduction. The ITGB3 protein product is the integrin beta chain beta 3. Integrins are integral cell-surface proteins composed of an alpha chain and a beta chain. A given chain may combine with multiple partners resulting in different integrins. Integrin beta 3 is found along with the alpha IIb chain in ...
Leukocyte adhesion during hypoxia is mediated by HIF-1-dependent induction of beta2 integrin gene expression.s profile, publications, research topics, and co-authors
Integrin receptors regulate cell fate by coupling the binding of extracellular adhesion proteins to the assembly of intracellular cytoskeletal and signaling complexes. A detailed, integrative view of adhesion complexes will provide insight into the molecular mechanisms that control cell morphology, survival, movement, and differentiation. To date, membrane receptor-associated signaling complexes have been refractory to proteomic analysis because of their inherent lability and inaccessibility. We developed a methodology to isolate ligand-induced integrin adhesion complexes, and we used this technique to analyze the composition of complexes associated with multiple receptor-ligand pairs and define core and receptor-specific subnetworks. In particular, we identified regulator of chromosome condensation-2 (RCC2) as a component of fibronectin-activated signaling pathways that regulate directional cell movement. The development of this proteomics pipeline provides the means to investigate the ...
TY - JOUR. T1 - Subclassification, molecular structure, function and ligand in integrin superfamily. AU - Matsuura, N.. AU - Takada, Y.. PY - 1995/7. Y1 - 1995/7. N2 - Integrins are the major family of cell surface receptors that mediate adhesion to the extracellular matrix and sometimes cell-cell adhesive interactions. These integrin-mediated adhesive interactions are involved in the regulation of many cellular functions, including embryonic development, tumor cell growth and metastasis, programmed cell death, hemostasis, inflammation, immune reaction, bone reabsorption, etc. Integrins are composed of alpha and beta transmembrane subunits selected from among 16 alpha and 8 beta subunits that heterodimerize to produce more than 20 different receptors which bind specific ligands. Ligand binding sites have been clarified by chimera integrin protein in some integrins. Integrins link to intracellular cytoskeletal complexes and bundles of actin filaments. There have been many reports about ...
Adhesion of cells to extracellular matrix proteins is mediated, in large part, by transmembrane receptors of the integrin family. The identification of specific integrins expressed in early embryos is an important first step to understanding the roles of these receptors in developmental processes. We have used polymerase chain reaction methods and degenerate oligodeoxynucleotide primers to identify and clone Xenopus integrin alpha subunits from neurula-stage (stage 17) cDNA. Partial cDNAs encoding integrin subunits alpha 2, alpha 3, alpha 4, alpha 5, alpha 6 and an alpha IIb-related subunit were cloned and used to investigate integrin mRNA expression in early embryos by RNase protection assay and whole-mount in situ hybridization methods. Considerable integrin diversity is apparent early in development with integrins alpha 2, alpha 3, alpha 4, alpha 5 and alpha 6 each expressed by the end of gastrulation. Both alpha 3 and alpha 5 are expressed as maternal mRNAs. Zygotic expression of alpha 2, ...
alpha 4 integrins are cell surface receptors that mediate cell-extracellular matrix (ECM) and cell-cell adhesions by interacting with fibronectin (FN) and vascular cell adhesion molecule 1 (VCAM-1), respectively. We have generated a null mutation in the gene for the alpha 4 integrin subunit. Homozygous null embryos express no alpha 4 integrins and show two unexpected defects, both of which lead to embryonic lethality. The first defect is failure of fusion of the allantois with the chorion during placentation. The second is in the development of the epicardium and coronary vessels leading to cardiac hemorrhage. Both processes clearly involve alpha 4 integrin interactions that were previously unsuspected. alpha 4 integrin and VCAM-1 are expressed at the sites of these interactions. These results raise the possibility of abortifacients targeting alpha 4 integrins, and raise serious questions about potential side effects of drugs currently being designed to block alpha 4 integrin functions in ...
The product of this gene belongs to the integrin alpha chain family. Integrins are heterodimeric integral membrane proteins composed of an alpha subunit and a beta subunit that function in cell surface adhesion and signaling. The encoded preproprotein is proteolytically processed to generate light and heavy chains that comprise the alpha 5 subunit. This subunit associates with the beta 1 subunit to form a fibronectin receptor. This integrin may promote tumor invasion, and higher expression of this gene may be correlated with shorter survival time in lung cancer patients. Note that the integrin alpha 5 and integrin alpha V subunits are encoded by distinct genes. [provided by RefSeq, Oct 2015 ...
Integrin alpha-IIb is a protein that in humans is encoded by the ITGA2B gene. ITGA2B, also known as CD41, encodes integrin alpha chain 2b. Integrins are heterodimeric integral membrane proteins composed of an alpha chain and a beta chain. Alpha chain 2b undergoes post-translational cleavage to yield disulfide-linked light and heavy chains that join with beta 3 to form a fibrinogen receptor expressed in platelets that plays a crucial role in coagulation. Mutations that interfere with this role result in thrombasthenia. In addition to adhesion, integrins are known to participate in cell-surface mediated signalling.[5] ...
Integrins are cell adhesion receptors which mediate interactions between the extracellular matrix and the actin cytoskeleton. They are heterodimers composed of α and β subunits. As adhesion receptors, integrins are important for cell-cell and cell-matrix interactions and therefore are essential for the structural integrity of an organ. Moreover, integrin-extracellular matrix interactions play important roles in the coordinated integration of external and internal cues that are essential for proper development. β1 integrin is the most widely expressed integrin and controls various developmental processes, including neurogenesis, chondrogenesis, skin and hair follicle morphogenesis, and myoblast fusion. To determine the role of β1 integrin in normal development of the mouse mammary gland, with a particular emphasis on how β1 integrins influcence proliferation, differentiation and apoptosis; we examined the consequence of conditional deletion of β1 integrin in mammary epithelia. ...
Luo, B.-H., Carman, C.V. & Springer, T.A. Structural basis of integrin regulation and signaling. Annu Rev Immunol. 25, 619-47 (2007).
Integrin alpha 6 antibody [MP 4F10] (integrin, alpha 6) for FACS, IHC-Fr, IP. Anti-Integrin alpha 6 mAb (GTX40142) is tested in Human samples. 100% Ab-Assurance.
The mouse monoclonal antibody recognizes human Integrin alpha L/CD11a. Integrins are heterodimeric integral membrane proteins composed of an alpha chain and a beta chain.
Integrins are cell‐surface adhesion molecules formed from eight different β chains and 18 different α chains that assemble as heterodimeric transmembrane receptors to mediate cell-cell and cell-matrix interactions
Abcam provides specific protocols for Anti-Integrin alpha 9+beta 1 antibody [Y9A2] (ab27947) : Flow cytometry protocols, Immunoprecipitation protocols…
Anti-Integrin alpha 2 antibody conjugated to FITC [AK7] validated for Flow Cyt and tested in Human. Referenced in 2 publications. Immunogen corresponding to…
Gene Information This gene product belongs to the integrin alpha chain family. Integrins are heterodimeric integral membrane glycoproteins composed of a distinct alpha chain and a common beta chain. They are found on a wide variety of cell types including T cells fibroblasts and platelets. Integrins are involved in cell adhesion and also participate in cell-surface mediated signalling. [provided by RefSeq Jul 2008]. ...
Integrins are heterodimeric transmembrane receptor proteins that mediate numerous cellular processes including cell adhesion, cytoskeletal rearrangement, and activation of cell signaling pathways. Integrins are composed of alpha and beta subunits. This gene encodes the alpha 8 subunit of the heterodimeric integrin alpha8beta1 protein. The encoded protein is a single-pass type 1 membrane protein that contains multiple FG-GAP repeats. This repeat is predicted to fold into a beta propeller structure. This gene regulates the recruitment of mesenchymal cells into epithelial structures, mediates cell-cell interactions, and regulates neurite outgrowth of sensory and motor neurons. The integrin alpha8beta1 protein thus plays an important role in wound-healing and organogenesis. Mutations in this gene have been associated with renal hypodysplasia/aplasia-1 (RHDA1) and with several animal models of chronic kidney disease. Alternate splicing results in multiple transcript variants encoding distinct ...
