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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 two subgroups: A, which contains Thrombospondin 1, TSP-1 and Thrombospondin-2, TSP-2, and B, which contains Thrombospondin 3, TSP-3, Thrombospondin 4, TSP-4 and TSP-5 (also designated Cartilage oligomeric matrix protein, 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 ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Cartilage Oligomeric Matrix Protein
Cartilage oligomeric matrix protein (COMP), also known as thrombospondin-5, is an extracellular matrix (ECM) protein primarily present in cartilage. In humans it is encoded by the ''COMP'' gene. Function The protein encoded by this gene is a noncollagenous extracellular matrix (ECM) protein. It consists of five identical glycoprotein subunits, each with EGF-like domain, EGF-like and calcium-binding (thrombospondin-like) domains. Oligomerization results from formation of a five-stranded coiled coil and disulfide bonds. Binding to other ECM proteins such as collagen appears to depend on divalent cations. Mutations can cause the osteochondrodysplasias pseudoachondroplasia (PSACH) and multiple epiphyseal dysplasia (MED). COMP is a marker of cartilage turnover. It is present in high quantities in Fibrosis, fibrotic scars and systemic sclerosis, and it appears to have a role in vascular wall remodeling. References Further reading * * * * * * * * * * * * * * * * ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Thrombospondin-2
Thrombospondin-2 is a protein that in humans is encoded by the ''THBS2'' gene. The protein encoded by this gene belongs to the thrombospondin family. It is a disulfide-linked homotrimeric glycoprotein that mediates cell-to-cell and cell-to-matrix interactions. The role of the protein in cancer is controversial, contrasting studies show positive and negative roles for cancer development. Studies of the mouse counterpart suggest that this protein may modulate the cell surface properties of mesenchymal cells and be involved in cell adhesion and migration. Interactions THBS2 has been shown to interact with MMP2 72 kDa type IV collagenase also known as matrix metalloproteinase-2 (MMP-2) and gelatinase A is an enzyme that in humans is encoded by the ''MMP2'' gene. The ''MMP2'' gene is located on chromosome 16 at position 12.2. Function Proteins of the .... References Further reading * * * * * * * * * * * * * * * * * * Thrombospondins {{g ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
THBS1
Thrombospondin 1, abbreviated as THBS1, is a protein that in humans is encoded by the ''THBS1'' gene. Thrombospondin 1 is a subunit of a disulfide-linked homotrimeric protein. This protein is an adhesive glycoprotein that mediates cell-to-cell and cell-to-matrix interactions. This protein can bind to fibrinogen, fibronectin, laminin, collagens types V and VII and integrins alpha-V/beta-1. This protein has been shown to play roles in platelet aggregation, angiogenesis, and tumorigenesis. Function The thrombospondin-1 protein is a member of the thrombospondin family. It is a multi-domain matrix glycoprotein that has been shown to be a natural inhibitor of neovascularization and tumorigenesis in healthy tissue. Both positive and negative modulation of endothelial cell adhesion, motility, and growth have been attributed to TSP1. This should not be surprising considering that TSP1 interacts with at least 12 cell adhesion receptors, including CD36, αv integrins, β1 integrins ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Thrombospondin 4
Thrombospondin-4 is a protein that in humans is encoded by the ''THBS4'' gene. The protein encoded by this gene belongs to the thrombospondin 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 ... protein family. Thrombospondin family members are adhesive glycoproteins that mediate cell-to-cell and cell-to-matrix interactions. This protein forms a pentamer and can bind to heparin and calcium. This protein may be involved in local signaling in the developing and adult nervous system, in bone formation and fracture healing, and in osteoarthritis. References Further reading * * * * * * * * * * * * * * Thrombospondins {{gene-5-stub ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Thrombospondin 3
