Misplaced Pages

COL3A1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2V53, 3DMW, 4AE2, 4AEJ, 4AK3, 4GYX
Identifiers
Aliases	COL3A1, EDS4A, collagen type III alpha 1, collagen type III alpha 1 chain, EDSVASC, PMGEDSV
External IDs	OMIM: 120180; MGI: 88453; HomoloGene: 55433; GeneCards: COL3A1; OMA:COL3A1 - orthologs
Gene location (Human) Chr. Chromosome 2 (human) Band 2q32.2 Start 188,974,373 bp End 189,012,746 bp
Gene location (Mouse) Chr. Chromosome 1 (mouse) Band 1 C1.1|1 23.67 cM Start 45,350,698 bp End 45,388,866 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in skin of hip parietal pleura visceral pleura tendon of biceps brachii periodontal fiber cartilage tissue stromal cell of endometrium skin of thigh skin of arm saphenous vein Top expressed in efferent ductule conjunctival fornix vas deferens cervix umbilical cord human fetus calvaria Gonadal ridge ascending aorta semi-lunar valve More reference expression data BioGPS More reference expression data
Gene ontology Molecular function metal ion binding integrin binding protein binding platelet-derived growth factor binding SMAD binding extracellular matrix structural constituent protease binding extracellular matrix structural constituent conferring tensile strength Cellular component collagen endoplasmic reticulum lumen extracellular space collagen type III trimer extracellular matrix extracellular region collagen-containing extracellular matrix Biological process positive regulation of Rho protein signal transduction skeletal system development negative regulation of neuron migration response to cytokine response to mechanical stimulus ageing extracellular matrix organization platelet activation heart development peptide cross-linking negative regulation of immune response blood vessel development regulation of immune response cerebral cortex development collagen catabolic process cellular response to amino acid stimulus integrin-mediated signaling pathway response to radiation cell-matrix adhesion digestive tract development transforming growth factor beta receptor signaling pathway aorta smooth muscle tissue morphogenesis skin development collagen fibril organization wound healing supramolecular fiber organization Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 1281 12825 Ensembl ENSG00000168542 ENSMUSG00000026043 UniProt P02461 P08121 RefSeq (mRNA) NM_000090 NM_001376916 NM_009930 RefSeq (protein) NP_000081 NP_034060 Location (UCSC) Chr 2: 188.97 – 189.01 Mb Chr 1: 45.35 – 45.39 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

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.

Protein structure and function

Type III collagen is synthesized by cells as a pre-procollagen.

The signal peptide is cleaved off producing a procollagen molecule. Three identical type III procollagen chains come together at the carboxy-terminal ends, and the structure is stabilized by the formation of disulphide bonds. Each individual chain folds into a left-handed helix and the three chains are then wrapped together into a right-handed superhelix, the triple helix. Prior to assembling the super-helix, each monomer is subjected to a number of post-translational modifications that occur while the monomer is being translated. First, on the order of 145 prolyl residues of the 239 in the triple-helical domain are hydroxylated to 4-hydroxyproline by prolyl-4-hydroxylase. Second, some of the lysine residues are hydroxylated or glycosylated, and some lysine as well as hydroxylysine residues undergo oxidative deamination catalysed by lysyl oxidase. Other post-translational modifications occur after the triple helix is formed. The large globular domains from both ends of the molecule are removed by C- and amino(N)-terminal-proteinases to generate triple-helical type III collagen monomers called tropocollagen. In addition, crosslinks form between certain lysine and hydroxylysine residues. In the extracellular space in tissues, type III collagen monomers assemble into macromolecular fibrils, which aggregate into fibers, providing a strong support structure for tissues requiring tensile strength.

The triple-helical conformation, which is a characteristic feature of all fibrillar collagens, is possible because of the presence of glycine as every third amino acid in the sequence of about 1000 amino acids. When the right-handed super-helix is formed, the glycine residues of each of the monomers are positioned at the center of the super-helix (where the three monomers "touch"). Each left-handed helix is characterized by a complete turn in about 3.3 amino acids. The periodicity induced by the glycines at non-integer spacing results in a super-helix that completes one turn in about 20 amino acids. This (Gly-X-Y)n sequence is repeated 343 times in the type III collagen molecule. Proline or hydroxyproline is often found in the X- and Y-position giving the triple helix stability.