Clone REA718 recognizes the human integrin β5 antigen, a 95 kDa glycoprotein single-pass type I membrane protein. Integrins are a family of transmembrane receptors that mediate adhesion of cells to extracellular matrices, as well as intercellular interactions. These interactions transduce signals that control complex cell functions such as proliferation, differentiation, and survival, and require the regulation of gene expression. Integrins are heterodimeric glycoprotein receptors and exist as non-covalently bound α and β subunits. The integrin αV/β5 heterodimer is found on many types of tissue cells, such as epithelial cells, endothelial cells, keratinocytes, and osteoblastic cells. It is a receptor for fibronectin and vitronectin and acts as a receptor for adenovirus type C. Additional information: Clone REA718 displays negligible binding to Fc receptors. - Nederland
Clone REA718 recognizes the human integrin β5 antigen, a 95 kDa glycoprotein single-pass type I membrane protein. Integrins are a family of transmembrane receptors that mediate adhesion of cells to extracellular matrices, as well as intercellular interactions. These interactions transduce signals that control complex cell functions such as proliferation, differentiation, and survival, and require the regulation of gene expression. Integrins are heterodimeric glycoprotein receptors and exist as non-covalently bound α and β subunits. The integrin αV/β5 heterodimer is found on many types of tissue cells, such as epithelial cells, endothelial cells, keratinocytes, and osteoblastic cells. It is a receptor for fibronectin and vitronectin and acts as a receptor for adenovirus type C. Additional information: Clone REA718 displays negligible binding to Fc receptors. - Lëtzebuerg
Integrin alpha V兔单克隆抗体[EPR5583](ab124968)可与小鼠, 大鼠, 人样本反应并经WB, Flow Cyt实验严格验证。所有产品均提供质保服务,中国75%以上现货。
Monoclonal antibody (mAb) AP7.4 is an anti-integrin antibody recombinantly expressed in Escherichia coli specific to alphavbeta3. It is known that in a variety of RGD-containing molecules, ligand specificity is regulated by structural determinants within the immediate vicinity of the RGD sequence. To better understand the role of the RGD sequence in integrin specificity, we report here the three-dimensional structure of Fab of mAb AP7.4 to a resolution of 2.25 A. The crystals belong to a triclinic space group P1 and the volume of the unit cell is consistent with the presence of two Fab molecules in it. The RGD sequence is located at the tip of a flexible loop in the complementary determining region (CDR-3) of the heavy chain. It has been shown that specific recognition of RGD ligands by their receptors is influenced mainly by the conformation of the tripeptide RGD and the amino acid residues flanking it on either side. Hence, the flexibility of the RGD-carrying loop observed in the crystal ...
Integrins are heterodimeric cell surface receptors composed of alpha and beta subunits, which mediate cell-cell and cell-extracellular matrix attachments. Aberrant
1. Lu X, Lu D, Scully M, Kakkar V. The role of integrins in cancer and the development of anti-integrin therapeutic agents for cancer therapy. Perspect Medicin Chem. 2008;2:57-73 2. Hynes RO. Integrins: a family of cell surface receptors. Cell. 1987;48:549-54 3. Hynes RO. Integrins: versatility, modulation, and signaling in cell adhesion. Cell. 1992;69:11-25 4. Serini G, Valdembri D, Bussolino F. Integrins and angiogenesis: a sticky business. Exp Cell Res. 2006;312:651-8 5. Brakebusch C, Bouvard D, Stanchi F, Sakai T, Fassler R. Integrins in invasive growth. J Clin Invest. 2002;109:999-1006 6. Hynes RO. Integrins: bidirectional, allosteric signaling machines. Cell. 2002;110:673-87 7. Vogel V, Sheetz M. Local force and geometry sensing regulate cell functions. Nat Rev Mol Cell Biol. 2006;7:265-75 8. Ginsberg MH, Partridge A, Shattil SJ. Integrin regulation. Curr Opin Cell Biol. 2005;17:509-16 9. Springer TA. Complement and the multifaceted functions of VWA and integrin I domains. Structure. ...
Rapid progress has been made in the understanding of the molecular interactions that result in cell adhesion. Many adhesive proteins present in extracellular matrices and in the blood contain the tripeptide arginine-glycine-aspartic acid (RGD) as their cell recognition site. These proteins include fibronectin, vitronectin, osteopontin, collagens, thrombospondin, fibrinogen, and von Willebrand factor. The RGD sequences of each of the adhesive proteins are recognized by at least one member of a family of structurally related receptors, integrins, which are heterodimeric proteins with two membrane-spanning subunits. Some of these receptors bind to the RGD sequence of a single adhesion protein only, whereas others recognize groups of them. The conformation of the RGD sequence in the individual proteins may be critical to this recognition specificity. On the cytoplasmic side of the plasma membrane, the receptors connect the extracellular matrix to the cytoskeleton. More than ten proved or suspected ...
Integrin alpha E beta 7 Peptides and Proteins available through Novus Biologicals. Browse our Integrin alpha E beta 7 Peptides and Proteins all backed by our Guarantee+.
Integrins are heterodimeric proteins made up of alpha and beta subunits. At least 18 alpha and 8 beta subunits have been described in mammals. Integrin family members are membrane receptors involved in cell adhesion and recognition in a variety of processes including embryogenesis, hemostasis, tissue repair, immune response and metastatic diffusion of tumor cells. This gene encodes a beta subunit. Multiple alternatively spliced transcript variants which encode different protein isoforms have been found for this gene. [provided by RefSeq, Jul 2008 ...
2015 Project header}} =,font color=red>Integrins,/font>= Integrins are a group of transmembrane cell adhesion proteins which anchor the cell to the extracellular matrix (ECM) by its cytoskeleton. Integrins not only anchor the cell, they are also involved in cell to cell adhesion,ref name="reffff">Alberts B, Johnson A, Lewis J, et al. Molecular Biology of the Cell. 4th edition. New York: Garland Science; 2002. Integrins. Available from: http://www.ncbi.nlm.nih.gov/books/NBK26867/,/ref>. However, integrins are not just adhesion proteins, as they can also induce intracellular signalling pathways in the extracellular matrix, which makes them play an important role in development, immune response, leukocyte trafficking and haemostasis. [[File:Integrin anchoring cytoskeleton to ecmII.png,thumb,350px,Figure 1:A simple diagram of how integrins interact with other proteins to anchor the cytoskeleton to the extracellular matrix]] The integrin family is one of the most highly studied cell adhesion ...
Role of RGD-binding integrins in uPAR-induced protrusions and adhesion. (A) Swiss 3T3 cells were injected with pRc/CMV-uPAR (100 μg/ml) and incubated in growth
FITC偶联Integrin alpha 1抗体[TS2/7](ab34176)可与人样本反应并经Flow Cyt实验严格验证,被4篇文献引用,实验条件参看说明书。中国75%以上现货。
The extracellular matrix (ECM) is an insoluble network of proteins that provides structural support to nearly all multicellular tissues and organs as well as solid malignancies (1). Most metazoan cells dynamically interact with ECM components via integrins, which are heterodimeric transmembrane proteins composed of α and β subunits (2). Most integrins expressed on the cell surface are present in inactive conformations, and their adhesion to ECM ligands must be precisely regulated via "inside-out" activation mechanisms. Such regulatory mechanisms occur after extracellular stimuli (e.g., growth factors or cytokines), alter intracellular effector proteins that in turn bind to integrin cytoplasmic regions, and induce conformational changes in the integrin extracellular domains (2). Following activation and engagement with ECM ligands, integrins regulate cytoskeletal dynamics as well as intracellular signal transduction cascades that lead to a wide variety of cellular responses, including ...
The integrin family of cell surface receptors is evolutionary conserved and found in all multicellular animals. In humans 8-alpha and 18-beta integrins are non-covalently associated into 24 dimers. Integrins mediate cell-extracellular matrix and cell-cell interactions and participate in cell signalling. This ideally places integrins to regulate vital processes such as cell adhesion, migration, differentiation and cytoskeleton dynamics. Integrins also play a fundamental role in regulating cell survival and anoikis. In this thesis molecular mechanisms employed by integrins to induce signal transduction, independently or through crosstalk with other receptors, were characterised.. Rictor-mTOR (mTORC2) was required for Akt Ser473 phosphorylation in response to β1 integrin-mediated adhesion as well as EGF-, PDGF- or LPA-stimulation of MCF7 cells. ILK and PAK were dispensable for Akt Ser473 phosphorylation upon β1 integrin-engagement or EGF-stimulation. PAK was needed when this phosphorylation was ...
