COL18A1 | |||||||||||||||||||||||||||||||||||||||||||||||||||
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Aliases | COL18A1 , KNO, KNO1, KS, Collagen, type XVIII, alpha 1, collagen type XVIII alpha 1, collagen type XVIII alpha 1 chain, GLCC | ||||||||||||||||||||||||||||||||||||||||||||||||||
External IDs | OMIM: 120328 MGI: 88451 HomoloGene: 7673 GeneCards: COL18A1 | ||||||||||||||||||||||||||||||||||||||||||||||||||
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Wikidata | |||||||||||||||||||||||||||||||||||||||||||||||||||
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Collagen alpha-1(XVIII) chain is a protein that in humans is encoded by the COL18A1 gene. [5]
This gene encodes the alpha chain of type XVIII collagen. This collagen is one of the multiplexins, extracellular matrix proteins that contain multiple triple-helix domains (collagenous domains) interrupted by non-collagenous domains. The proteolytically produced C-terminal fragment of type XVIII collagen is endostatin, a potent antiangiogenic protein. Mutations in this gene are associated with Knobloch syndrome. The main features of this syndrome involve retinal abnormalities so type XVIII collagen may play an important role in retinal structure and in neural tube closure. Two transcript variants encoding different isoforms have been found for this gene. [6]
Endostatin is a naturally occurring, 20-kDa C-terminal fragment derived from type XVIII collagen. It is reported to serve as an anti-angiogenic agent, similar to angiostatin and thrombospondin.
Decorin is a protein that in humans is encoded by the DCN gene.
Type XVIII collagen is a type of collagen which can be cleaved to form endostatin. The endostatin is from the c terminus end of the collagen XVIII, and is known to have an inhibitory effect on the growth of blood vessels. This is seen with tumors, where endostatin inhibits the growth of the blood vessels of the tumor as well as the overall growth of the tumor.
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.
Collagen alpha-1(VII) chain is a protein that in humans is encoded by the COL7A1 gene. It is composed of a triple helical, collagenous domain flanked by two non-collagenous domains, and functions as an anchoring fibril between the dermal-epidermal junction in the basement membrane. Mutations in COL7A1 cause all types of dystrophic epidermolysis bullosa, and the exact mutations vary based on the specific type or subtype. It has been shown that interactions between the NC-1 domain of collagen VII and several other proteins, including laminin-5 and collagen IV, contribute greatly to the overall stability of the basement membrane.
Collagen alpha-5(IV) chain is a protein that in humans is encoded by the COL4A5 gene.
Brain-specific angiogenesis inhibitor 2 is a protein that in humans is encoded by the BAI2 gene. It is a member of the adhesion-GPCR family of receptors.
Collagen alpha-3(IV) chain is a protein that in humans is encoded by the COL4A3 gene.
Collagen alpha-4(IV) chain is a protein that in humans is encoded by the COL4A4 gene.
Collagen alpha-2(IV) chain is a protein that in humans is encoded by the COL4A2 gene.
Collagen alpha-6(IV) chain is a protein that in humans is encoded by the COL4A6 gene.
Collagen alpha-1(XI) chain is a protein that in humans is encoded by the COL11A1 gene.
Collagen alpha-2(VIII) chain is a protein that in humans is encoded by the COL8A2 gene. Mutations of the gene are linked to posterior polymorphous dystrophy type 2.
Collagen alpha-1(VIII) chain is a protein that in humans is encoded by the COL8A1 gene.
Collagen alpha-1(XV) chain is a protein that in humans is encoded by the COL15A1 gene.
Collagen alpha-1(XIII) chain is a protein that in humans is encoded by the COL13A1 gene.
Collagen alpha-1(XIX) chain is a protein that in humans is encoded by the COL19A1 gene.
Collagen alpha-1(XXV) chain is a protein that in humans is encoded by the COL25A1 gene.
Angiogenesis is the process of forming new blood vessels from existing blood vessels, formed in vasculogenesis. It is a highly complex process involving extensive interplay between cells, soluble factors, and the extracellular matrix (ECM). Angiogenesis is critical during normal physiological development, but it also occurs in adults during inflammation, wound healing, ischemia, and in pathological conditions such as rheumatoid arthritis, hemangioma, and tumor growth. Proteolysis has been indicated as one of the first and most sustained activities involved in the formation of new blood vessels. Numerous proteases including matrix metalloproteinases (MMPs), a disintegrin and metalloproteinase domain (ADAM), a disintegrin and metalloproteinase domain with throbospondin motifs (ADAMTS), and cysteine and serine proteases are involved in angiogenesis. This article focuses on the important and diverse roles that these proteases play in the regulation of angiogenesis.
Tumstatin is a protein fragment cleaved from collagen that serves as both an antiangiogenic and proapoptotic agent. It has similar function to canstatin, endostatin, restin, and arresten, which also affect angiogenesis. Angiogenesis is the growth of new blood vessels from pre-existing blood vessels, and is important in tumor growth and metastasis. Angiogenesis is stimulated by many growth factors, the most prevalent of which is vascular endothelial growth factor (VEGF).
This article incorporates text from the United States National Library of Medicine, which is in the public domain.