NationMaster - Encyclopedia: Integrin

Integrins are cell surface receptors that interact with the extracellular matrix and mediate various intracellular signals. They define cellular shape, mobility, and regulate the cell cycle. These integral membrane proteins are attached to the cellular plasma membrane through a single transmembrane helix. In biochemistry, a receptor is a protein on the cell membrane or within the cytoplasm or cell nucleus that binds to a specific molecule (a ligand), such as a neurotransmitter, hormone, or other substance, and initiates the cellular response to the ligand. ... Illustration depicting extracellular matrix (basement membrane and interstitial matrix) in relation to epithelium, endothelium and connective tissue In biology, the extracellular matrix (ECM) is the extracellular part of animal tissue that usually provides structural support to the cells in addition to performing various other important functions. ... Cell signaling is part of a complex system of communication that governs basic cellular activities and coordinates cell actions. ... The cell cycle, or cell-division cycle, is the series of events that take place in a eukaryotic cell leading to its replication. ... An Integral Membrane Protein (IMP) is a protein molecule (or assembly of proteins) that is permanently attached to the biological membrane. ... Drawing of a cell membrane A component of every biological cell, the cell membrane (or plasma membrane) is a thin and structured bilayer of phospholipid and protein molecules that envelopes the cell. ... Transmembrane domain usually denotes a single transmembrane alpha helix of a transmembrane protein. ...

Integrin plays a role in the attachment of cells to other cells, and also plays a role in the attachment of a cell to the material part of a tissue that is not part of any cell (the extracellular matrix). Besides the attachment role, integrin also plays a role in signal transduction, a process by which a cell transforms one kind of signal or stimulus into another. The signal that the integrin converts comes from the extracellular matrix to the cell. Illustration depicting extracellular matrix (basement membrane and interstitial matrix) in relation to epithelium, endothelium and connective tissue In biology, the extracellular matrix (ECM) is the extracellular part of animal tissue that usually provides structural support to the cells in addition to performing various other important functions. ... In biology, signal transduction refers to any process by which a cell converts one kind of signal or stimulus into another, most often involving ordered sequences of biochemical reactions inside the cell, that are carried out by enzymes and linked through second messengers resulting in what is thought of as...

There are many types of integrin, and many cells have multiple types on their surface. Integrins are of vital importance to all animals and have been found in many animals tested, from sponges to mammals. Integrins have been extensively studied in humans. The word Animals when used alone has several possible meanings in the English language. ...

Other types of protein that play a role in cell-cell and cell-matrix interaction and communication are cadherins, CAMs and selectins. A representation of the 3D structure of myoglobin, showing coloured alpha helices. ... Cadherins are a class of proteins which are expressed on the surface of cells. ... Cell Adhesion Molecules (CAMs) are proteins located on the cell surface involved with the binding with other cells or with the extracellular matrix (ECM) in the process called cell adhesion. ... Selectins are a family of cell-surface adhesion molecules of leukocytes and endothelial cells. ...

Structure

Integrins are obligate heterodimers containing two distinct chains, called the α (alpha) and β (beta) subunits. In mammals, 19 α and 8 β subunits have been characterized, whereas the Drosophila and Caenorhabditis genomes encode only five α and two β subunits.^[1] Look up obligate in Wiktionary, the free dictionary. ... Sucrose, or common table sugar, is composed of glucose and fructose. ... Subclasses & Infraclasses Subclass â€ Allotheria* Subclass Prototheria Subclass Theria Infraclass â€ Trituberculata Infraclass Metatheria Infraclass Eutheria Mammals (class Mammalia) are warm-blooded, vertebrate animals characterized by the presence of sweat glands, including those that produce milk, and by the presence of: hair, three middle ear bones used in hearing, and a neocortex... Type species Drosophila funebris (Fabricius, 1787) Drosophila is a genus of small flies, belonging to the family Drosophilidae, whose members are often called fruit flies, or more appropriately vinegar flies, wine flies, pomace flies, grape flies, and picked fruit-flies, a reference to the characteristic of many species to linger... This genus contains the noted model organism Caenorhabditis elegans and several other species for which a genome sequence is available for, or which is currently being determined. ... In biology the genome of an organism is the whole hereditary information of an organism that is encoded in the DNA (or, for some viruses, RNA). ...

