Sandbox Q123
From Proteopedia
(Difference between revisions)
												
			
			| Line 3: | Line 3: | ||
== Structural insights ==  | == Structural insights ==  | ||
| - | <scene name='43/430871/Cv/3'>  | + | <scene name='43/430871/Cv/3'>Fibronectin (FN) is a dimer of homologous monomers</scene> linked by S-S bond. Each monomer contains 3 types of repeating units: FN I, FN II and FN III. Type I and type II repeats are disulfide-bonded loops, containing about 45 and 60 amino-acids each, while type III repeats are about 90 amino-acids long without S-S bonds<ref name="Pancov">PMID:12244123</ref><ref name="Proctor">PMID:3326130</ref><ref name="Richard">PMID:3916323</ref>. Each module contains several numbered protein binding domains, i.e., FN I<sub>6</sub>-FN II<sub>1-2</sub>-FN I<sub>7-9</sub> is the gelatin binding domain (GBD).   | 
== Function ==  | == Function ==  | ||
| - | + | FN is a glycoprotein which binds extracellular matrix components like integrin, collagen, fibrin and others.  It plays an important role in cell adhesion, migration and differentiation <ref name="Pancov"/><ref name="Proctor"/>. In addition, FN is also important for the adherence of pathogens to host tissues and the linking between proteins and cells<ref name="Proctor"/><ref name="Mosher">PMID:6326663</ref>.  | |
== Relevance ==  | == Relevance ==  | ||
| - | + | FN is associated with inflammation area and the process of wound healing<ref name="Proctor"/><ref name="Mosher"/>, and it is a potential marker for radiation resistance.  | |
== Disease ==  | == Disease ==  | ||
| - | Overexpression of Fn1 is associated with lung cancer<ref>PMID:16397245</ref>.  | + | FN can be divided into soluble and insoluble forms. Soluble FN can be found in plasma and other fluids which circulate in human body. The insoluble form is mainly found on the surface of cells and the extracellular matrix (ECM)<ref name="Pancov"/><ref name="Proctor"/><ref name="Mosher"/>. Although FN can  be synthesised by many cell types, soluble (plasma) FN was found to be mainly produced by hepatocytes. Therefore, for patients with liver diseases, the concentration of their plasma FN is lower<ref name="Proctor"/><ref name="Mosher"/>. In addition, Overexpression of Fn1 is associated with lung cancer<ref>PMID:16397245</ref>.  | 
Revision as of 07:44, 10 November 2022
  | |||||||||||
References
- ↑ 1.0 1.1 1.2 Pankov R, Yamada KM. Fibronectin at a glance. J Cell Sci. 2002 Oct 15;115(Pt 20):3861-3. PMID:12244123
 - ↑ 2.0 2.1 2.2 2.3 2.4 2.5 Proctor RA. Fibronectin: a brief overview of its structure, function, and physiology. Rev Infect Dis. 1987 Jul-Aug;9 Suppl 4:S317-21. doi:, 10.1093/clinids/9.supplement_4.s317. PMID:3326130 doi:http://dx.doi.org/10.1093/clinids/9.supplement_4.s317
 - ↑ Hynes R. Molecular biology of fibronectin. Annu Rev Cell Biol. 1985;1:67-90. doi: 10.1146/annurev.cb.01.110185.000435. PMID:3916323 doi:http://dx.doi.org/10.1146/annurev.cb.01.110185.000435
 - ↑ 4.0 4.1 4.2 4.3 Mosher DF. Physiology of fibronectin. Annu Rev Med. 1984;35:561-75. doi: 10.1146/annurev.me.35.020184.003021. PMID:6326663 doi:http://dx.doi.org/10.1146/annurev.me.35.020184.003021
 - ↑ Han S, Khuri FR, Roman J. Fibronectin stimulates non-small cell lung carcinoma cell growth through activation of Akt/mammalian target of rapamycin/S6 kinase and inactivation of LKB1/AMP-activated protein kinase signal pathways. Cancer Res. 2006 Jan 1;66(1):315-23. PMID:16397245 doi:http://dx.doi.org/10.1158/0008-5472.CAN-05-2367
 
