Type V collagen

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Type V collagen is a form of fibrillar [1] collagen associated with classical Ehlers-Danlos syndrome. It is found within the dermal/epidermal junction, placental tissues, as well as in association with tissues containing type I collagen. [2]

Contents

Type V collagen is a part of the family of collagen proteins consisting of Collagen I- Collagen XXVIII. Collagen proteins are often associated with the strengthening and support of many tissues including skin, bones, muscles, and ligaments. There are some studies that suggest that Type V collagen is responsible for the formation of other collagen fibrils in different tissues within the body. [3] According to studies, Collagen V regulates the heterotypic fiber diameter. [4] Type V Collagen is considered a regulatory fibril forming collagen. [5] Collagen V is associated with the COL5A1 gene which is the gene which provides instructions to produce Collagen V. Type V Collagen, like other collagens, is made up of procollagen molecules.

Collagen V molecular isoforms are α1(V)α2(V)α3(V), α1(V)3, and α1(V)2 α2(V). These procollagen molecules are made up of three different α -polypeptide chains. [5] These α -polypeptide chains are α1(V), α2(V), and α3(V). Different combinations of these chains form the Type V collagen Isoforms. Procollagen molecules then form mature collagen with the help of enzymes. After the chains are formed, they arrange into thin fibrils. These collagen fibrils then assort with type I collagen fibrils. [3]

Type V collagen is a part of the Extracellular Matrix (ECM). [5] Collagen V is gene expression modulated by TGF-β. Type V collagen has shown that it is resistant to digestion by interstitial collagenases. Denatured collagen V on the other hand, can be degraded by gelatinases as well as metalloproteinases. [5]

Alternative names

Type V collagen has a few alternative names alpha 1 These include: type V collagen preproprotein, CO5A1_HUMAN, and collagen type V alpha. [3] Type V collagen can also be abbreviated to COLV or collagen V.

Diseases associated with type V collagen

Some studies show that a mutation in the gene that codes for Type V collagen is linked as the cause of a form of Ehlers Danlos Syndrome.  Ehlers Danlos Syndrome Classical Type is the result of mutations of the COL5A1 gene which codes Type V Collagen. This form of the Ehlers Danlos- Syndrome (classical type) is associated with hypermobility, scarring and elasticity of the skin and other tissues. Researchers discovered the cause of this form of Ehlers Danlos is due to the mutation that produces less chains from the three chains that make up Type V Collagen. Over 100 mutations to the gene COL5A1 have been identified. These mutations result in the underproduction of pro-α1(V) chains. With these mutations, Type V Collagen fibrils are not fully developed and disorganized. This results in the different symptoms of Ehlers Danlos Syndrome. [3]

Health

Type V Collagen studies show that Collagen V plays some other roles in different parts of the body. These roles can be both beneficial and harmful.

Beneficial roles that Type V collagen plays in the body are:

Harmful roles that Type V collagen can play in the body.

Autoimmunity against type V collagen is associated with lung transplant failure. [6] [7] [8]

Genes

Related Research Articles

Collagen is the main structural protein in the extracellular matrix found in the body's various connective tissues. As the main component of connective tissue, it is the most abundant protein in mammals, making up from 25% to 35% of the whole-body protein content. Collagen consists of amino acids bound together to form a triple helix of elongated fibril known as a collagen helix. It is mostly found in connective tissue such as cartilage, bones, tendons, ligaments, and skin.

<span class="mw-page-title-main">Ehlers–Danlos syndromes</span> Group of genetic connective tissues disorders

Ehlers–Danlos syndromes (EDS) are a group of 13 genetic connective-tissue disorders in the current classification, with the latest type discovered in 2018. Symptoms often include loose joints, joint pain, stretchy velvety skin, and abnormal scar formation. These may be noticed at birth or in early childhood. Complications may include aortic dissection, joint dislocations, scoliosis, chronic pain, or early osteoarthritis.

<span class="mw-page-title-main">Collagen, type II, alpha 1</span>

Collagen, type II, alpha 1 , also known as COL2A1, is a human gene that provides instructions for the production of the pro-alpha1(II) chain of type II collagen.

<span class="mw-page-title-main">ADAMTS2</span> Protein-coding gene in the species Homo sapiens

A disintegrin and metalloproteinase with thrombospondin motifs 2 (ADAM-TS2) also known as procollagen I N-proteinase is an enzyme that in humans is encoded by the ADAMTS2 gene.