In addition, variants of some of the subunits are formed by differential splicing, for example 4 variants of the beta-1 subunit exist. Through different combinations of these alpha and beta subunits, some 24 unique integrins are generated, although the number varies according to different studies. ^[2] CD49a is an integrin alpha subunit. ... CD49b is an integrin alpha subunit. ... Expression pattern Orthologs Human Mouse Entrez Ensembl Uniprot Refseq Location Pubmed search Integrin, alpha 2b (platelet glycoprotein IIb of IIb/IIIa complex, antigen CD41), also known as ITGA2B, is a human gene. ... CD49c is an integrin alpha subunit. ... CD49d is an integrin alpha subunit. ... Expression pattern Orthologs Human Mouse Entrez Ensembl Uniprot Refseq Location Pubmed search Integrin, alpha 5 (fibronectin receptor, alpha polypeptide), also known as ITGA5, is a human gene. ... CD11a is one of the two components of lymphocyte function-associated antigen-1. ... Integrin alpha M is a protein involved in the complement system. ... Expression pattern Orthologs Human Mouse Entrez Ensembl Uniprot Refseq Location Pubmed search Integrin, alpha V (vitronectin receptor, alpha polypeptide, antigen CD51), also known as ITGAV, is a human gene. ... CDC11c is a type I transmembrane protein found at high levels on most human dendritic cells, but also on monocytes, macrophages, neutrophils, and some B cells that induces cellular activation and helps trigger neutrophil respiratory burst; expressed in hairy cell leukemias, acute nonlymphocytic leukemias, and some B-cell chronic lymphocytic... CD29 is an integrin unit associated with very late antigen receptors. ... CD18 is the beta subunit of LFA-1. ... CD61 is a cluster of differentiation found on thrombocytes. ...

Integrin subunits span the plasma membrane and in general have very short cytoplasmic domains of about 40-70 amino acids. The exception is the beta-4 subunit which has a cytoplasmic domain of 1088 amino acids, one of the largest known cytoplasmic domains of any membrane protein. Outside the cell plasma membrane, the alpha and beta chains lie close together along a length of about 23nm, the final 5nm N-termini of each chain form a ligand-binding region for the ECM, or extracellular matrix. Drawing of a cell membrane A component of every biological cell, the cell membrane (or plasma membrane) is a thin and structured bilayer of phospholipid and protein molecules that envelopes the cell. ... This article is about the class of chemicals. ... Drawing of a cell membrane A component of every biological cell, the cell membrane (or plasma membrane) is a thin and structured bilayer of phospholipid and protein molecules that envelopes the cell. ... A nanometre (American spelling: nanometer, symbol nm) is a unit of length in the metric system, equal to one thousand-millionth of a metre, which is the current SI base unit of length. ... The N-terminal end refers to the extremity of a protein or polypeptide terminated by an amino acid with a free amine group (NH2). ... It has been suggested that this article or section be merged with ligand. ... Illustration depicting extracellular matrix (basement membrane and interstitial matrix) in relation to epithelium, endothelium and connective tissue In biology, the extracellular matrix (ECM) is the extracellular part of animal tissue that usually provides structural support to the cells in addition to performing various other important functions. ...

The molecular mass of the integrin subunits can vary from 90 kDa to 160 kDa. β subunits have four cysteine-rich repeated sequences. Both α and β subunits bind several divalent cations. The role of the α cations is unknown, but they may stabilize the folds of the protein. The β cations are more interesting: they are directly involved in coordinating at least some of the ligands that integrins bind. The molecular mass (abbreviated Mr) of a substance, formerly also called molecular weight and abbreviated as MW, is the mass of one molecule of that substance, relative to the unified atomic mass unit u (equal to 1/12 the mass of one atom of carbon-12). ... The unified atomic mass unit (u), or dalton (Da), is a small unit of mass used to express atomic and molecular masses. ... Cysteine is a naturally occurring, sulfur-containing amino acid that is found in most proteins, although only in small quantities. ... In chemistry, divalent anions are atoms or radicals with 2 additional electrons when compared to their elemental state (that is, with 2 more electrons than protons); for instance, S-- is the sulfide anion. ... A cation is an ion with positive charge. ... It has been suggested that this article or section be merged with ligand. ...