Integrin alpha M (ITGAM) Antibody is a Rabbit Polyclonal antibody against Integrin alpha M (ITGAM). Integrin alpha M (ITGAM), also named as CD11B and CR3A, belongs to the integrin alpha chain family. It is implicated in various adhesive interactions of mo
In their roles as major adhesion receptors, integrins signal across the plasma membrane in both directions. Recent structural and cell biological data suggest models for how integrins transmit signals between their extracellular ligand binding adhesion sites and their cytoplasmic domains, which link …
The ability of cells to migrate is a fundamental physiological process involved in embryonic development, tissue homeostasis, immune surveillance and wound healing. In order for cells to migrate, they must interact with their environment using adhesion receptors, such as integrins, and form specialized adhesion complexes that mediate responses to different extracellular cues. In this review, we discuss the role of integrin adhesion complexes (IACs) in cell migration, highlighting the layers of regulation that are involved, including intracellular signalling cascades, mechanosensing and reciprocal feedback to the extracellular environment. We also discuss the role of IACs in extracellular matrix remodeling and how they impact upon cell migration. ...
Integrins interact with extracellular matrix (ECM) and deliver intracellular signaling for cell proliferation, survival, and motility. During tumor metastasis, integrin-mediated cell adhesion to and migration on the ECM proteins are required for cancer cell survival and adaptation to the new microenvironment. Using stable isotope labeling by amino acids in cell culture-mass spectrometry, we profiled the phosphoproteomic changes induced by the interactions of cell integrins with type I collagen, the most common ECM substratum. Integrin-ECM interactions modulate phosphorylation of 517 serine, threonine, or tyrosine residues in 513 peptides, corresponding to 357 proteins. Among these proteins, 33 key signaling mediators with kinase or phosphatase activity were subjected to small interfering RNA-based functional screening. Three integrin-regulated kinases, DBF4, PAK2, and GRK6, were identified for their critical role in cell adhesion and migration possibly through their regulation of actin ...
マウス・モノクローナル抗体 ab24697 交差種: Hu 適用: IP,Neut,Flow Cyt,Inhibition,BL,ICC/IF…Integrin alpha 2+beta 1抗体一覧…画像、プロトコール、文献などWeb上の情報が満載のアブカムの…
Control of integrin activation and signaling plays crucial roles in cell adhesion, spreading and migration. Here, we report that selective breakage of two conserved disulfide bonds located at the knees of integrin alpha(4)C589-C594 and beta(7)C494-C526 activated alpha(4)beta(7). This activated integrin had a unique structure that was different from the typical extended conformation of active integrin. In addition, these activated alpha(4)beta(7) integrins spontaneously clustered on the cell membrane and triggered integrin downstream signaling independent of ligand binding. Although these disulfide bonds were not broken during alpha(4)beta(7) activation by inside-out signaling or Mn2+, they could be specifically reduced by 0.1 mM dithiothreitol, a reducing strength that could be produced in vivo under certain conditions. Our findings reveal a novel mechanism of integrin activation under specific reducing conditions by which integrin can signal and promote cell spreading in the absence of ligand ...
Integrins alpha-1/beta-1, alpha-2/beta-1, alpha-10/beta-1 and alpha-11/beta-1 are receptors for collagen. Integrins alpha-1/beta-1 and alpha-2/beta-2 recognize the proline-hydroxylated sequence G-F-P-G-E-R in collagen. Integrins alpha-2/beta-1, alpha-3/beta-1, alpha-4/beta-1, alpha-5/beta-1, alpha-8/beta-1, alpha-10/beta-1, alpha-11/beta-1 and alpha-V/beta-1 are receptors for fibronectin. Alpha-4/beta-1 recognizes one or more domains within the alternatively spliced CS-1 and CS-5 regions of fibronectin. Integrin alpha-5/beta-1 is a receptor for fibrinogen. Integrin alpha-1/beta-1, alpha-2/beta-1, alpha-6/beta-1 and alpha-7/beta-1 are receptors for lamimin. Integrin alpha-4/beta-1 is a receptor for VCAM1. It recognizes the sequence Q-I-D-S in VCAM1. Integrin alpha-9/beta-1 is a receptor for VCAM1, cytotactin and osteopontin. It recognizes the sequence A-E-I-D-G-I-E-L in cytotactin. Integrin alpha-3/beta-1 is a receptor for epiligrin, thrombospondin and CSPG4. Alpha-3/beta-1 may mediate with ...
Integrins are dimeric molecules consisting of one α subunit and one β subunit. The composition of integrins dictates ligand binding and cellular response (migration, attachment, and cell survival) to their interaction with the substrate or extracellular matrix. Danen et al. used cells engineered to express either β1 or β3 and showed that it is the presence of the β1 or β3 subunit that dictates whether cells move randomly or in a directed fashion. Epithelial GE11 cells engineered to express αvβ3 (GEβ3) or α5β1 (GEβ1) cells were tested in a wounding assay, or motility was monitored in sparsely seeded cultures on fibronectin. Although both cells exhibited motile behavior that was greater than the β1-deficient parent GE11 line, the GEβ3 cells moved as a sheet in a directed fashion, and the GEβ1 cells moved randomly in all directions. GEβ3 cells, but not GEβ1 cells, exhibited remodeling of the actin cytoskeleton and the formation of lamellipodia either during cell migration or in ...
Th1 and Th2 cells were analyzed for the expression of different integrins by super array gene array analysis (Super Array). (A) Heatmap analysis of differential expression of α and β integrin molecules in Th1 and Th2 cells. (B) The histogram analysis of super array. Red indicates the minimum and blue indicates the maximum expression in the scale. (C) Venn diagram analysis summarizes the number of integrins upregulated (blue circle), downregulated (red circle), and unaltered (common area) in MBP-primed Th2 cells compared to Th1 cells. The mRNA expression of αV, α4, β1, and β3 in Th1 and Th2 cells was verified by semi-quantitative RT-PCR (D) and realtime PCR (E) analyses. Results represent three independent experiments. ap,0.01, bp,0.05, cp,0.01, and dp,0.05 vs. control expression of αV, α4, β3, and β1 respectively ...
Diagram of the collagen overlay model for integrin stimulation in cardiomyocytes with RGD peptide. Cardiomyocytes are plated on laminin-coated plates in media d
Integrins: Molecular and Biological Responses to the Extracellular Matrix (Robert P. Mecham, David A. Cheresh) pe OKIAN.ro. Pret: 962.99 lei. Integrins: Mo
This gene encodes a beta subunit of integrin, which can combine with different alpha chains to form a variety of integrin heterodimers. Integrins are integral cell-surface receptors that participate in cell adhesion as well as cell-surface mediated signaling. The alphav beta5 integrin is involved in adhesion to vitronectin. [provided by RefSeq, Aug 2017] ...
This book represents the most current, comprehensive, and authoritative study of integrins on the market today. It provides an overview of the diverse
The extracellular matrix (ECM) consists of a complex mixture of structural and functional macromolecules and serves an important role in tissue and organ morphogenesis and in the maintenance of cell and tissue structure and function. Specific interactions between cells and the ECM are mediated by transmembrane molecules, mainly integrins and perhaps also proteoglycans, CD36, or other cell-surface-associated components. These interactions lead to a direct or indirect control of cellular activities such as adhesion, migration, differentiation, proliferation, and apoptosis. In addition, integrins function as mechanoreceptors and provide a force-transmitting physical link between the ECM and the cytoskeleton. Integrins are a family of glycosylated, heterodimeric transmembrane adhesion receptors that consist of noncovalently bound alpha- and beta-subunits ...
These data show that high levels of αvβ6 integrins are significantly associated with poor prognosis. There is also a trend towards worse prognosis with high levels of αSMA. However, there were no differences observed between samples with UIP or NSIP histology, although this study was not sufficiently powered to detect a difference between the two groups. Furthermore, there was no apparent relationship between the number of fibroblastic foci and mortality, consistent with previous reports [8]. This is the first study to demonstrate a tissue immunomarker in ILD with a significant association with the prognosis. A notable observation is that the median survival of patients with the highest expression of the αvβ6 integrin was only 25 months, which is comparable to the published survival data in IPF. This suggests that increased expression of the αvβ6 integrin may represent a distinct endotype of progressive fibrotic ILD, and could be useful as a biomarker for disease progression and ...
