COL2A1 is the alpha-1 chain of type II collagen which is a fibrillar collagen found in cartilage and the vitreous humor of the eye. Mutations in this protein are associated with achondrogenesis, chondrodysplasia, early onset familial osteoarthritis, SED congenita, Langer-Saldino achondrogenesis, Kniest dysplasia, Stickler syndrome type I, and spondyloepimetaphyseal dysplasia Strudwick type. In addition, defects in processing chondrocalcin, a calcium binding protein that is the C-propeptide of this collagen molecule, are also associated with chondrodysplasia. There are two transcripts identified for this gene. Type II collagen is specific for cartilaginous tissues. Thus COL2A1 is essential for the normal embryonic development of the skeleton, for linear growth and for the ability of cartilage to resist compressive forces. The regulation of COL2A1, likely results from a balance of both positive and negative proteins. The inhibition of COL2A1 transcription following treatment of chick sternal chondrocytes with growth factors was accompanied by increased EF1 expression. Overexpression of EF1 in differentiated chondrocytes resulted in decreased expression of a reporter construct containing a collagen II promoter/enhancer insert.
This gene encodes the alpha-3 chain, one of the three alpha chains of type VI collagen, a beaded filament collagen found in most connective tissues. The alpha-3 chain of type VI collagen is much larger than the alpha-1 and -2 chains. This difference in size is largely due to an increase in the number of subdomains, similar to von Willebrand Factor type A domains, that are found in the amino terminal globular domain of all the alpha chains. These domains have been shown to bind extracellular matrix proteins, an interaction that explains the importance of this collagen in organizing matrix components. Mutations in the type VI collagen genes are associated with Bethlem myopathy, a rare autosomal dominant proximal myopathy with early childhood onset. Mutations in this gene are also a cause of Ullrich congenital muscular dystrophy, also referred to as Ullrich scleroatonic muscular dystrophy, an autosomal recessive congenital myopathy that is more severe than Bethlem myopathy. Multiple transcript variants have been identified, but the full-length nature of only some of these variants has been described.
Collagen alpha-1(VIII) chain, also known as endothelial collagen, C3orf7 and COL8A1, can be cleaved into vastatin chain. COL8A1 is a short chain collagen and a major component of the basement membrane of the corneal endothelium. COL8A1 forms homotrimers, or heterotrimers in association with alpha 2(VIII) type collagens. Four homotrimers can form a tetrhedron stabilized by central interacting C-terminal NC1 trimers. COL8A1 contains one C1q domain and is primarily expressed in the subendothelium of large blood vessels. The expression level can be up-regulated during vascular injury, in atherosclerosis and in diabetes. COL8A1 may have a role in the maintenance of vessel wall integrity and structure, in particular in atherogenesis.
Ubiquinone biosynthesis protein COQ7 homolog; also known as Coenzyme Q biosynthesis protein 7 homolog; Timing protein clk-1 homolog and COQ7; is a mitochondrion inner membrane and peripheral membrane protein which belongs to theCOQ7 family. It is expressed dominantly in heart and skeletal muscle. COQ7 is synthesized as a preprotein that is imported into the mitochondrial matrix; where the sequence is cleaved off and the mature protein becomes loosely associated with the inner membrane. This enzyme is responsible for the hydroxylation of 5-demethoxyubiquinone to 5-hydroxyubiquinone. Human COQ7 protein is mostly helical; and contains an alpha-helical membrane insertion. It has a potential N-glycosylation site; a phosphorylation site for protein kinase C and another for casein kinase II; and three N-myristoylation sites. COQ7 is involved in lifespan determination in ubiquinone-independent manner. It is also involved in ubiquinone biosynthesis. COQ7 is potential central metabolic regulator.
COL9A1; which is short for Collagen alpha-1(IX) chain; is a 921 aa. protein. It is a secreted protein; and exists in extracellular space and extracellular matrix. This protein is a heterotrimer of an alpha 1(IX); an alpha 2(IX) and an alpha 3(IX) chain.Each subunit is composed of three triple-helical domains interspersed with non-collagenous domains. The globular domain at the N-terminus of type IX collagen molecules represents the NC4 domain which may participate in electrostatic interactions with polyanionic glycosaminoglycans in cartilage. It ia a structural component of hyaline cartilage and vitreous of the eye.
This gene encodes the pro-alpha1 chains of type I collagen whose triple helix comprises two alpha1 chains and one alpha2 chain. Type I is a fibril-forming collagen found in most connective tissues and is abundant in bone, cornea, dermis and tendon. Mutations in this gene are associated with osteogenesis imperfecta types I-IV, Ehlers-Danlos syndrome type VIIA, Ehlers-Danlos syndrome Classical type, Caffey Disease and idiopathic osteoporosis. Reciprocal translocations between chromosomes 17 and 22, where this gene and the gene for platelet-derived growth factor beta are located, are associated with a particular type of skin tumor called dermatofibrosarcoma protuberans, resulting from unregulated expression of the growth factor. Two transcripts, resulting from the use of alternate polyadenylation signals, have been identified for this gene.
Lascia la tua email e seleziona le aree che vuoi seguire per ricevere novita di prodotto, approfondimenti tecnici e promozioni piu pertinenti.
Puoi scegliere le macro-aree Life Science e Diagnostica oppure le singole specializzazioni.
Seleziona uno o piu ambiti di interesse per ricevere comunicazioni piu utili e mirate.
Aggiornamenti su ricerca, strumentazione e applicazioni per il mondo Life Science.
Novita, approfondimenti e promozioni per laboratori diagnostici e flussi operativi.
2025 TEMA Ricerca - All Rights Reserved.