There are various ways of categorizing the integrins. For example, a subset of the α chains has an additional structural element (or "domain") inserted toward their N-terminal, the so called alpha-A domain (because it has a similar structure to the A-domains found in the protein von Willebrand factor: it is also termed the α-I domain). 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). This α-I domain is the binding site for ligands of such integrins. 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 chain. The N-terminal end refers to the extremity of a protein or polypeptide terminated by an amino acid with a free amine group (NH2). ... Von Willebrand factor is a blood glycoprotein of the coagulation system. ... Tropocollagen triple helix. ... Drawing of the structure of cork as it appeared under the microscope to Robert Hooke from Micrographia which is the origin of the word cell being used to describe the smallest unit of a living organism Cells in culture, stained for keratin (red) and DNA (green) The cell is the...

In both cases, the A-domains carry up to three divalent cation binding sites. One is permanently occupied in physiological concentrations of divalent cations, and carries either a calcium or magnesium ion, the principal divalent cations in blood at median concentrations of 1.4 mM (calcium) and 0.8 mM (magnesium). The other two sites become occupied by cations when ligands bind - at least for those ligands involving an acidic amino acid in their interaction sites. An acidic amino acid features in the integrin-interaction site of many ECM proteins, for example, as part of the amino acid sequence Arginine-Glycine-Aspartic acid ("RGD" in the one-letter aminoacid code). For other uses, see Concentration (disambiguation). ... Arginine (abbreviated as Arg or R)[1] is an Î±-amino acid. ... For the plant, see Glycine (plant). ... Aspartic acid (abbreviated as Asp or D; Asx or B represent either aspartic acid or asparagine[1] ) is an Î±-amino acid with the chemical formula HO2CCH(NH2)CH2CO2H. The L-isomer is a protonated varient of one of the 20 proteinogenic amino acids, i. ...

High resolution structure

Despite many years of effort, discovering the high resolution structure of integrins proved to be challenging: membrane proteins are classically difficult to purify, and integrins are also large, complex and linked to many sugar trees ("highly glycosylated"). Low resolution images of detergent extracts of intact integrin GPIIbIIIa, obtained using electron microscopy, and even data from indirect techniques, investigating the solution properties of integrins using ultracentrifugation and light scattering, were combined with fragmentary high resolution crystallographic or NMR data from single or paired domains of single integrin chains, and molecular models postulated for the rest of the chains. Despite these wide-ranging efforts, the X-ray crystal structure obtained for the complete extracellular region of one integrin, αvβ3 was a surprise.^[3] In the NATO phonetic alphabet, X-ray represents the letter X. An X-ray picture (radiograph) taken by Röntgen An X-ray is a form of electromagnetic radiation with a wavelength approximately in the range of 5 pm to 10 nanometers (corresponding to frequencies in the range 30 PHz...

It showed the molecule to be folded into an inverted V-shape which brings the ligand-binding sites close to the cell membrane. Perhaps more importantly, the crystal structure was also obtained for the same integrin bound to a small ligand containing the RGD-sequence, the drug cilengitide.^[4] As detailed above, this finally revealed why divalent cations (in the A-domains) are critical for RGD-ligand binding to integrins. The interaction with such sequences is believed to be a primary switch by which ECM exerts its effects on cell behaviour. Cilengitide is a molecule found in snake venom which is useful in research on integrins, because of its RGD peptide sequence. ...