Integrin beta 3 antibody [JM2E5] (FITC) (integrin subunit beta 3) for FACS. Anti-Integrin beta 3 mAb (GTX43357) is tested in Human, Dog, Pig, Horse, Bovine samples. 100% Ab-Assurance.
高い抗原親和性、特異性と安定した品質を兼ね備えたアブカムのウサギ・モノクローナル抗体 RabMAb® ab52971 交差種: Hu 適用: WB,IHC-P,IHC-Fr
The polymorphisms C807T end G873A of the platelet integrin alpha2b ta1 collagen receptor glycoprotein GP Ia-IIa are linked to the expression density of this receptor. The GPIa T807/A873 allele causes a higher receptor expression, enhancing platelet binding to collagen. This might present a genetic predisposition for the development of...
The cell adhesion molecule integrin alpha(v)beta(3) is an important player in the process of tumor angiogenesis and metastasis. Abegrin (TM), a fully humanized anti-integrin alpha(v)beta(3) monoclonal antibody, was currently in clinical trials for cancer therapy. Herein, we labeled Abegrin (TM) with In-111, evaluated the in vitro and in vivo characteristics, and investigated whether the expression of integrin alpha(v)beta(3) in tumors could be imaged with In-111-labeled Abegrin (TM).. The binding affinity and specificity of Abegrin (TM) was analyzed using U87MG glioblastoma cells. Abegrin (TM) was coupled with 1,4,7,10-tetraazadodecane-N,N′,NaEuro(3),N′aEuro(3)-tetraacetic acid (DOTA) for In-111 radiolabeling. gamma Imaging of In-111-DOTA-Abegrin (TM) was carried out in nude mice bearing both integrin alpha(v)beta(3)-positive U87MG and integrin alpha(v)beta(3)-negative HT-29 tumors. Biodistribution and blocking studies of In-111-DOTA-Abegrin (TM) were investigated in U87MG tumor-bearing nude ...
Integrins[edit]. Integrins involved in cellular adhesion are primarily expressed on leukocytes. β2 integrins on rolling ... Integrin molecules migrate to the cell surface and congregate in high-avidity patches. Intracellular integrin domains associate ... Integrin ligands ICAM-1 and VCAM-1 are activated by inflammatory cytokines, while ICAM-2 is constitutively expressed by some ... During chemotaxis, cell movement is facilitated by the binding of β1 integrins to components of the extracellular matrix: VLA-3 ...
Symptoms of CMT usually begin in early childhood or early adulthood, but can begin later. Some people do not experience symptoms until their early 30s or 40s. Usually, the initial symptom is foot drop early in the course of the disease. This can also cause hammer toe, where the toes are always curled. Wasting of muscle tissue of the lower parts of the legs may give rise to a "stork leg" or "inverted champagne bottle" appearance. Weakness in the hands and forearms occurs in many people as the disease progresses. Loss of touch sensation in the feet, ankles, and legs, as well as in the hands, wrists, and arms occurs with various types of the disease. Early- and late-onset forms occur with 'on and off' painful spasmodic muscular contractions that can be disabling when the disease activates. High-arched feet (pes cavus) or flat-arched feet (pes planus) are classically associated with the disorder.[3] Sensory and proprioceptive nerves in the hands and feet are often damaged, while unmyelinated pain ...
Onset occurs in infancy or early childhood, usually before 3 years of age. Progression is slow until the teenage years at which point it may accelerate, resulting in severe disability. Symptoms are usually more severe and rapidly progressive than in the other more common Charcot-Marie-Tooth diseases. Some patients may never walk and solely use wheelchairs by the end of their first decade, while others may need only a cane (walking stick) or similar support through life. Dejerine-Sottas disease is characterized by moderate to severe lower and upper extremity weakness and loss of sensation, which occur mainly in the lower legs, forearms, feet and hands. Loss of muscle mass and reduced muscle tone can occur as the disease progresses. Other symptoms may include pain in the extremities, curvature of the spine, clawed hands, foot deformities, ataxia, peripheral areflexia, and slow acquisition of motor skills in childhood. Symptoms that are less common can include limitation of eye movements, other eye ...
Giancotti, FG; Ruoslahti, E (Aug 13, 1999). "Integrin signaling". Science. 285 (5430): 1028-32. doi:10.1126/science.285.5430. ... Cells use mainly the receptor integrin to interact with ECM proteins. This signaling can influence the cell cycle and cellular ...
Integrin network. *PI3K-AKT Network. Relevant biophysical endothelial function mediators: *Endothelial shear stress ...
"The integrin binding site 2 (IBS2) in the talin rod domain is essential for linking integrin beta subunits to the cytoskeleton ... integrin binding. • protein binding. • vinculin binding. • protein complex binding. • actin binding. • cadherin binding. • ... "The Talin head domain binds to integrin beta subunit cytoplasmic tails and regulates integrin activation". The Journal of ... Calderwood DA (Feb 2004). "Integrin activation". Journal of Cell Science. 117 (Pt 5): 657-66. doi:10.1242/jcs.01014. PMID ...
integrin binding. • cell adhesion molecule binding. Cellular component. • integral component of membrane. • Golgi apparatus. • ... alpha9-beta1 integrin-vascular cell adhesion molecule-1 complex. • membrane. • filopodium. • plasma membrane. • apical part of ... Primarily, the VCAM-1 protein is an endothelial ligand for VLA-4 (Very Late Antigen-4 or integrin α4β1) of the β1 subfamily of ... Yonekawa K, Harlan JM (2005). "Targeting leukocyte integrins in human diseases". J. Leukoc. Biol. 77 (2): 129-40. doi:10.1189/ ...
Integrin signalling Integrin αvβ3 (a cell-surface adhesion molecule) is important for tumor attachment, cell-to-cell ... Several different integrins bind to fibronectin. Fibronectin-integrin interactions are important in tumor cell migration, ... invasion, metastasis and cell proliferation by signaling through integrins. Integrin-mediated tumor cell adhesion to ECM ... Endoglin is a cell-surface disulfide-linked homodimeric glycoprotein which binds to integrins and other RGD ligands and is a co ...
Cell adhesion molecules, such as integrins, are critical to the attachment and migration of endothelial cells to the ...
Integrin alpha-IIb is a protein that in humans is encoded by the ITGA2B gene. ITGA2B, also known as CD41, encodes integrin ... Porter JC, Hogg N (1999). "Integrins take partners: cross-talk between integrins and other membrane receptors". Trends Cell ... integrin complex. • integral component of plasma membrane. • platelet alpha granule membrane. • integral component of membrane ... 2004). "Integrin alphaIIbbeta3 and its antagonism". Arterioscler. Thromb. Vasc. Biol. 23 (6): 945-52. doi:10.1161/01.ATV. ...
... integrin function depend on both cell type (Natural killer cell or Leukocytes) and the integrin activation stimulus. The ... 2 directly bind the C-terminal region of beta integrin cytoplasmic tails and exert integrin-specific activation effects". J. ... Bialkowska K, Ma YQ, Bledzka K, Sossey-Alaoui K, Izem L, Zhang X, Malinin N, Qin J, Byzova T, Plow EF (2010). "The integrin co- ... Therefore, they are responsible for cell to cell crosstalk via cell-cell contacts and integrin mediated cell adhesion through ...
integrins link intracellular actin filaments to extracellular matrix proteins Receptors platelet-derived growth factor receptor ...
Crucial for the Entry of the KSHV [10] is the EPH receptor A2[11] , Hrs[12] , TSG101[13] and a few Integrins, whose identity ... July 2016). "Integrins as Herpersvirus Receptors and Mediators of the Host Signalosome". Reviews in Advance. 3 (1): 215-236. ...
"Platelet and osteoclast β3 integrins are critical for bone metastasis". Proceedings of the National Academy of Sciences of the ...