In addition to being an integral structural component of many organs, type III collagen is also an important regulator of the diameter of type I and II collagen fibrils. Type III collagen is also known to facilitate platelet aggregation through its binding to platelets and therefore, play an important role in blood clotting.

Tissue distribution

Type III collagen is found as a major structural component in hollow organs such as large blood vessels, uterus and bowel. It is also found in many other tissues together with type I collagen.

Gene

The COL3A1 gene is located on the long (q) arm of chromosome 2 at 2q32.2, between positions 188974372 and 189012745. The gene has 51 exons and is approximately 40 kbp long. The COL3A1 gene is in tail-to-tail orientation with a gene for another fibrillar collagen, namely COL5A2.

Two transcripts are generated from the gene using different polyadenylation sites. Although alternatively spliced transcripts have been detected for this gene, they are the result of mutations; these mutations alter RNA splicing, often leading to the exclusion of an exon or use of cryptic splice sites. The resulting defective protein is the cause of a severe, rare disease, the vascular type of Ehlers-Danlos syndrome (vEDS). These studies have also provided important information about RNA splicing mechanisms in multi-exon genes.

Clinical significance

Mutations in the COL3A1 gene cause Ehlers-Danlos syndrome, vascular type (vEDS; also known as the EDS type IV; OMIM 130050). It is the most severe form of EDS, since patients often die suddenly due to rupture of large arteries or other hollow organs.

A few patients with arterial aneurysms without clear signs of EDS have also been found to have COL3A1 mutations.

More recently, mutations in COL3A1 have also been identified in patients with severe brain anomalies suggesting that type III collagen is important for the normal development of the brain during embryogenesis. This disease is similar to that caused by mutations in GRP56 (OMIM 606854). Type III collagen is a known ligand for the receptor GRP56.

The first single base mutation in the COL3A1 gene was reported in 1989 in a patient with vEDS and changed a glycine amino acid to a serine Since then, over 600 different mutations have been characterized in the COL3A1 gene. About 2/3 of these mutations change a glycine amino acid to another amino acid in the triple-helical region of the protein chain. A large number of RNA splicing mutations have also been identified. Interestingly, most of these mutations lead to exon skipping, and produce a shorter polypeptide, in which the Gly-Xaa-Yaa triplets stay in frame and there are no premature termination codons.

The functional consequences of COL3A1 mutations can be studied in a cell culture system. A small bunch biopsy of skin is obtained from the patient and used to start the culture of skin fibroblasts which express type III collagen. The type III collagen protein synthesized by these cells can be studied for its thermal stability. In other words, the collagens can be subjected to a short digestion by proteinases called trypsin and chymotrypsin at increasing temperatures. Intact type III collagen molecules, which have formed a stable triple helix, can withstand such treatment till about 41oC, whereas molecules with mutations that lead to glycine substitutions fall apart at a much lower temperature.

It is difficult to predict the clinical severity based on the type and location of COL3A1 mutations. Another important clinical implication is that several studies have reported on mosaicism. This refers to a situation where one of the parents carries the mutation in some, but not all of her or his cells, and appears phenotypically healthy, but has more than one affected offspring. In such a situation the risk for another affected child is higher than in a genotypically normal parent.

Type III collagen could also be important in several other human diseases. Increased amounts of type III collagen are found in many fibrotic conditions such as liver and kidney fibrosis, and systemic sclerosis. This has led to a search for serum biomarkers that could be used for diagnosing these conditions without having to obtain a tissue biopsy. The most widely used biomarker is the N-terminal propeptide of type III procollagen, which is cleaved off during the biosynthesis of type III collagen.

Animal models

Four different mouse models with COL3A1 defects have been reported. Inactivation of the murine COL3A1 gene using homologous recombination technique led to a shorter life span in homozygous mutant mice. The mice died prematurely from a rupture of major arteries mimicking the human vEDS phenotype. These mice also had a severe malformation of the brain. Another study discovered mice with a naturally occurring large deletion of the COL3A1 gene. These mice died suddenly due to thoracic aortic dissections. The third type of mutant mice were transgenic mice with a Gly182Ser mutation. These mice developed severe skin wounds, demonstrated vascular fragility in the form of reduced tensile strength and died prematurely at the age of 13–14 weeks. The fourth mouse model with defective COL3A1 gene is the tight skin mouse (Tsk2/+), which resembles the human systemic sclerosis.

