Sandbox Q123: Difference between revisions

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== Structural insights ==

<scene name='43/430871/Cv/3'>Fn is a dimer of homologous monomers</scene> linked by S-S bond. Each monomer contains 3 types of repeating units: ~~FnI~~, ~~FnII~~ and ~~FnIII~~. 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., ~~FnI~~6-~~FnII~~1-2-~~FnI~~7-9 is the gelatin binding domain (GBD).

<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 I6-FN II1-2-FN I7-9 is the gelatin binding domain (GBD).

== Function ==

~~[[Fibronectin]] (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"~~>PMID:12244123<~~/~~ref~~><ref name="Proctor"~~>PMID:3326130<~~/~~ref~~>. In addition, Fn is also important for the adherence of pathogens to host tissues and the linking between proteins and cells<ref name="Mosher">PMID:6326663</ref>.

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 ==

Fn is associated with inflammation area and the process of wound healing~~. Fn~~ is a potential marker for radiation resistance.

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 ==

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>.

Sandbox Q123: Difference between revisions

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 == Structural insights ==
-<scene name='43/430871/Cv/3'>Fn is a dimer of homologous monomers</scene> linked by S-S bond. Each monomer contains 3 types of repeating units: FnI, FnII and FnIII. 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., FnI<sub>6</sub>-FnII<sub>1-2</sub>-FnI<sub>7-9</sub> is the gelatin binding domain (GBD).
+<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 ==
-[[Fibronectin]] (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">PMID:12244123</ref><ref name="Proctor">PMID:3326130</ref>. In addition, Fn is also important for the adherence of pathogens to host tissues and the linking between proteins and cells<ref name="Mosher">PMID:6326663</ref>.
+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 ==
-Fn is associated with inflammation area and the process of wound healing. Fn is a potential marker for radiation resistance.
+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 ==
-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>.