<span class="mw-page-title-main">Collagen, type I, alpha 1</span> Mammalian protein found in Homo sapiens

Collagen, type I, alpha 1, also known as alpha-1 type I collagen, is a protein that in humans is encoded by the COL1A1 gene. COL1A1 encodes the major component of type I collagen, the fibrillar collagen found in most connective tissues, including cartilage.

<span class="mw-page-title-main">Collagen, type XI, alpha 2</span>

Collagen alpha-2(XI) chain is a protein that in humans is encoded by the COL11A2 gene.

Fibrillogenesis is the development of fine fibrils normally present in collagen fibers of connective tissue. It is derived from the Greek fibrillo and genesis.

<span class="mw-page-title-main">Sack–Barabas syndrome</span> Medical condition

Sack–Barabas syndrome is an older name for the medical condition vascular Ehlers–Danlos syndrome (vEDS). It affects the body's blood vessels and organs, making them prone to rupture.

<span class="mw-page-title-main">Collagen, type III, alpha 1</span>

Type III Collagen is a homotrimer, or a protein composed of three identical peptide chains (monomers), each called an alpha 1 chain of type III collagen. Formally, the monomers are called collagen type III, alpha-1 chain and in humans are encoded by the COL3A1 gene. Type III collagen is one of the fibrillar collagens whose proteins have a long, inflexible, triple-helical domain.

Collagen IV is a type of collagen found primarily in the basal lamina. The collagen IV C4 domain at the C-terminus is not removed in post-translational processing, and the fibers link head-to-head, rather than in parallel. Also, collagen IV lacks the regular glycine in every third residue necessary for the tight, collagen helix. This makes the overall arrangement more sloppy with kinks. These two features cause the collagen to form in a sheet, the form of the basal lamina. Collagen IV is the more common usage, as opposed to the older terminology of "type-IV collagen". Collagen IV exists in all metazoan phyla, to whom they served as an evolutionary stepping stone to multicellularity.

<span class="mw-page-title-main">Tenascin X</span> Protein-coding gene in the species Homo sapiens

A member of the tenascin family, tenascin X (TN-X) also known as flexillin or hexabrachion-like protein is a 450kDa glycoprotein that is expressed in connective tissues. TN-X possesses a modular structure composed, from the N- to the C-terminal part by a Tenascin assembly domain (TAD), a series of 18.5 repeats of epidermal growth factor (EGF)-like motif, a high number of Fibronectin type III (FNIII) module, and a fibrinogen (FBG)-like globular domain. In humans, tenascin X is encoded by the TNXB gene.

<span class="mw-page-title-main">Collagen, type V, alpha 1</span> Mammalian protein found in Homo sapiens

Collagen alpha-1(V) chain is a protein that in humans is encoded by the COL5A1 gene.

<span class="mw-page-title-main">Collagen, type V, alpha 2</span>

Collagen alpha-2(V) chain is a protein that in humans is encoded by the COL5A2 gene.

<span class="mw-page-title-main">Collagen, type I, alpha 2</span> Mammalian protein found in Homo sapiens

Collagen alpha-2(I) chain is a protein that in humans is encoded by the COL1A2 gene.

<span class="mw-page-title-main">Collagen, type XII, alpha 1</span>

Collagen alpha-1(XII) chain is a protein that in humans is encoded by the COL12A1 gene.

<span class="mw-page-title-main">Collagen, type V, alpha 3</span> Mammalian protein found in Homo sapiens

Collagen alpha-3(V) chain is a protein that in humans is encoded by the COL5A3 gene.

Collagen VI (ColVI) is a type of collagen primarily associated with the extracellular matrix of skeletal muscle. ColVI maintains regularity in muscle function and stabilizes the cell membrane. It is synthesized by a complex, multistep pathway that leads to the formation of a unique network of linked microfilaments located in the extracellular matrix (ECM). ColVI plays a vital role in numerous cell types, including chondrocytes, neurons, myocytes, fibroblasts, and cardiomyocytes. ColVI molecules are made up of three alpha chains: α1(VI), α2(VI), and α3(VI). It is encoded by 6 genes: COL6A1, COL6A2, COL6A3, COL6A4, COL6A5, and COL6A6. The chain lengths of α1(VI) and α2(VI) are about 1,000 amino acids. The chain length of α3(VI) is roughly a third larger than those of α1(VI) and α2(VI), and it consists of several spliced variants within the range of 2,500 to 3,100 amino acids.