Integrins are cell-surface proteins that bind cells to ECM structures, such as fibronectin and laminin, and also to integrin ... Binding to integrins unfolds fibronectin molecules, allowing them to form dimers so that they can function properly. ... This cell-to-ECM adhesion is regulated by specific cell-surface cellular adhesion molecules (CAM) known as integrins. ... Fibronectins bind collagen and cell-surface integrins, causing a reorganization of the cell's cytoskeleton to facilitate cell ...
Hemidesmosomes diagram showing interaction between integrins and laminin, including how integrins are linked to keratin ... Integrins link extracellular matrix to keratin intermediate filaments, which interacts with intracellular domain of integrins ... can induce conformational changes in integrins and initiate signalling cascades.[22] Extracellular domains of integrins can ... Cell-matrix junctions are mainly mediated by integrins, which also clusters like cadherins to form firm adhesions. Integrins ...
Stewart M, Thiel M, Hogg N (1996). "Leukocyte integrins.". Curr. Opin. Cell Biol. 7 (5): 690-6. PMID 8573344. doi:10.1016/0955- ... Ugarova TP, Yakubenko VP (2001). "Recognition of fibrinogen by leukocyte integrins.". Ann. N. Y. Acad. Sci. 936 (1): 368-85. ... 1990). "Integrin distribution and cytoskeleton organization in normal and malignant monocytes.". Leukemia 4 (10): 682-7. PMID ... "Entrez Gene: ITGAX integrin, alpha X (complement component 3 receptor 4 subunit)".. ...
Knocking down β1 integrin inhibited cancer cell migration, whereas overexpressing the integrin in Cdc42-deficient cells ... Levels of β1 integrin were reduced in Cdc42-deficient cells. β1 integrin is important for adhesion to the extracellular matrix ... found that Cdc42 drives the process of initiating a metastatic tumor in a new tissue by promoting the expression of β1 integrin ... restored endothelial invasion.[10] Cdc42 promoted β1 integrin expression by activating a transcription factor called SRF. A ...
... is an integrin alpha X chain protein. Integrins are heterodimeric integral membrane proteins composed of an alpha chain ... CD11c, also known as Integrin, alpha X (complement component 3 receptor 4 subunit) (ITGAX), is a gene that encodes for CD11c . ... This protein combines with the beta 2 chain (ITGB2) to form a leukocyte-specific integrin referred to as inactivated-C3b (iC3b ... 1990). "Integrin distribution and cytoskeleton organization in normal and malignant monocytes". Leukemia. 4 (10): 682-7. PMID ...
Berditchevski F, Chang S, Bodorova J, Hemler M (1997). "Generation of monoclonal antibodies to integrin-associated proteins. ... Berditchevski F, Chang S, Bodorova J, Hemler ME (1997). "Generation of monoclonal antibodies to integrin-associated proteins. ... proteins Cyp-A and CyP-B and certain integrins.[11][12][13] It is expressed by many cell types, including epithelial cells, ...
Integrin antagonists and immonochemotherapy with 5-fluorouracil plus polysaccharide-K have shown promising results. ... integrins/cadherins) in prostate cancer". Int Braz J Urol. 37 (3): 302-6. doi:10.1590/S1677-55382011000300002. PMID 21756376. ...
integrin binding. • protein binding. • hormone activity. • heparin binding. • identical protein binding. • macromolecular ... cell adhesion mediated by integrin. • glucose homeostasis. • sequestering of BMP in extracellular matrix. • sequestering of ... 1uzk: INTEGRIN BINDING CBEGF22-TB4-CBEGF33 FRAGMENT OF HUMAN FIBRILLIN-1, CA BOUND TO CBEGF23 DOMAIN ONLY ... 1uzp: INTEGRIN BINDING CBEGF22-TB4-CBEGF33 FRAGMENT OF HUMAN FIBRILLIN-1, SM BOUND FORM CBEGF23 DOMAIN ONLY. ...
CS1 maint: Multiple names: authors list (link) Brakebusch, C; Fässler, R (2003). "The integrin-actin connection, an eternal ... Schwartz, MA; Ingber, DE (1994). "Integrating with integrins". Molecular Biology of the Cell. 5 (4): 389-93. doi:10.1091/mbc. ... bound to the cytoplasmic domains of integrins. He then discovered other focal adhesion components including paxillin and ...
Schnapp, L (2006). Integrin, Adhesion/cell-matrix. Seattle: Elsevier. García AJ (December 2005). "Get a grip: integrins in cell ... Integrins and the Ig-superfamily CAMs do not depend on Ca2+ while cadherins and selectins depend on Ca2+. In addition, ... integrins participate in cell-matrix interactions, while other CAM families participate in cell-cell interactions. Integrins, ... Integrins are heterodimeric, as they consist of an alpha and beta subunit. There are currently 18 alpha subunits and 8 beta ...
When an integrin receptor binds to its ECM ligand and is activated, additional integrins cluster around the activated site. In ... and integrin receptors (of which there exist several types on chondrocytes). Using the integrin-linked mechanotransduction ... Integrins have been identified on the upper shaft of the cilium, acting as anchors to the collagen matrix around it. Recent ... Integrin signaling is just one example of multiple pathways that are activated when cartilage is loaded. Some intracellular ...
... and αvβ6-integrins may be promising integrin-targeting therapies for further clinical investigation. ... However, no integrin inhibitor has shown favorable results thus far. However, conjugates of cytotoxic agents with the triplet ... Preclinical studies have shown the effectiveness of several integrin inhibitors for blocking cancer progression, especially by ... This review summarizes the current understanding of integrin biology in ovarian cancer metastasis and various therapeutic ...
Flow Cytometry for the detection of mouse Integrin alphaV. Find MSDS or SDS, a COA, data sheets and more information. ... This Anti-mouse Integrin alphaV Antibody, clone RMV-7 (Preservative free) is validated for use in Western Blotting, ... Anti-mouse Integrin alphaV, clone RMV-7 2472968 Anti-mouse Integrin alphaV, clone RMV-7 (Preservative free) - Q2067202 Q2067202 ... Integrin alphaV, also known as CD51, a member of the integrin family, is a 140 kD protein expressed on activated T cells, ...
Integrin expression may also be regulated by miRNAs, which can also modulate integrin signaling and function. Integrins are ... Similarly, α4 also associates with β7 while integrin β7 also associates with αE. Integrin β1 and integrin β4 are regulated by ... there are no integrin α subunits known to be regulated by miRNA. As for the RGD ligand integrins, integrin α5 is the only α ... Integrin β2 associates with αD, αL,αM, and αX, and is exclusively expresse on the surface of leukocytes. To date, integrins β2 ...
Integrins receive signals from other receptors that lead to activation of ligand binding (inside-out signaling) and matrix ... Integrins: emerging paradigms of signal transduction.. Schwartz MA1, Schaller MD, Ginsberg MH. ...
Getting integrins into shape: recent insights into how integrin activity is regulated by conformational changes. J Cell Sci ... Synaptic integrins in developing, adult, and mutant muscle: selective association of al, a7A and a7B integrins with the ... Porter JC, Hogg N. Integrins take partners: cross-talk between integrins and other membrane receptors. Trends Cell Biol 1998; 8 ... Hynes R. Integrins, versatility, modulation, and signaling in cell adhesion. Cell 1992; 69: 11-25.PubMedGoogle Scholar ...
Thus, CD98hc is not required for integrin expression, integrin affinity, or integrin-mediated adhesion. ... 5 D and E ). Thus, the portion of CD98hc that binds β1 integrins and enhances integrin signaling promotes tumorigenesis and ... Thus, CD98hc is an integrin-associated protein that mediates integrin-dependent signals, which promote tumorigenesis. ... that binds to β1 integrins stimulates teratocarcinoma growth and mediates integrin signaling indicates that the β1 integrin- ...
... leukocyte integrins im Englisch-Deutsch-Wörterbuch, mit echten Sprachaufnahmen, Illustrationen, Beugungsformen, ... ... leukocyte integrin. • leukocyte integrins. leukocyte migration. leukocyte phosphatase. leukocyte picture. leukocyte typing. ... Im Forum nach leukocyte integrins suchen. » Im Forum nach leukocyte integrins fragen. Recent Searches ... leukocyte integrins in anderen Sprachen:. Deutsch - Englisch. Eintragen in .... English - Bulgarian. English - Bosnian. English ...
