collagen type IX alpha 2 chain
עודכן לאחרונה 18 Aug 2020
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ה COL9A2 gene provides instructions for making part of a large molecule called type IX collagen. Collagens are a family of proteins that strengthen and support connective tissues, such as skin, bone, cartilage, tendons, and ligaments. In particular, type IX collagen is an important component of cartilage, which is a tough, flexible tissue that makes up much of the skeleton during early development. Most cartilage is later converted to bone, except for the cartilage that continues to cover and protect the ends of bones and is present in the nose and external ears.
Normal function
ה COL9A2 gene provides instructions for making part of a large molecule called type IX collagen. Collagens are a family of proteins that strengthen and support connective tissues, such as skin, bone, cartilage, tendons, and ligaments. In particular, type IX collagen is an important component of cartilage, which is a tough, flexible tissue that makes up much of the skeleton during early development. Most cartilage is later converted to bone, except for the cartilage that continues to cover and protect the ends of bones and is present in the nose and external ears.
Type IX collagen is made up of three proteins that are produced from three distinct genes: one α1(IX) chain, which is produced from the COL9A1 gene, one α2(IX) chain, which is produced from the COL9A2 gene, and one α3(IX) chain, which is produced from the COL9A3 gene. Type IX collagen is more flexible than other types of collagen molecules and is closely associated with type II collagen. Researchers believe that the flexible nature of type IX collagen allows it to act as a bridge that connects type II collagen with other cartilage components. Studies have shown that type IX collagen also interacts with the proteins produced from the MATN3 ו COMP genes.
Conditions referring to this gene or chromosome
Other names
alpha 2 type IX collagen
CO9A2_HUMAN
collagen IX, alpha-2 polypeptide
collagen type IX alpha 2
collagen, type IX, alpha 2
EDM2
epiphyseal dysplasia, multiple 2
Related patient information and medicines
Patient information leaflet
סקלרודרמה מקומית
Localised scleroderma causes one or more patches of hard skin. There are different types. Generalised morphoea symptoms This is a ... Causes of localised scleroderma The cause is not clear. What is known is that cells called fibroblasts make too much of a protein called collagen. The collagen gets deposited in the skin, causing scarring and.
Patient information leaflet
האם אני יכול לקחת קנדסארטן וקולגן יחד?
There are no known sign... It is generally considered safe to take these together. Why this happens Candesartan is a blood pressure medication (an angiotensin II receptor blocker) that works on the hormonal system controlling blood vessels. Collagen is a protein supplement used for skin, joint, and bone health. These two substances are processed.
Patient information leaflet
האם אני יכול לקחת ביוטין וקולגן יחד?
יש no known harmful interactions between biotin and collagen. In fact, they are frequently taken together in 'hair, skin, and nails' supplements because they work in different ways to support the ... Why this happens Biotin is a B-vitamin (B7) that helps the body convert nutrients into energy and supports the production of keratin. Collagen.
Patient information leaflet
האם אני יכול לקחת אדקל-די3 וקולגן יחד?
יש no known harmful interaction between Adcal-D3 and collagen supplements. In fact, they are often used together to support bone and joint health. Why this happens Adcal-D3 provides calcium and vitamin D3, while collagen provides amino acids. These substances are processed by the body through different pathways and do not interfere with each.
Patient information leaflet
האם אני יכול לקחת קולגן ואומגה-3 יחד?
...interactions between collagen and omega-3 supplementsWhy this happens Collagen מטופל? a protein that מטופל? broken down into amino acids in the digestive tract, while omega-3 is a fatty acid. Our בודק אינטראקציות בין תרופות helps you check whether your prescriptions, over-the-counter medicines, and supplements are safe to take together. Disclaimer.
Patient information leaflet
האם אני יכול לקחת קרבוסיסטאין וקולגן יחד?
Why this happens Carbocisteine works by breaking down the chemical bonds in mucus to make it thinner and easier to cough up. Collagen is a protein used by the body for skin, joint, and bone health. These two substances are processed by the body through different pathways and do not interfere with how the other is absorbed, broken down, or used by.
קריאה נוספת והפניות
- collagen type IX alpha 2 chain; MedlinePlus, National Library of Medicine.
- Baker S, Booth C, Fillman C, Shapiro M, Blair MP, Hyland JC, Ala-Kokko L. A loss of function mutation in the COL9A2 gene causes autosomal recessive Stickler syndrome. Am J Med Genet A. 2011 Jul;155A(7):1668-72. doi: 10.1002/ajmg.a.34071. Epub 2011 Jun 10.
- Briggs MD, Chapman KL. Pseudoachondroplasia and multiple epiphyseal dysplasia: mutation review, molecular interactions, and genotype to phenotype correlations. Hum Mutat. 2002 May;19(5):465-78. doi: 10.1002/humu.10066.
- Briggs MD, Wright MJ, Mortier GR. Multiple Epiphyseal Dysplasia, Autosomal Dominant. 2003 Jan 8 [updated 2024 Jul 4]. In: Adam MP, Bick S, Mirzaa GM, Wallace SE, Amemiya A, editors. GeneReviews(R) [Internet]. Seattle (WA): University of Washington, Seattle; 1993-2026. Available from http://www.ncbi.nlm.nih.gov/books/NBK1123/
- Higashino K, Matsui Y, Yagi S, Takata Y, Goto T, Sakai T, Katoh S, Yasui N. The alpha2 type IX collagen tryptophan polymorphism is associated with the severity of disc degeneration in younger patients with herniated nucleus pulposus of the lumbar spine. Int Orthop. 2007 Feb;31(1):107-11. doi: 10.1007/s00264-006-0117-8. Epub 2006 Apr 4.
- Jim JJ, Noponen-Hietala N, Cheung KM, Ott J, Karppinen J, Sahraravand A, Luk KD, Yip SP, Sham PC, Song YQ, Leong JC, Cheah KS, Ala-Kokko L, Chan D. The TRP2 allele of COL9A2 is an age-dependent risk factor for the development and severity of intervertebral disc degeneration. Spine (Phila Pa 1976). 2005 Dec 15;30(24):2735-42. doi: 10.1097/01.brs.0000190828.85331.ef.
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