The structure poses many questions, especially regarding ligand binding and signal transduction. The ligand binding site is directed towards the C-terminal of the integrin, the region where the molecule emerges from the cell membrane. If it emerges orthogonally from the membrane, the ligand binding site would apparently be obstructed, especially as integrin ligands are typically massive, and well cross-linked components of the ECM. In fact, little is known about the angle which membrane proteins subtend to the plane of the membrane - it is a problem difficult to address with available technologies. The default assumption is that they emerge rather like little lollipops - the evidence for this sweet supposition is noticeable by its absence. The integrin structure has drawn attention to this problem, which may have implications for how membrane proteins work. In mathematics, orthogonal is synonymous with perpendicular when used as a simple adjective that is not part of any longer phrase with a standard definition. ...

Although the crystal structure changed surprisingly little after binding to cilengitide, the current hypothesis is that integrin function involves changes in shape to move the ligand binding site into a more accessible position away from the cell surface, and this shape change also triggers intracellular signaling. And there is a wide body of cell biological and biochemical literature that supports this view. Perhaps the most convincing evidence involves the use of antibodies that only recognize integrins when they have bound to their ligands, or are activated. As the "footprint" that an antibody makes on its binding target is roughly a circle about 3 nm in diameter, the resolution of this technique is low. Nevertheless, these so-called LIBS (Ligand-Induced-Binding-Sites) antibodies unequivocally show that dramatic changes in integrin shape routinely occur. Each antibody binds to a specific antigen; an interaction similar to a lock and key. ...

Function

However, they are also involved in a wide range of other biological activities. These include: binding of viruses, including adenovirus, Echo viruses, Hanta viruses and foot and mouth disease viruses, to cells; immune patrolling. Cell migration. Genera Mastadenovirus Aviadenovirus Atadenovirus Siadenovirus Adenoviruses are viruses of the family Adenoviridae. ... Foot-and-mouth disease (FMD), sometimes called hoof-and-mouth disease, is a highly contagious but non-fatal viral disease of cattle and pigs. ...

A very prominent function of the integrins is seen in the molecule GPIIbIIIa, an integrin on the surface of blood platelets (thrombocytes) responsible for cross-linking platelets in fibrin within a developing blood clot. This switches its adhesiveness for fibrin/fibrinogen from being non-adhesive to being intensely sticky, in a fast and precisely controlled manner. As such it provides a thought-model for how many integrins are believed to be regulated. As you may have noted, although blood is normally very rich in platelets, we do not spontaneously clot. This is clearly good news. On the other side, and equally positively, even minor wounds are rapidly blocked by the mass of fibrin, platelets and erythrocytes in a blood clot. A primary event in clot formation is the binding of platelets to exposed collagen in the wound site, which leads to their "activation", and a clotting cascade. Among the many molecular events during activation, is the switching of gpiiaiib integrin from a quiescent state, unable to bind to fibrinogen/fibrin, to an active state, able to bind strongly to fibrinogen/fibrin. This is a remarkable event: first it involves all the gpiibiia on a single platelet (some 50000 molecules), second it is completed within 5 seconds, third, it increases the affinity of the integrin concerned over several orders of magnitude. Fourth, it involves wide spread changes in the molecular structure of the GPIIbIIIa molecule, as resolved by LIBS antibodies, which gain the ability to bind GPIIbIIIa only following activation of the platelets. Finally, it is intensely locallized to the precise region of the damage, be it a couple of square micrometres, or the results of falling off a mountain bike at high speed.