The β3 integrin was found to coprecipitate with the αV integrin antibody, from which the authors conclude that αVβ3 integrin ( ... Previous investigations have suggested that integrins, in particular the β3 integrin, is involved in the eutrophic remodeling ... β3 integrin, whereas Martinez-Lemus et al12 found involvement of both αVβ3 and αVβ1 integrins in myogenic responsiveness to ... 14 enzymes that are closely associated with integrins.15 There are thus several ways by which the blocking of integrins in the ...
The interactions between integrins and the extracellular matrix have been identified as important regulators of vascular cell ... The interactions between integrins and the extracellular matrix have been identified as important regulators of vascular cell ... Strömblad, S., & Cheresh, D. A. (1996). Integrins, angiogenesis and vascular cell survival. Chemistry and Biology. Elsevier Ltd ...
integrin heterodimer is a component of hemidesmosomes," Proceedings of the National Academy of Sciences of the United States of ... integrin subunit," Journal of Cell Biology, vol. 136, no. 6, pp. 1333-1347, 1997. View at Publisher · View at Google Scholar ... integrins and assembly of hemidesmosomes in an in vitro model of wound healing," Journal of Cell Biology, vol. 115, no. 6, pp. ... integrins as therapeutic targets in autoimmune disease," New England Journal of Medicine, vol. 348, no. 1, pp. 68-72, 2003. ...
Integrin alpha beta-propellor (IPR013519). Short name: Int_alpha_beta-p Description. Integrins are cell adhesion molecules that ... Alpha integrins are proposed to contain a domain containing a 7-fold repeat that adopts a beta-propellor fold. Some of these ...
... αV-integrins via RGD motif that resides on virus capsid. In contrast, echovirus 1 (E-1) has no RGD and uses integrin α2β1 as ... β1 integrin and enters via macropinocytosis. In this paper, we review what is known about receptors and endocytosis of integrin ... Endocytosis of Integrin-Binding Human Picornaviruses. Pirjo Merilahti,1,2 Satu Koskinen,1 Outi Heikkilä,1,2 Eveliina Karelehto, ... Three enterovirus types and one parechovirus have experimentally been shown to bind and use integrin receptors in cellular ...
An integrin protein in a cell membrane moves like a sunflower seeking the sun, connecting every animal cell to its environment ... An integrin protein in a cell membrane moves like a sunflower seeking the sun, connecting every animal cell to its environment ...
AG Extracellular Matrix and Integrins in Cardiovascular Disease. Integrin signaling and heart failure Integrins are ... Integrin activation and atherosclerosis Although integrins are highly expressed on the cell surface, they do not bind their ... ß2 integrin activation on T cells is also a critical step during the process of extravasation and recruitment of T cells within ... Beta2-integrin activation on T cell subsets is an independent prognostic factor in unstable angina pectoris. Basic Res Cardiol ...
IPR015812. Integrin_bsu. IPR014836. Integrin_bsu_cyt_dom. IPR002369. Integrin_bsu_VWA. IPR032695. Integrin_dom_sf. IPR036465. ... IPR015812. Integrin_bsu. IPR014836. Integrin_bsu_cyt_dom. IPR002369. Integrin_bsu_VWA. IPR032695. Integrin_dom_sf. IPR036465. ... Integrin betaUniRule annotation. ,p>Information which has been generated by the UniProtKB automatic annotation system, without ... Integrin betaSequence analysis. ,p>Information which has been generated by the UniProtKB automatic annotation system, without ...
Read about integrins and their associated proteins and importance in human disease. Find antibodies, proteins, modulators and ... Integrins, associated proteins and disease. Integrins are a family of cell surface transmembrane receptors, each consisting of ... While most integrins connect to the actin cytoskeleton and reside in adhesion structures, called focal adhesions, integrin α6β4 ... His main objective is to decipher the function of integrins in differentiation and migration, and how integrins and associated ...
Integrin extracellular domains are yielding to high-resolution structural analyses, and intracellular proteins … ... Inside-out signals regulate integrin affinity for adhesive ligands, and ligand-dependent outside-in signals regulate ... Integrin signaling is bidirectional. Inside-out signals regulate integrin affinity for adhesive ligands, and ligand-dependent ... Integrin regulation Curr Opin Cell Biol. 2005 Oct;17(5):509-16. doi: 10.1016/j.ceb.2005.08.010. ...
Integrins are cell‐surface adhesion molecules formed from eight different β chains and 18 different α chains that assemble as ... Integrin subunit pairings. There are 18 α‐ and 8 β‐integrin subunits from which 24 different functional integrins are currently ... The integrin superfamily first emerged in the metazoa and has expanded with evolution creating 24 different integrins in humans ... de Melker AA and Sonnenberg A (1999) Integrins: alternative splicing as a mechanism to regulate ligand binding and integrin ...
Mice Lacking αv Integrins Develop Colitis.. Determining the precise contributions of αv integrins to immune functions in vivo ... Ulcerative colitis and autoimmunity induced by loss of myeloid αv integrins. Adam Lacy-Hulbert, Aileen M. Smith, Hamid Tissire ... Ulcerative colitis and autoimmunity induced by loss of myeloid αv integrins. Adam Lacy-Hulbert, Aileen M. Smith, Hamid Tissire ... Deletion of αv integrins in endothelial and hematopoietic cells in αv-tie2 mice. (a and b) Small intestine from tie2-CRE ...
Embryos mutant for β-integrin (A,mys), αPS1 integrin (B,mew), αPS2 integrin (C,if), and αPS3 integrin (D,scab) have a range of ... Genes for integrin ligands interact with slit. The midline axon phenotype of integrin mutants is part of a more complex ... How do integrins contribute to axon guidance?. Integrins are concentrated in the growth cones ofDrosophila axons (Takagi et al ... Integrin phenotypes in the CNS do not demonstrate a direct role for integrins in growth cone guidance. In contrast, ...
Integrins are found in all animals while integrin-like receptors are found in plant cells. Integrins work alongside other ... Media related to Integrins at Wikimedia Commons MBInfo - Integrin-Mediated Signalling MBInfo - Integrin Activation Eukaryotic ... The following are 16 of the ~24 integrins found in vertebrates: Beta-1 integrins interact with many alpha integrin chains. Gene ... integrins of the β2 family). This α-I domain is the binding site for ligands of such integrins. Those integrins that dont ...
Recently ADAP was shown genetically to positively regulate T cell activation, TCR-induced integrin clustering, and T cell ... The mechanism by which ADAP couples TCR stimulation to integrin clustering remains unclear; however, studies of ADAP, the ... exchange factor Vav1, and WASP suggest that TCR and integrin clustering may be controlled by distinct signaling pathways. ...
They found that OSCC-3 attached to RGD-alginate in an α5β1 integrin-dependent manner and proliferated when attached to RGD- ... Cancer cell angiogenic capability is regulated by 3D culture and integrin engagement. Proc. Natl. Acad. Sci. U.S.A. 106, 399- ... which constitute the primary integrin recognition site in many extracellular matrix (ECM) proteins. ...
IPR013649 Integrin_alpha-2. IPR018184 Integrin_alpha_C_CS. IPR028994 Integrin_alpha_N. IPR032695 Integrin_dom_sf. IPR002035 VWF ... IPR013649 Integrin_alpha-2. IPR018184 Integrin_alpha_C_CS. IPR028994 Integrin_alpha_N. IPR032695 Integrin_dom_sf. IPR002035 VWF ... IntegrinUniRule annotation. ,p>Information which has been generated by the UniProtKB automatic annotation system, without ... Belongs to the integrin alpha chain family.UniRule annotation. Automatic assertion according to rulesi ...
reacts with the integrin heterodimer of 165 kDa which comprises the CD11b receptor ...
