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Matricellular Proteins
A matricellular protein is a dynamically expressed non-structural protein that is present in the extracellular matrix (ECM). Rather than serving as stable structural elements in the ECM, these proteins are rapidly turned over and have regulatory roles. They characteristically contain binding sites for ECM structural proteins and cell surface receptors, and may sequester and modulate activities of specific growth factors. Examples of matricellular proteins include the CCN family of proteins (also known as CCN intercellular signaling protein), fibulins, osteopontin, periostin, SPARC family members, tenascin(s), and thrombospondins. Many of these proteins have important functions in wound healing and tissue repair. See also * CCN protein CCN proteins are a family of extracellular matrix (ECM)-associated proteins involved in intercellular signaling. Due to their dynamic role within the ECM they are considered matricellular proteins. Background The acronym CCN is derived from the fi ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Protein
Proteins are large biomolecules and macromolecules that comprise one or more long chains of amino acid residues. Proteins perform a vast array of functions within organisms, including catalysing metabolic reactions, DNA replication, responding to stimuli, providing structure to cells and organisms, and transporting molecules from one location to another. Proteins differ from one another primarily in their sequence of amino acids, which is dictated by the nucleotide sequence of their genes, and which usually results in protein folding into a specific 3D structure that determines its activity. A linear chain of amino acid residues is called a polypeptide. A protein contains at least one long polypeptide. Short polypeptides, containing less than 20–30 residues, are rarely considered to be proteins and are commonly called peptides. The individual amino acid residues are bonded together by peptide bonds and adjacent amino acid residues. The sequence of amino acid residue ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Extracellular Matrix
In biology, the extracellular matrix (ECM), also called intercellular matrix, is a three-dimensional network consisting of extracellular macromolecules and minerals, such as collagen, enzymes, glycoproteins and hydroxyapatite that provide structural and biochemical support to surrounding cells. Because multicellularity evolved independently in different multicellular lineages, the composition of ECM varies between multicellular structures; however, cell adhesion, cell-to-cell communication and differentiation are common functions of the ECM. The animal extracellular matrix includes the interstitial matrix and the basement membrane. Interstitial matrix is present between various animal cells (i.e., in the intercellular spaces). Gels of polysaccharides and fibrous proteins fill the Interstitial fluid, interstitial space and act as a compression buffer against the stress placed on the ECM. Basement membranes are sheet-like depositions of ECM on which various epithelial cells rest ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
CCN Intercellular Signaling Protein
CCN proteins are a family of extracellular matrix (ECM)-associated proteins involved in intercellular signaling. Due to their dynamic role within the ECM they are considered matricellular proteins. Background The acronym CCN is derived from the first three members of the family discovered, namely CYR61 (cysteine-rich angiogenic protein 61 or CCN1), CTGF (connective tissue growth factor or CCN2), and NOV (nephroblastoma overexpressed or CCN3). Together with three Wnt-induced secreted proteins, they comprise the CCN family of matricellular proteins. These proteins have now been renamed CCN1-6 by international consensus. Members of the CCN protein family are characterized by having four conserved cysteine-rich domains, which include the insulin-like growth factor-binding domain (IGFBP), the Von Willebrand factor type C domain (VWC), the thrombospondin type 1 repeat (TSR), and a C-terminal domain (CT) with a cysteine knot motif. CCN proteins have been shown to play important roles in ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Fibulin
Fibulin (FY-beau-lin) (now known as Fibulin-1 FBLN1) is the prototypic member of a multigene family, currently with seven members. Fibulin-1 is a calcium-binding glycoprotein. In vertebrates, fibulin-1 is found in blood and extracellular matrices. In the extracellular matrix, fibulin-1 associates with basement membranes and elastic fibers. The association with these matrix structures is mediated by its ability to interact with numerous extracellular matrix constituents including fibronectin, proteoglycans, laminins and tropoelastin. In blood, fibulin-1 binds to fibrinogen and incorporates into clots. Fibulins are secreted glycoproteins that become incorporated into a fibrillar extracellular matrix when expressed by cultured cells or added exogenously to cell monolayers. The five known members of the family share an elongated structure and many calcium-binding sites, owing to the presence of tandem arrays of epidermal growth factor-like domains. They have overlapping binding sites ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Osteopontin