Feline cutaneous asthenia is a rare inheritable skin disease of cats characterised by abnormal elasticity, stretching, and improper healing of the skin. Pendulous wing-like folds of skin form on the cat's back, shoulders and haunches. Even stroking the cat can cause the skin to stretch and tear. A recessive autosomal form of feline cutaneous asthenia has been identified in Siamese cats and related breeds. In the homozygous state, it is apparently lethal. Feline cutaneous asthenia is similar to the Ehlers–Danlos syndrome of humans.

FKBP14 is a gene which codes for a structural protein named FKBP prolyl isomerase 14. This protein is believed to aid in the process of procollagen folding and is located in the endoplasmic reticulum that functions to process and transport proteins. Procollagens are collagen precursors located in the extracellular matrix that give tissues elasticity, strength, and support. This gene is involved in patterning the collagen structure. FKBP prolyl isomerase 14 may also be involved in altering other factors in the extracellular matrix. Mutations of this gene are associated with the kyphoscoliotic type of Ehlers-Danlos syndrome. This condition is characterized by a high range of joint movement, muscle atrophy, curved spine, and delicate cardiovascular vessels. These symptoms are brought about by a loss of the protein which results in a disruption of endoplasmic reticulum activities and extracellular matrix organization. FKBP14 mRNA levels are found higher in ovarian cancer tissues than healthy ovarian tissue and knocked down expression of FKBP14 by lentiviral shRNA leads to an impaired proliferative ability of ovarian cancer cells.

<span class="mw-page-title-main">Daniel S. Greenspan</span> American biomedical scientist

Daniel S. Greenspan is an American biomedical scientist, academic and researcher. He is Kellett professor of Cell and Regenerative Biology at the University of Wisconsin-Madison School of Medicine and Public Health. He has authored over 120 publications. His research has mainly focused on genes encoding proteins of the extracellular space and possible links between defects in such genes and human development and disease.

References

  1. ↑ Wenstrup RJ, Florer JB, Brunskill EW, Bell SM, Chervoneva I, Birk DE (December 2004). "Type V collagen controls the initiation of collagen fibril assembly". The Journal of Biological Chemistry. 279 (51): 53331–53337. doi: 10.1074/jbc.M409622200 . PMID   15383546.
  2. ↑ Malfait F, Wenstrup R, De Paepe A (1993). Adam MP, Mirzaa GM, Pagon RA, Wallace SE, Bean LJ, Gripp KW, Amemiya A (eds.). "Ehlers-Danlos Syndrome, Classic Type". GeneReviews. Seattle (WA): University of Washington, Seattle. PMID   20301422.
  3. 1 2 3 4 "COL5A1 gene: MedlinePlus Genetics". medlineplus.gov. Retrieved 2023-04-26.
  4. 1 2 Martin, Patricia; Teodoro, Walcy R.; Velosa, Ana Paula P.; de Morais, Jymenez; Carrasco, Solange; Christmann, Romy B.; Goldenstein-Schainberg, Cláudia; Parra, Edwin R.; Katayama, Maria Lúcia; Sotto, Mirian N.; Capelozzi, Vera L.; Yoshinari, Natalino H. (September 2012). "Abnormal collagen V deposition in dermis correlates with skin thickening and disease activity in systemic sclerosis". Autoimmunity Reviews. 11 (11): 827–835. doi:10.1016/j.autrev.2012.02.017. ISSN   1873-0183. PMID   22406224.
  5. 1 2 3 4 5 6 7 8 9 10 11 Mak, Ki M.; Png, Chien Yi M.; Lee, Danielle J. (May 2016). "Type V Collagen in Health, Disease, and Fibrosis". Anatomical Record (Hoboken, N.J.: 2007). 299 (5): 613–629. doi: 10.1002/ar.23330 . ISSN   1932-8494. PMID   26910848.
  6. ↑ "Studies on Collagen". www.collagencomplete.com. Retrieved 2016-07-13.
  7. ↑ Haque MA, Mizobuchi T, Yasufuku K, Fujisawa T, Brutkiewicz RR, Zheng Y, et al. (August 2002). "Evidence for immune responses to a self-antigen in lung transplantation: role of type V collagen-specific T cells in the pathogenesis of lung allograft rejection". Journal of Immunology. 169 (3): 1542–1549. doi: 10.4049/jimmunol.169.3.1542 . PMID   12133982.
  8. ↑ Iwata T, Philipovskiy A, Fisher AJ, Presson RG, Chiyo M, Lee J, et al. (October 2008). "Anti-type V collagen humoral immunity in lung transplant primary graft dysfunction". Journal of Immunology. 181 (8): 5738–5747. doi:10.4049/jimmunol.181.8.5738. PMC   2997998 . PMID   18832733.
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