  • As for the RGD ligand integrins, integrin α5 is the only α subunit found to be regulated by miRNAs (miR-31, miR-17-92 cluster, and miR-148 b). (nih.gov)
  • Although integrins are highly expressed on the cell surface, they do not bind their respective ligand unless activated from within the cell (inside-out signaling). (uni-heidelberg.de)
  • de Melker AA and Sonnenberg A (1999) Integrins: alternative splicing as a mechanism to regulate ligand binding and integrin signaling events. (els.net)
  • Those integrins that don't carry this inserted domain also have an A-domain in their ligand binding site, but this A-domain is found on the β subunit. (wikipedia.org)
  • It's a new ligand for binding to integrins," she said. (biologynews.net)
  • 40 1.79*10^6 3.47*10^6 4.00*10^5 a) which ligand leads to the greates degree of dimerization of the integrin-ligand complex at 20C? (physicsforums.com)
  • I'm not sure how to find the tfraction of total integrin-ligand complexes. (physicsforums.com)
  • Once activated by a ligand, integrins can induce changes in cell cycle, growth factor signaling pathways, cytoskeletal organization, and movement. (fold.it)
  • Brooks, P.C., MMP-9 binds to a ligand induced cryptic site with β1 integrin: role in angiogenesis and tumor growth, In Vitro Cellular & Developmental Biology Animal, (Mar. 2000) vol. 36, No. 3, Part 2, pp. 29.A. Print. (freepatentsonline.com)
  • 1999) The integrin alpha v beta 6 binds and activates latent TGF beta 1: a mechanism for regulating pulmonary inflammation and fibrosis. (els.net)
  • The association of the laminin-binding integrins (α3β1, α6β1, α6β4 and α7β1) with the tetraspanin CD151 strengthens cell adhesion through mechanisms that include the clustering of the integrins in the plasma membrane. (abcam.com)
  • To definitively address the role of CD98hc in integrin function and tumorigenesis, we disrupted the CD98hc gene. (pnas.org)
  • Longitudinal tract axons in Drosophila embryos doubly heterozygous for slit and an integrin gene, encoding αPS1, αPS2, αPS3, or βPS1, take ectopic trajectories across the midline of the CNS. (jneurosci.org)
  • Additionally, SBA reduced the mRNA expression of integrins by down regulating the gene expression level of ACTN2 . (mdpi.com)
  • To test whether Cdc42 is essential for directed cell migration in mammalian cells and to investigate the cross-talks between integrin and Cdc42 mediated signalling, fibroblastoid cell lines lacking a functional Cdc42 gene were established and analyzed in wound closure assays. (uni-muenchen.de)
  • For example, genetic ablation of the αv integrin gene in epithelial cells of the murine skin leads to development of squamous cell carcinomas ( 6 ), revealing tumor suppressor-like functions for αv integrins during epithelial cell homeostasis. (aacrjournals.org)
  • In addition, several kinases regulate integrin traffic. (biologists.org)
  • The identification of their substrates has demonstrated how these kinases regulate integrin traffic by controlling small GTPases or stabilizing cytoskeletal tracks that are crucial for efficient traffic of integrins to the plasma membrane. (biologists.org)
  • β1 integrin (also known as CD29) is a member of the subfamily of collagen-binding integrins (including α1β1, α2β1, α10β1 and α11β1) which bind to the triple-helical GFOGER sequence on collagen fibrils. (nature.com)
  • In this study, we have investigated the role of β1 integrin and ILK in the activation of the AKT/mTOR pathway, and the role of AKT/mTOR in the subsequent expression and translation of collagen in human tendon cells. (nature.com)
  • Alpha 10 binds to a beta-1 chain, forming a collagen type-II-binding integrin, which is expressed in cartilage. (thefreedictionary.com)
  • CD61 binds non-covalently with the alpha integrins CD41 and CD51, to form the alpha IIb beta3 (CD41/CD61) and alpha v beta3 (CD51/CD61) complexes. (fishersci.com)
  • Although the molecular bases for its antiangiogenic activity are not fully elucidated ( 16 ), recent observations have shown that trans -resveratrol binds purified β 3 integrin chain in vitro ( 17 ). (aacrjournals.org)
  • Integrin binds to a sequence of three amino acids (arginine-glycine-aspartic acid, also known as RGD). (phys.org)
  • Ma YQ , Qin J and Plow EF (2007) Platelet integrin alpha(IIb)beta(3): activation mechanisms. (els.net)
  • Integrin β3/Akt signaling contributes to platelet-induced hemangioendothelioma growth. (sigmaaldrich.com)
  • Furthermore, direct platelet-EOMA cell contact was required and the proliferation was mediated via integrin β3/Akt signaling in EOMA cells. (sigmaaldrich.com)
  • SiRNA knockdown of integrin β3 and inhibition of Akt activity significantly abolished platelet-induced EOMA cell proliferation in vitro and tumor development in vivo. (sigmaaldrich.com)
  • These include coxsackievirus A9 (CV-A9), echovirus 9, and human parechovirus 1 that are among the most common and epidemic human picornaviruses and bind to α V-integrins via RGD motif that resides on virus capsid. (hindawi.com)
  • Two of these, talin and kindlin, bind directly to the cytoplasmic domain of the integrin β subunit and are key regulators of integrin affinity ("inside-out" activation). (abcam.com)
  • Integrins carrying this domain either bind to collagens (e.g. integrins α1 β1, and α2 β1), or act as cell-cell adhesion molecules (integrins of the β2 family). (wikipedia.org)
  • The β2 integrins LFA-1 and Mac-1 (CD11a/CD18 and CD11b/CD18) bind to ICAM1, and the β1 integrins (such as VLA-4) bind VCAM1 . (humpath.com)
  • Moreover, intraperitoneal injection of the α V integrin blocking peptide cRGDfV (Calbiochem, United Kingdom) increased the growth response and also greatly reduced the calculated remodeling index. (ahajournals.org)
  • Thus, to the extent that the α V integrin blocking peptide is having a specific effect, and future experiments need to determine this, the results point to an important role for this integrin in the remodeling process. (ahajournals.org)
  • The mature α11 peptide is 1166-amino acid-long (M.W. 145 kDa in SDS-PAGE under non-reducing conditions), which is longer than any other currently identified integrin α-chain (with the closest being αE, which is composed of 1160 amino acids). (atlasgeneticsoncology.org)
  • By combining administration of an engineered mouse serum albumin/IL-2 fusion with an Fc fusion to an integrin-binding peptide (2.5F-Fc), significant survival improvements are achieved in three syngeneic mouse tumor models, including complete responses with protective immunity. (rupress.org)
  • Using peptide array technology, we identified set of overlapping peptides derived from the soluble CD23 sequence that interact with integrins expressed on the surface of monocytic cells and with purified αVβ3 and αVβ5 integrins in in vitro Biacore assays. (bl.uk)
  • CD98 heterodimers, comprised of a heavy chain (CD98hc, SLC3A2) and one of several light chains, interact with integrins through CD98hc. (pnas.org)
  • The acquisition of integrins such as α v β 3 has been correlated to the process of tumor progression in multiple tissues, suggesting that approaches effectively targeting the integrins might inhibit or reverse progression. (cancernetwork.com)
  • Substantial evidence from preclinical studies shows that increased expression of integrin αvβ3 in tumor cells promotes the metastatic and bone-invasive phenotype. (mdpi.com)
  • Integrin α v β 3 is a marker that is specifically and preferentially overexpressed on multiple tumor types and on angiogenic tumor neovasculature. (dovepress.com)
  • Stromal cells within a tumor microenvironment also play important roles in tumorigenesis and metastases, and many integrins are expressed in tumor-associated stromal components, including fibroblasts, vascular endothelial cells, and inflammatory cells. (aacrjournals.org)
  • In this issue of Clinical Cancer Research , Conti and colleagues make an important step toward deciphering how metastatic tumor cells manipulate their repertoire of integrins in response to altered ECM composition of the malignant organ to promote their growth and survival ( 3 ). (aacrjournals.org)
  • Collectively, these data suggest that in certain forms of cancer, αv integrins provide differential functions in tumor initiation versus tumor progression. (aacrjournals.org)
  • address this important topic by analyzing resected liver metastases derived from primary colorectal adenocarcinomas, and show that subpopulations of metastatic tumor cells express elevated levels of αvβ3 and αvβ5 integrins. (aacrjournals.org)
  • Furthermore, they show that tumor cells overexpressing these integrins preferentially reside near regions of tumor-induced fibrosis, or desmoplastic reactions. (aacrjournals.org)
  • Recently, integrins have emerged as a key target in anti-cancer therapy as integrins are involved in promoting tumor metastasis and cancer blood vessel formation. (fold.it)
