User:Hcs22e/Type I collagen

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Type I Collagen is the most abundant collagen of the human body, consisting of around 90% of the body's total collagen in vertebrates. Due to this, it is also the most abundant protein type found in all vertebrates. Type I forms large, eosinophilic fibers known as collagen fibers, which make up most of the rope-like dense connective tissue in the body[1]. Collagen I itself is created by the combination of both a proalpha1 and a proalpha2 chain created by the COL1alpha1 and COL1alpha2 genes respectively. The Col I gene itself takes up a triple-helical conformation due to its Glycine-X-Y structure, x and y being any type of amino acid. Collagen can also be found in two different isoforms, either as a homotrimer or a heterotrimer, which both can be found during different periods of development. Homotrimers in particular playing an important role in wound healing[2], however heterotrimers are the dominant isoform found in the body[3].

As mentioned Type 1 collagen can be found in a myriad of different places in the body, mainly forming the matrix of connective tissues. It is present in scar tissue, the end product when tissue heals by repair, as well as tendons, ligaments, the endomysium of myofibrils, the organic part of bone, the dermis, the dentin, and organ capsules.

Formation:[edit]

The type 1 Collagen creation process begins with the production and the combination of two separate subunits called the pro-alpha1(I) and pro-alpha2(I) chains. These pro-alpha chains are encoded by the COL1A1 and COL1A2 genes respectively and when combined together produce type I pro-collagen[4]. This transcriptional process takes place within the cell inside of the endoplasmic reticulum and must undergo post-translational modifications in order to make the final type 1 collagen product[5]. The procollagen complex is then modified by different enzyme proteinases which cleave N and C terminal propeptides that are present on either side of the molecule. This process occurs outside of the cellular membrane at which post processing, the molecules cross link and form a final type 1 collagen product.

The chemical structure of collagen type 1

Structure:[edit]

Type 1 collagen has a triple-helical form which is caused by its amino acid composition. Its specific domain follows an order of G-X-Y In which the X and Y slots are occupied by any amino acid other than guanine however these slots are typically occupied by both hydroxyproline and proline, not in any particular order[6]. This specific conformation will end up being repeated and packed into a hexagonal structure in order to form collagen fibrils.

The molecular mass of type 1 collagen is 300,000 g/mol and assembles in one of two higher order molecular assemblies. It forms a large solid structure formed by strict and non-flexible protein interactions[7]. This large multi-protein structure is crucially held together by mainly hydrogen bonds and the fibrils conform to a typical diameter size between 25 - 400 nanometers in this fibril conformation[8].

Implications in Disease:[edit]

Mutations in genes encoding collagen type 1 are known to cause a myriad of different conditions including:

Cardiac Valvular type Ehlors-Danlos Syndrome: This type of Ehlors-Danlos is caused by mutations within the COL1alpha2 gene, which is responsible for encoding the collagen pro-alpha2 chain. [9]

Vascular type Ehlors-Danlos Syndrome: Some patients with Vascular type Ehlors-Danlos, which is casued by mutations in COL3alpha1, are known to also have mutations in the COL1alpha1 gene. However the exact associations remain unknown. [10]

Athrochalasia type Ehlors-Danlos Syndrome: This type of Ehlors-Danlos is caused by the mutation of the COL1alpha1 and COL1alpha2 genes, which are responsible for encoding the proalpha1 and proalpha2 chains respectively.

Osteogenisis Imperfecta (types 1-4): Mutations in COL1alpha 1 and/or COL1alpha2 are known to cause several different types of Osterogenisis Imperfecta with the severity of said diseases being related to the type and frequency of the mutations occurring. [11] Add more from same source. For further information on COL1's effect in this disease, see Collagen, type 1, alpha 1.

Caffey Disease: This condition is caused by a mutation in the COL1alpha gene that replaces arginine with cysteine at the 836 protein site. This particular mutation causes the fibrils of type 1 to vary much greater in both the size and the shape. [12]

References[edit]

  1. ^ "Collagen: What It Is, Types, Function & Benefits". Cleveland Clinic. Retrieved 2023-10-25.
  2. ^ Ricard-Blum, Sylvie (2011-1). "The Collagen Family". Cold Spring Harbor Perspectives in Biology. 3 (1): a004978. doi:10.1101/cshperspect.a004978. ISSN 1943-0264. PMC 3003457. PMID 21421911. {{cite journal}}: Check date values in: |date= (help)
  3. ^ Ricard-Blum, Sylvie (2011-1). "The Collagen Family". Cold Spring Harbor Perspectives in Biology. 3 (1): a004978. doi:10.1101/cshperspect.a004978. ISSN 1943-0264. PMC 3003457. PMID 21421911. {{cite journal}}: Check date values in: |date= (help)
  4. ^ "COL1A2 gene: MedlinePlus Genetics". medlineplus.gov. Retrieved 2023-10-25.
  5. ^ Canty-Laird, Elizabeth G.; Lu, Yinhui; Kadler, Karl E. (2012-01-15). "Stepwise proteolytic activation of type I procollagen to collagen within the secretory pathway of tendon fibroblasts in situ". Biochemical Journal. 441 (Pt 2): 707–717. doi:10.1042/BJ20111379. ISSN 0264-6021. PMC 3430002. PMID 21967573. {{cite journal}}: no-break space character in |first3= at position 5 (help); no-break space character in |first= at position 10 (help); no-break space character in |title= at position 40 (help)
  6. ^ Naomi, Ruth; Ridzuan, Pauzi Muhd; Bahari, Hasnah (2021-08-09). "Current Insights into Collagen Type I". Polymers. 13 (16): 2642. doi:10.3390/polym13162642. ISSN 2073-4360. PMC 8399689. PMID 34451183.{{cite journal}}: CS1 maint: unflagged free DOI (link)
  7. ^ Xia, Shiyu; Chen, Zhenhang; Shen, Chen; Fu, Tian-Min (2021-9). "Higher-order assemblies in immune signaling: supramolecular complexes and phase separation". Protein & Cell. 12 (9): 680–694. doi:10.1007/s13238-021-00839-6. ISSN 1674-800X. PMC 8403095. PMID 33835418. {{cite journal}}: Check date values in: |date= (help)
  8. ^ Naomi, Ruth; Ridzuan, Pauzi Muhd; Bahari, Hasnah (2021-08-09). "Current Insights into Collagen Type I". Polymers. 13 (16): 2642. doi:10.3390/polym13162642. ISSN 2073-4360. PMC 8399689. PMID 34451183.{{cite journal}}: CS1 maint: unflagged free DOI (link)
  9. ^ "Cardiac-Valvular Ehlers-Danlos Syndrome (cvEDS)". The Ehlers Danlos Society. Retrieved 2023-09-27.
  10. ^ "Ehlers Danlos Syndromes - Symptoms, Causes, Treatment | NORD". rarediseases.org. Retrieved 2023-09-27.
  11. ^ Gajko-Galicka, Anna (2002). "Mutations in type I collagen genes resulting in osteogenesis imperfecta in humans". Acta Biochimica Polonica. 49 (2): 433–441. ISSN 0001-527X. PMID 12362985.
  12. ^ "Caffey disease: MedlinePlus Genetics". medlineplus.gov. Retrieved 2023-09-27.
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