Osteopontin (OPN), also known as bone /sialoprotein I (BSP-1 or BNSP), early T-lymphocyte activation (ETA-1), secreted phosphoprotein 1 (SPP1), 2ar and Rickettsia resistance (Ric), is a protein that in humans is encoded by the ''SPP1'' gene (secreted phosphoprotein 1). The murine ortholog is ''Spp1''. Osteopontin is a SIBLING (glycoprotein) that was first identified in 1986 in osteoblasts. The prefix '' osteo-'' indicates that the protein is expressed in bone, although it is also expressed in other tissues. The suffix ''-pontin'' is derived from "pons," the Latin word for bridge, and signifies osteopontin's role as a linking protein. Osteopontin is an extracellular structural protein and therefore an organic component of bone. The gene has 7 exons, spans 5 kilobases in length and in humans it is located on the long arm of chromosome 4 region 22 (4q1322.1). The protein is composed of ~300 amino acids residues and has ~30 carbohydrate residues attached, including 10 sialic aci ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Periostin
Periostin (POSTN, PN, or osteoblast-specific factor OSF-2) is a protein that in humans is encoded by the ''POSTN'' gene. Periostin functions as a ligand for alpha-V/beta-3 and alpha-V/beta-5 integrins to support adhesion and migration of epithelial cells. Periostin is a gla domain vitamin K dependent factor. Function Periostin is a secreted extracellular matrix protein that was originally identified in cells from the mesenchymal lineage (osteoblasts, osteoblast-derived cells, the periodontal ligament, and periosteum). It has been associated with the epithelial-mesenchymal transition in cancer and with the differentiation of mesenchyme in the developing heart. This protein shares a homology with fasciclin I, a secreted cell adhesion molecule found in insects. In many cancers, periostin binds to integrins on cancer cells, activating the Akt/PKB- and FAK-mediated signaling pathways. This leads to increased cell survival, invasion, angiogenesis, metastasis, and the epithelia ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Tenascin
Tenascins are extracellular matrix glycoproteins. They are abundant in the extracellular matrix of developing vertebrate embryos and they reappear around healing wounds and in the stroma of some tumors. Types There are four members of the tenascin gene family: tenascin-C, tenascin-R, tenascin-X and tenascin-W. * Tenascin-C is the founding member of the gene family. In the embryo it is made by migrating cells like the neural crest; it is also abundant in developing tendons, bone and cartilage. * Tenascin-R is found in the developing and adult nervous system. * Tenascin-X is found primarily in loose connective tissue; mutations in the human tenascin-X gene can lead to a form of Ehlers-Danlos syndrome. * Tenascin-W is found in the kidney and in developing bone. The basic structure is 14 EGF-like repeats towards the N-terminal end, and 8 or more fibronectin-III domains which vary upon species and variant. Tenascin-C is the most intensely studied member of the family. It has an ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Thrombospondins
Thrombospondins (TSPs) are a family of secreted glycoproteins with antiangiogenic functions. Due to their dynamic role within the extracellular matrix they are considered matricellular proteins. The first member of the family, thrombospondin 1 (THBS1), was discovered in 1971 by Nancy L. Baenziger. Types The thrombospondins are a family of multifunctional proteins. The family consists of thrombospondins 1-5 and can be divided into 2 subgroups: A, which contains TSP-1 and TSP-2, and B, which contains TSP-3, TSP-4 and TSP-5 (also designated cartilage oligomeric protein or COMP). TSP-1 and TSP-2 are homotrimers, consisting of three identical subunits, whereas TSP-3, TSP-4 and TSP-5 are homopentamers. TSP-1 and TSP-2 are produced by immature astrocytes during brain development, which promotes the development of new synapses. Thrombospondin 1 Thrombospondin 1 (TSP-1) is encoded by THBS1. It was first isolated from platelets that had been stimulated with thrombin, and so was design ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
CCN Protein
CCN proteins are a family of extracellular matrix (ECM)-associated proteins involved in intercellular signaling. Due to their dynamic role within the ECM they are considered matricellular proteins. Background The acronym CCN is derived from the first three members of the family discovered, namely CYR61 (cysteine-rich angiogenic protein 61 or CCN1), CTGF (connective tissue growth factor or CCN2), and NOV (nephroblastoma overexpressed or CCN3). Together with three Wnt-induced secreted proteins, they comprise the CCN family of matricellular proteins. These proteins have now been renamed CCN1-6 by international consensus. Members of the CCN protein family are characterized by having four conserved cysteine-rich domains, which include the insulin-like growth factor-binding domain (IGFBP), the Von Willebrand factor type C domain (VWC), the thrombospondin type 1 repeat (TSR), and a C-terminal domain (CT) with a cysteine knot motif. CCN proteins have been shown to play important roles in ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Matricellular Proteins
A matricellular protein is a dynamically expressed non-structural protein that is present in the extracellular matrix (ECM). Rather than serving as stable structural elements in the ECM, these proteins are rapidly turned over and have regulatory roles. They characteristically contain binding sites for ECM structural proteins and cell surface receptors, and may sequester and modulate activities of specific growth factors. Examples of matricellular proteins include the CCN family of proteins (also known as CCN intercellular signaling protein), fibulins, osteopontin, periostin, SPARC family members, tenascin(s), and thrombospondins. Many of these proteins have important functions in wound healing and tissue repair. See also * CCN protein CCN proteins are a family of extracellular matrix (ECM)-associated proteins involved in intercellular signaling. Due to their dynamic role within the ECM they are considered matricellular proteins. Background The acronym CCN is derived from the fi ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