Attachment of cell to the ECM

Integrins couple the ECM outside a cell to the cytoskeleton (in particular the microfilaments) inside the cell. Which ligand in the ECM the integrin can bind to is mainly decided by which α and β subunits the integrin is made of. Among the ligands of integrins are fibronectin, vitronectin, collagen, and laminin. The connection between the cell and the ECM enables the cell to endure pulling forces without being ripped out of the ECM. The ability of a cell to create this kind of bond is also of vital importance in ontogeny. The eukaryotic cytoskeleton. ... This article or section should be merged with actin Microfilaments or actin filaments are made up of two twisted monomeric actin subunits. ... In chemistry, a ligand is an atom, ion, or molecule (see also: functional group) that generally donates one or more of its electrons through a coordinate covalent bond to, or shares its electrons through a covalent bond with, one or more central atoms or ions (these ligands act as a... Fibronectin is a high-molecular-weight glycoprotein containing about 5% carbohydrate that binds to receptor proteins that span the cells membrane, called integrins. ... Vitronectin is an abundant glycoprotein found in blood plasma and the extracellular matrix. ... Tropocollagen triple helix. ... Laminins are the major non-collagenous component of the basal lamina, such as those on which cells of an epithelium sit. ... Ontogeny (also ontogenesis or morphogenesis) describes the origin and the development of an organism from the fertilized egg to its mature form. ...

Cell attachment to the ECM is a basic requirement to build a multicellular organism. Integrins are not simply hooks, but give the cell critical signals about the nature of its surroundings. Together with signals arising from receptors for soluble growth factors like VEGF, EGF and many others, they enforce a cellular decision on what biological action to take, be it attachment, movement, death, or differentiation. Thus integrins lie at the heart, both literally and figuratively, of many cellular biological processes. The attachment of the cell takes place through formation of cell adhesion complexes, which consist of integrins and many cytoplasmic proteins which include talin, vinculin, paxillin and alpha-actinin. These act by regulating kinases like FAK (focal adhesion kinase) and Src kinase family members to phosphorylate substrates such as p130CAS thereby recruiting signaling adaptors such as Crk. These adhesion complexes attach to the actin cytoskeleton. The integrins thus serve to link across the plasma membrane two networks: the extracellular ECM and the intracellular actin filamentous system. Vascular endothelial growth factor or VEGF is an important signal protein involved in angiogenesis. ... Epidermal Growth Factor or EGF is a 6045 Da protein with 53 amino acid residues and three intramolecular disulfide bonds. ... Schematic of cell adhesion The study of cell adhesion is part of cell biology. ... Talin is protein which connects integrin to the cytoskeleton. ... The adherent culture of BPAE cells featured in the digital image above was immunofluorescently labeled with primary anti-vinculin mouse monoclonal antibodies followed by goat anti-mouse Fab heavy and light chain fragments conjugated to Rhodamine Red-X. (www. ... In biochemistry, a kinase is a type of enzyme that transfers phosphate groups from high-energy donor molecules, such as ATP, to specific target molecules (substrates); the process is termed phosphorylation. ...

One of their most important functions of surface integrins is their role in cell migration. Cells adhere to a substrate through their integrins. During movement, the cell makes new attachments to the substrate at its front and concurrently releases those at its rear. When released from the substrate, integrin molecules are taken back into the cell by endocytosis; they are transported through the cell to its front by the endocytic cycle where they are added back to the surface. In this way they are cycled for reuse, enabling the cell to make fresh attachments at its leading front. Cell migration is a central process in the development and maintenance of multicellular organisms. ... For other uses, see Substrate. ... Endocytosis (IPA: ) is a process whereby cells absorb material (molecules such as proteins) from the outside by engulfing it with their cell membrane. ... It has been suggested that this article or section be merged into Endocytosis. ...

Signal transduction

Integrins play an important role in cell signaling. Connection with ECM molecules can cause a signal to be relayed into the cell through protein kinases that are connected with the intracellular end of the integrin molecule. In biochemistry, a kinase is a type of enzyme that transfers phosphate groups from high-energy donor molecules, such as ATP, to specific target molecules (substrates); the process is termed phosphorylation. ...

The term cell growth is used in two different ways in biology. ... This does not adequately cite its references or sources. ... Embryonic stem cells differentiate into cells in various body organs. ... A section of mouse liver showing an apoptotic cell indicated by an arrow Apoptosis (pronounced apo tÅ sis) is a process of suicide by a cell in a multicellular organism. ...