Thrombospondin-3 (TSP3) is a protein that in humans is encoded by the ''THBS3'' gene. The protein encoded by this gene belongs to the thrombospondin family. Thrombospondin family members are adhesive glycoproteins that mediate cell-to-cell and cell-to-matrix interactions. TSP3 has been found to be involved in the regulation of skeletal maturation. This protein forms a pentameric molecule linked by a single disulfide bond. This gene shares a common promoter with metaxin 1. Identified as the gene on chromosome 1 responsible for mediating an associated with genetic susceptibility to SARS-CoV-2 Severe acute respiratory syndrome coronavirus 2 (SARS‑CoV‑2) is a strain of coronavirus that causes COVID-19, the respiratory illness responsible for the COVID-19 pandemic. The virus previously had the Novel coronavirus, provisional nam ... infection. References Further reading * * * * * * * * * * * * * Thrombospondins {{gene-1-stub ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
TSP1
Thrombospondin 1, abbreviated as THBS1, is a protein that in humans is encoded by the ''THBS1'' gene. Thrombospondin 1 is a subunit of a disulfide-linked homotrimeric protein. This protein is an adhesive glycoprotein that mediates cell-to-cell and cell-to-matrix interactions. This protein can bind to fibrinogen, fibronectin, laminin, collagens types V and VII and integrins alpha-V/beta-1. This protein has been shown to play roles in platelet aggregation, angiogenesis, and tumorigenesis. Function The thrombospondin-1 protein is a member of the thrombospondin family. It is a multi-domain matrix glycoprotein that has been shown to be a natural inhibitor of neovascularization and tumorigenesis in healthy tissue. Both positive and negative modulation of endothelial cell adhesion, motility, and growth have been attributed to TSP1. This should not be surprising considering that TSP1 interacts with at least 12 cell adhesion receptors, including CD36, αv integrins, β1 integrins ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Caspase
Caspases (cysteine-aspartic proteases, cysteine aspartases or cysteine-dependent aspartate-directed proteases) are a family of protease enzymes playing essential roles in programmed cell death. They are named caspases due to their specific cysteine protease activity – a cysteine in its active site nucleophilically attacks and cleaves a target protein only after an aspartic acid residue. As of 2009, there are 12 confirmed caspases in humans and 10 in mice, carrying out a variety of cellular functions. The role of these enzymes in programmed cell death was first identified in 1993, with their functions in apoptosis well characterised. This is a form of programmed cell death, occurring widely during development, and throughout life to maintain cell homeostasis. Activation of caspases ensures that the cellular components are degraded in a controlled manner, carrying out cell death with minimal effect on surrounding tissues. Caspases have other identified roles in programmed cell ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
ADAMTS14
ADAMTS14 encodes a member of the ADAMTS protein family. Family members share several distinct protein modules, including a propeptide region, a metalloproteinase domain, a disintegrin-like domain, and a thrombospondin type 1 (TS) motif. Individual members of this family differ in the number of C-terminal TS motifs, and some have unique C-terminal domains. The proteolytic process of the encoded preproprotein generates a mature enzyme. The enzyme cleaves the amino-propeptides of fibrillar collagens, enabling collagen fibril formation before the assembly of collagen, a major extracellular matrix (ECM) protein. References ADAMTS {{gene-stub ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
ADAMTS13
ADAMTS13 (''a disintegrin and metalloproteinase with a thrombospondin type 1 motif, member 13'')—also known as ''von Willebrand factor-cleaving protease'' (VWFCP)—is a zinc-containing metalloprotease enzyme that cleaves von Willebrand factor (vWf), a large protein involved in blood clotting. It is secreted into the blood and degrades large vWf multimers, decreasing their activity, hence ''ADAMTS13'' acts to reduce thrombus formation. Genetics The ''ADAMTS13'' gene maps to the ninth chromosome (9q34). Discovery Since 1982 it had been known that thrombotic thrombocytopenic purpura (TTP), one of the microangiopathic hemolytic anemias (see below), was characterized in its familial form by the presence in plasma of unusually large von Willebrand factor multimers (ULVWF). In 1994, vWF was shown to be cleaved between a tyrosine at position 1605 and a methionine at 1606 by a plasma metalloprotease enzyme when it was exposed to high levels of shear stress. In 1996, two research grou ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