See also

• Collagen
• Ehlers-Danlos syndrome

Notes

The 2019 version of this article was updated by an external expert under a dual publication model. The corresponding academic peer reviewed article was published in Gene and can be cited as: Helena Kuivaniemi, Gerard Tromp (7 May 2019). "Type III collagen (COL3A1): Gene and protein structure, tissue distribution, and associated diseases". Gene. Gene Wiki Review Series. 707: 151–171. doi:10.1016/J.GENE.2019.05.003. ISSN 0378-1119. PMC 6579750. PMID 31075413. Wikidata Q65950306.

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Further reading

• Malfait F, Francomano C, Byers P, Belmont J, Berglund B, Black J, et al. (March 2017). "The 2017 international classification of the Ehlers-Danlos syndromes". American Journal of Medical Genetics. Part C, Seminars in Medical Genetics. 175 (1): 8–26. doi:10.1002/ajmg.c.31552. PMID 28306229.
• Malfait F (October 2018). "Vascular aspects of the Ehlers-Danlos Syndromes". Matrix Biology. 71–72: 380–395. doi:10.1016/j.matbio.2018.04.013. PMID 29709596. S2CID 13705584.
• Kuivaniemi H, Tromp G, Prockop DJ (November 1991). "Genetic causes of aortic aneurysms. Unlearning at least part of what the textbooks say". The Journal of Clinical Investigation. 88 (5): 1441–4. doi:10.1172/JCI115452. PMC 295644. PMID 1939638.
• Kuivaniemi H, Tromp G, Prockop DJ (1997). "Mutations in fibrillar collagens (types I, II, III, and XI), fibril-associated collagen (type IX), and network-forming collagen (type X) cause a spectrum of diseases of bone, cartilage, and blood vessels". Human Mutation. 9 (4): 300–15. doi:10.1002/(SICI)1098-1004(1997)9:4<300::AID-HUMU2>3.0.CO;2-9. PMID 9101290. S2CID 6890740.
• Kuivaniemi H, Tromp G, Prockop DJ (April 1991). "Mutations in collagen genes: causes of rare and some common diseases in humans". FASEB Journal. 5 (7): 2052–60. doi:10.1096/fasebj.5.7.2010058. PMID 2010058. S2CID 24461341.
• Byers PH, Belmont J, Black J, De Backer J, Frank M, Jeunemaitre X, Johnson D, Pepin M, Robert L, Sanders L, Wheeldon N (March 2017). "Diagnosis, natural history, and management in vascular Ehlers-Danlos syndrome". American Journal of Medical Genetics. Part C, Seminars in Medical Genetics. 175 (1): 40–47. doi:10.1002/ajmg.c.31553. PMID 28306228.
• Boudko SP, Engel J, Okuyama K, Mizuno K, Bächinger HP, Schumacher MA (November 2008). "Crystal structure of human type III collagen Gly991-Gly1032 cystine knot-containing peptide shows both 7/2 and 10/3 triple helical symmetries". The Journal of Biological Chemistry. 283 (47): 32580–9. doi:10.1074/jbc.M805394200. PMID 18805790.
• Lamberg A, Helaakoski T, Myllyharju J, Peltonen S, Notbohm H, Pihlajaniemi T, Kivirikko KI (May 1996). "Characterization of human type III collagen expressed in a baculovirus system. Production of a protein with a stable triple helix requires coexpression with the two types of recombinant prolyl 4-hydroxylase subunit". The Journal of Biological Chemistry. 271 (20): 11988–95. doi:10.1074/jbc.271.20.11988. PMID 8662631.

External links

• Collagen+type+III at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
• "COL3A1". Ehlers Danlos Syndrome Variant Database. Archived from the original on 2021-01-26. Retrieved 2018-12-05.
• "Report for CCDS2297.1". Consensus Coding Sequence (CDS) Database. National Center for Biotechnology Information (NCBI).
• Byers PH, Adam MP, Everman DB, Mirzaa GM, Pagon RA, Wallace SE, Bean LJH, Gripp KW, Amemiya A (1993). "Vascular Ehlers-Danlos Syndrome". Ehlers-Danlos Syndrome Type IV. NCBI/NIH/UW. PMID 20301667. {{cite book}}: |work= ignored (help)

• Genes on human chromosome 2
• Misplaced Pages articles with corresponding academic peer reviewed articles
• Misplaced Pages articles with corresponding articles published in Gene
• Collagens