  • Aim of this study was to investigate the role of integrins and Cdc42 in cell migration and in particular the cross-talk between these molecules. (uni-muenchen.de)
  • In Integrin Protocols, Anthony Howlett and a distinguished panel of experimentalists describe in detail a series of cutting-edge methods for dissecting the role of integrins in biological processes. (springer.com)
  • Determining the precise contributions of αv integrins to immune functions in vivo has been limited by the lethal phenotype of αv knockout mice, which die from vascular and developmental defects ( 2 ). (pnas.org)
  • To test this model in vivo, we mutated the integrin binding site of PDE4D5 in mice. (jci.org)
  • In vivo, the β 2 integrin-dependent recruitment of leukocytes to the inflamed peritoneum of uPAR-deficient mice was significantly reduced as compared with wild-type animals. (rupress.org)
  • We demonstrated now, that fourfold reduction of beta1 integrin expression in keratinocytes in vivo did not impair wound healing. (uni-muenchen.de)
  • Finally, we analysed the importance of specific amino acids of the intracellular domain of beta1 integrin in keratinocytes in vivo by generating 8 mice strains which in skin express only point or deletion mutants of beta1 integrin. (uni-muenchen.de)
  • Role of alpha 4-integrins in lymphocyte homing to mucosal tissues in vivo. (jimmunol.org)
  • Blocking α4 and β1 integrin chains in vivo restored erythroblastic differentiation and the erythropoietic stress response in Swap-70-/- mice. (haematologica.org)
  • Furthermore, CD98hc is required for efficient adhesion-induced activation of Akt and Rac GTPase, major contributors to the integrin-dependent signals involved in cell survival and cell migration. (pnas.org)
  • These data establish an important role for CD98hc in integrin-dependent signals that contribute to tumorigenesis. (pnas.org)
  • However, a key unresolved question is how integrins propagate signals across the plasma membrane. (nih.gov)
  • Integrins also are involved in transforming or translating cell signals. (biologynews.net)
  • First, we explored the ability of integrins to transmit mechanical signals in an in vitro model of tendon differentiation to explore whether integrins play a role in mechanotransduction at an early stage in the life of a tendon cell. (nature.com)
  • Cells are exposed to several types of integrin stimuli, which generate responses generally referred to as "integrin signals", but the specific responses to different integrin stimuli are poorly defined. (diva-portal.org)
  • In conclusion, the results showed that "integrin signals" are composedof separate sets of reactions triggered by different types of integrin stimulation. (diva-portal.org)
  • We conclude, therefore, that a novel integrin/contactin complex coordinates signals from extracellular matrix and the axonal surface to regulate both oligodendrocyte survival and myelination by controlling Fyn activity. (jneurosci.org)
  • Instead, CD98hc was involved in the cell's ability to exert force on the matrix and did so by dint of its capacity to interact with integrins to support downstream signals that lead to activation of RhoA small GTPase. (sigmaaldrich.com)
  • Integrin beta 7 associates with integrin alpha 4 (CD49d) to form the alpha 4 beta 7 integrin LPAM-1, expressed on intraepithelial lymphocytes. (fishersci.ca)
  • Homing to Peyer's patches but not to peripheral lymph nodes is inhibited by Fab fragments of mAb PS/2 against the alpha 4-integrin chain, by mAb DATK32 recognizing a combinatorial epitope on the alpha 4/beta 7-integrin, and by mAb FIB30 against the beta 7-chain. (jimmunol.org)
  • The results support a major, but not exclusive role of the alpha 4/beta 7-integrin in lymphocyte traffic to mucosal sites. (jimmunol.org)
  • Thus, integrins provide cells with the capacity to sense and respond to their microenvironment and they control vital cellular functions for embryonic development, tissue homoeostasis, blood clotting and immunity. (els.net)
  • These results support a model in which integrins are an upstream component of the mechanosensory cellular apparatus, regulating fundamental tendon cell functions relevant to exercise-induced adaptation and mechanotherapy. (nature.com)
  • CD98hc was not required for biosynthesis of cellular Fn or the maintenance of the repertoire or affinity of cellular Fn binding integrins, which are important contributors to Fn assembly. (sigmaaldrich.com)
  • Finally, overexpression of the portion of CD98hc that interacts with integrin β1A subunit leads to anchorage and serum-independent growth of CHO cells in vitro ( 10 ). (pnas.org)
  • ß2 integrin activation on T cells is also a critical step during the process of extravasation and recruitment of T cells within the atherosclerotic plaque. (uni-heidelberg.de)
  • We dissect the contribution of αv on different immune cell populations, identifying myeloid cells [macrophages, dendritic cells (DCs), and/or neutrophils] as the critical expressers of αv integrins. (pnas.org)
  • Integrins are embedded on the surfaces of all animal cells, connecting each cell to its surroundings and allowing it to communicate and respond to external forces. (ucsf.edu)
  • These linking elements are called "integrins" and they connect the inner and outer worlds of our cells. (yinyoga.com)
  • There are many types of integrin, and many cells have multiple types on their surface. (wikidoc.org)
  • Western blot analysis of Integrin β1 [pTpT 788/789 ] (Product # 44-872G ) was performed on extracts of serum-starved mitotic HeLa cells generated by treatment with 100 ng/mL taxol for 16 hours. (thermofisher.com)
  • The cells were divided into control, SBA treated groups, integrin inhibitor groups, and SBA + integrin inhibitor groups to determine the integrin function in SCA. (mdpi.com)
  • Deletion of alpha4 integrins from adult hematopoietic cells reveals roles in homeostasis, regeneration, and homing. (semanticscholar.org)
  • However, keratinocyte stem cells with normal levels of beta1 integrin had a competitive advantage over the hypomorphic cells and expanded steadily in the skin of mice harbouring both cell types in the epidermis. (uni-muenchen.de)
  • Because the initial critical step in ovarian cancer metastasis is the attachment of cancer cells to the peritoneum or omentum and because clinical trials have provided positive results for anti-angiogenic therapy, therapies targeting integrins may be the most feasible approach for treating cancer. (mdpi.com)
  • It also associates with alpha E (CD103) to form the alpha E beta 7 integrin HML-1, expressed on T cells adjacent to mucosal epithelium and intraepithelial lymphocytes. (fishersci.ca)
  • Integrin beta 7 plays an important role in the adhesion of leukocytes to endothelial cells promoting the transmigration of leukocytes to extravascular spaces during the inflammatory response. (fishersci.ca)
  • Although LFA-1 is expressed on virtually all leukocytes and is the major, but not exclusive, CD18-related T cell integrin, other integrins expressed on T cells include VLA-4 (CD49d/CD29) and integrin β 7 ( 8 , 9 ). (jimmunol.org)
  • CD61 is a 90-110 kDa member of the beta integrin family expressed by a wide variety of cells, including leukocytes, platelets, endothelial and smooth muscle cells. (fishersci.com)
  • Several recent publications have provided mechanistic insight into how integrin traffic is regulated in cells. (biologists.org)
  • It has become clear that during gastrulation - a period during which cells participate in morphogenetic movements that lead to the generation of a tripoblastic embryo - the integrin repertoire of each cell is in constant flux. (uwaterloo.ca)
  • This study reveals that cells form early adhesions from integrin clusters as a first response to their environment, and that these universal, modular units of adhesion assemble without the need for external stimuli from the surrounding surface. (phys.org)
  • We show that Crim1 acts in LE cells, where it colocalizes with and regulates the levels of active β1 integrin and of phosphorylated FAK and ERK. (biologists.org)
  • Substitution of the residues in the RKC motif reduced or abolished binding of the peptides to integrins expressed on cells and in vitro, as measured by Biacore analysis, and abolished the competition with CD23. (bl.uk)
  • Most monocytic cells will express a combination of the different CD23-binding integrins simultaneously and, therefore, the cytokine output of that cell will be the net result of the interaction of CD23 with a combination of integrins. (bl.uk)
  • Epithelial cells expressing either β1 or β3 integrins, in which p53 activity is suppressed, undergo G 2 arrest but show little apoptosis after treatment with cisplatin or other genotoxicants. (aspetjournals.org)
  • The apoptotic response is strongly enhanced by the c-Src[Y530F] oncogene in cells expressing β1 integrins, whereas such sensitization is reduced when these cells are engineered to express β3 integrins instead. (aspetjournals.org)