The alpha2beta1 integrin: a novel collectin/C1q receptor. 2007

Mary M Zutter, and Brian T Edelson
Department of Pathology, Cancer Biology and Immunology, Vanderbilt University School of Medicine, C3321A MCN, 1161 21st Avenue S, Nashville, TN 37232, USA. mary.zutter@vanderbilt.edu

Our laboratory focuses on the alpha2beta1 integrin, a receptor for a number of matrix and non-matrix ligands, including collagens, laminins, decorin, E-cadherin, matrix metalloproteinase-1 (MMP-1), endorepellin, and several viruses. The alpha2beta1 integrin is expressed on numerous different cell types, including epithelial cells, endothelial cells, fibroblasts, and hematopoietic elements, including platelets and specific subsets of leukocytes. Although alpha2beta1 integrin expression is widespread, it is not ubiquitous. Rather, it is expressed in a differentiation-dependent and activation-dependent manner. Interactions between the alpha2beta1 integrin and extracellular matrix ligands have been implicated in important biological processes including inflammation and immunity. Studies from a number of laboratories have demonstrated a role for the alpha2beta1 integrin during the immune response. Our laboratory generated an alpha2beta1 integrin-deficient mouse to define the role of the alpha2beta1 integrin in vivo. Our studies demonstrated that the alpha2-null mice have a profound defect in the innate immune response. We have recently reported the identification of a novel family of ligands for the alpha2beta1 integrin, which include C1q and the collectins. The goal of this article is to review the important role that the interaction between the alpha2beta1 integrin and C1q plays in the innate immune response. The identification of C1q and the collectins as ligands for the alpha2beta1 integrin suggests that the integrin may play important roles in a number of immunological responses.

UI MeSH Term Description Entries
D007113 Immunity, Innate The capacity of a normal organism to remain unaffected by microorganisms and their toxins. It results from the presence of naturally occurring ANTI-INFECTIVE AGENTS, constitutional factors such as BODY TEMPERATURE and immediate acting immune cells such as NATURAL KILLER CELLS. Immunity, Native,Immunity, Natural,Immunity, Non-Specific,Resistance, Natural,Innate Immune Response,Innate Immunity,Immune Response, Innate,Immune Responses, Innate,Immunity, Non Specific,Innate Immune Responses,Native Immunity,Natural Immunity,Natural Resistance,Non-Specific Immunity
D008407 Mast Cells Granulated cells that are found in almost all tissues, most abundantly in the skin and the gastrointestinal tract. Like the BASOPHILS, mast cells contain large amounts of HISTAMINE and HEPARIN. Unlike basophils, mast cells normally remain in the tissues and do not circulate in the blood. Mast cells, derived from the bone marrow stem cells, are regulated by the STEM CELL FACTOR. Basophils, Tissue,Basophil, Tissue,Cell, Mast,Cells, Mast,Mast Cell,Tissue Basophil,Tissue Basophils
D008562 Membrane Glycoproteins Glycoproteins found on the membrane or surface of cells. Cell Surface Glycoproteins,Surface Glycoproteins,Cell Surface Glycoprotein,Membrane Glycoprotein,Surface Glycoprotein,Glycoprotein, Cell Surface,Glycoprotein, Membrane,Glycoprotein, Surface,Glycoproteins, Cell Surface,Glycoproteins, Membrane,Glycoproteins, Surface,Surface Glycoprotein, Cell,Surface Glycoproteins, Cell
D011951 Receptors, Complement Molecules on the surface of some B-lymphocytes and macrophages, that recognize and combine with the C3b, C3d, C1q, and C4b components of complement. Complement Receptors,Complement Receptor,Complement Receptor Type 1,Receptor, Complement
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D015850 Interleukin-6 A cytokine that stimulates the growth and differentiation of B-LYMPHOCYTES and is also a growth factor for HYBRIDOMAS and plasmacytomas. It is produced by many different cells including T-LYMPHOCYTES; MONOCYTES; and FIBROBLASTS. Hepatocyte-Stimulating Factor,Hybridoma Growth Factor,IL-6,MGI-2,Myeloid Differentiation-Inducing Protein,Plasmacytoma Growth Factor,B Cell Stimulatory Factor-2,B-Cell Differentiation Factor,B-Cell Differentiation Factor-2,B-Cell Stimulatory Factor 2,B-Cell Stimulatory Factor-2,BSF-2,Differentiation Factor, B-Cell,Differentiation Factor-2, B-Cell,IFN-beta 2,IL6,Interferon beta-2,B Cell Differentiation Factor,B Cell Differentiation Factor 2,B Cell Stimulatory Factor 2,Differentiation Factor 2, B Cell,Differentiation Factor, B Cell,Differentiation-Inducing Protein, Myeloid,Growth Factor, Hybridoma,Growth Factor, Plasmacytoma,Hepatocyte Stimulating Factor,Interferon beta 2,Interleukin 6,Myeloid Differentiation Inducing Protein,beta-2, Interferon
D037222 Collectins A class of C-type lectins that target the carbohydrate structures found on invading pathogens. Binding of collectins to microorganisms results in their agglutination and enhanced clearance. Collectins form trimers that may assemble into larger oligomers. Each collectin polypeptide chain consists of four regions: a relatively short N-terminal region, a collagen-like region, an alpha-helical coiled-coil region, and carbohydrate-binding region. Collagenous Lectins,Collectin,Lectins, Collagenous
D038982 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. CD49b-CD29,Glycoprotein Ia-IIa,Platelet Membrane Glycoprotein Heterodimer Ia-IIa,VLA-2,Very Late Antigen-2,alpha2beta1Integrin,CD49b CD29,Glycoprotein Ia IIa,Late Antigen-2, Very,Platelet Membrane Glycoprotein Heterodimer Ia IIa,VLA 2,Very Late Antigen 2,alpha2beta1, Integrin

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