Selected vertebrate integrins

Tropocollagen triple helix. ... Laminins are the major non-collagenous component of the basal lamina, such as those on which cells of an epithelium sit. ... Integrin alpha4beta1 (Very Late Antigen-4) is an integrin dimer. ... Red blood cells (erythrocytes) are present in the blood and help carry oxygen to the rest of the cells in the body Blood is a circulating tissue composed of fluid plasma and cells (red blood cells, white blood cells, platelets). ... Fibronectin is a high-molecular-weight glycoprotein containing about 5% carbohydrate that binds to receptor proteins that span the cells membrane, called integrins. ... VCAM-1 (vascular cell adhesion molecule-1), also known as CD106, is a molecule with a considerable role in the human immune system. ... NIH/3T3 Fibroblasts A fibroblast is a type of cell that synthesizes and maintains the extracellular matrix of many animal tissues. ... LFA-1 stands for Lymphocyte function-associated antigen-1. ... T cells are a subset of lymphocytes that play a large role in the immune response. ... Intercellular adhesion molecules (ICAMs) are molecules that promote adhesion between cells. ... Intercellular adhesion molecules are members a family of cell adhesion molecules. ... Macrophage-1 antigen (or integrin alphaMbeta2) is a complement receptor (CR3) consisting of CD11b and CD18. ... Monocyte A monocyte is a leukocyte, part of the human bodys immune system that protects against blood-borne pathogens and moves quickly (aprox. ... Look up Serum in Wiktionary, the free dictionary. ... A 250 ml bag of newly collected platelets. ... In zootomy, epithelium is a tissue composed of a layer of cells. ... Laminins are the major non-collagenous component of the basal lamina, such as those on which cells of an epithelium sit. ...

Additional images

References

External links

Categories: Cell signaling | Signal transduction | Transmembrane proteins | Cell adhesion proteins Typical structure of a chemokine receptor, with seven transmembrane domains and a characteristic DRY motif in the second intracellular domain. ... TGFÎ² receptors are single pass serine/threonine kinase receptors. ... A tumor necrosis factor receptor (TNFR) is, as its name would indicate, a receptor which binds tumor necrosis factors (TNF). ... Pattern recognition receptors, or PRRs, are a class of cell surface receptors which are employed by the cells of the immune system to identify foreign (disease-associated) biomolecules in the body. ... Toll-like receptors (TLRs) are type I transmembrane proteins that serve as a key part of the innate immune system. ... TLR 1 is a member of the Toll-like receptor family of pattern recognition receptors of the innate immune system. ... TLR-2 is the name for a biomolecule, which plays a role in the human immune system. ... TLR 3 is one of 11 Toll-like receptors part of the innate immune system. ... TLR 4 is a toll-like receptor. ... TLR 5 is a toll-like receptor. ... TLR 6 is a toll-like receptor. ... TLR 7 is a toll-like receptor. ... TLR 8 is a toll-like receptor. ... TLR 9 is a toll-like receptor. ... TLR 10 is a toll-like receptor. ... // Fc-receptor(s) Introduction Fc-receptor(s) are structures on the surface of cells and can contribute to the protective functions of the immune system. ... FcÎµRI, or Fc epsilon RI, is the high-affinity receptor for immunoglobulin E (IgE), an antibody isotype involved in allergy and (arguably) resistance to parasites. ... CD23 or Fc epsilon RII is the low affinty receptor for IgE, an antibody isotype involved in allergy and (arguably) resistance to parasites and is important in regulation of IgE levels. ... CD64 is a Fc receptor. ... The CD32 in action The AmigaCD32 was the worlds first 32bit CD_ROM based game console. ... CD16 is a Fc receptor. ... CD89 is a Fc receptor. ... FcÎ±/Î¼R is a Fc receptor. ... The neonatal Fc receptor is a Fc receptor which is similar in structure to MHC Class I. MeSH neonatal+Fc+receptor Transmembrane receptors: immune receptors Antigen receptor (B-cell receptor, T cell receptor) - Complement - Fc (FcÎµRI, FcÎµRII, FcÎ³RI, FcÎ³RII, FcÎ³RIII, FcÎ±RI, FcÎ±/Î¼R, Neonatal... Lymphocyte homing receptors are cell adhesion molecules which target addressins. ... The CD44 protein is a cell-surface glycoprotein involved in cell-cell interactions, cell adhesion and migration. ... L-selectin, also known as CD62L, is a cell adhesion molecule found on leukocytes. ... Integrin alpha4beta1 (Very Late Antigen-4) is an integrin dimer. ... LFA-1 stands for Lymphocyte function-associated antigen-1. ... This article or section is in need of attention from an expert on the subject. ... Antigen presentation stimulates T cells to become either cytotoxic CD8+ cells or helper CD4+ cells. ... A Complement receptor is a receptor of the complement system, a part of the mediated innate immune system. ... A formyl peptide receptor is a member of a class of G protein-coupled receptors involved in chemotaxis. ... It has been suggested that this article or section be merged into Immunophilin. ... Killer-cell immunoglobulin-like receptors (KIRs), are a family of cell surface proteins found on important cells of the immune system called natural killer (NK) cells. ... This does not cite any references or sources. ... A membrane protein is a protein molecule that is attached to, or associated with the membrane of a cell or an organelle. ... Cell Adhesion Molecules (CAMs) are proteins located on the cell surface involved with the binding with other cells or with the extracellular matrix (ECM) in the process called cell adhesion. ... Cell Adhesion Molecules (CAMs) are proteins located on the cell surface involved with the binding with other cells or with the extracellular matrix (ECM) in the process called cell adhesion. ... Neural Cell Adhesion Molecule (NCAM, also the cluster of differentiation CD56) is a homophilic binding glycoprotein expressed on the surface of neurons, glia and skeletal muscle. ... Myelin protein zero is a glycoprotein associated with Charcot-Marie-Tooth disease. ... Intercellular adhesion molecules (ICAMs) are molecules that promote adhesion between cells. ... Intercellular adhesion molecules (ICAMs) are molecules that promote adhesion between cells. ... ICAM4 is an intercellular adhesion molecule responsible for the Landsteiner-Wiener blood type. ... VCAM-1 (vascular cell adhesion molecule-1), also known as CD106, is a molecule with a considerable role in the human immune system. ... CD31 is a cluster of differentiation molecule. ... L1 is a transmembrane protein; it is a neuronal cell adhesion molecule, member of the L1 protein family. ... Cadherins are a class of proteins which are expressed on the surface of cells. ... The desmogleins are a family of cadherins consisting of proteins DSG1, DSG2, DSG3, and DSG4. ... T-cadherin is a unique member of cadherin superfamily because it lacks the transmembrane and cytoplasmic domains and is anchored to the cells membrane through the GPI anchor. ... Selectins are a family of cell-surface adhesion molecules of leukocytes and endothelial cells. ... E-selectin, also known as CD62E, is a cell adhesion molecule expressed only on endothelial cells activated by cytokines. ... L-selectin, also known as CD62L, is a cell adhesion molecule found on leukocytes. ... P-selectin is a cell adhesion molecule (CAM) found in granules in endothelial cells (cells lining blood vessels) and activated platelets. ... LFA-1 stands for Lymphocyte function-associated antigen-1. ... Integrin alphaXbeta2 (p150,95, CR4) is a complement receptor composed of CD11c and CD18. ... Macrophage-1 antigen (or integrin alphaMbeta2) is a complement receptor (CR3) consisting of CD11b and CD18. ... Integrin alpha4beta1 (Very Late Antigen-4) is an integrin dimer. ... In medicine, glycoprotein IIb/IIIa, also gpIIb/IIIa, is an integrin found on platelets. ... Carcinoembryonic antigen (CEA) is a glycoprotein involved in cell adhesion. ... CD22 or cluster of differentiation-22, is a molecule belonging to the SIGLEC family of lectins. ... CD24 is a cell adhesion molecule. ... The CD44 protein is a cell-surface glycoprotein involved in cell-cell interactions, cell adhesion and migration. ... CD146 is a cell adhesion molecule. ... CD164 is a cell adhesion molecule. ...

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