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	<title>Translations:Collagen/23/en - Revision history</title>
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		<title>FuzzyBot: Importing a new version from external source</title>
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		<summary type="html">&lt;p&gt;Importing a new version from external source&lt;/p&gt;
&lt;p&gt;&lt;b&gt;New page&lt;/b&gt;&lt;/p&gt;&lt;div&gt;# Inside the cell&lt;br /&gt;
## Two types of alpha chains – alpha-1 and alpha 2, are formed during [[translation (genetics)|translation]] on ribosomes along the [[rough endoplasmic reticulum]] (RER). These peptide chains known as preprocollagen, have registration peptides on each end and a [[signal peptide]].&lt;br /&gt;
## Polypeptide chains are released into the lumen of the RER.&lt;br /&gt;
## Signal peptides are cleaved inside the RER and the chains are now known as pro-alpha chains.&lt;br /&gt;
## [[Hydroxylation]] of [[lysine]] and [[proline]] amino acids occurs inside the lumen. This process is dependent on and consumes [[ascorbic acid]] (vitamin C) as a [[cofactor (biochemistry)|cofactor]].&lt;br /&gt;
## [[Glycosylation]] of specific hydroxylysine residues occurs.&lt;br /&gt;
## Triple alpha helical structure is formed inside the endoplasmic reticulum from two alpha-1 chains and one alpha-2 chain.&lt;br /&gt;
## [[Procollagen]] is shipped to the [[Golgi apparatus]], where it is packaged and secreted into extracellular space by [[exocytosis]].&lt;br /&gt;
# Outside the cell&lt;br /&gt;
## Registration peptides are cleaved and tropocollagen is formed by [[procollagen peptidase]].&lt;br /&gt;
## Multiple tropocollagen molecules form collagen fibrils, via covalent cross-linking ([[aldol reaction]]) by [[lysyl oxidase]] which links hydroxylysine and lysine residues. Multiple collagen fibrils form into collagen fibers.&lt;br /&gt;
## Collagen may be attached to cell membranes via several types of protein, including [[fibronectin]], [[laminin]], [[fibulin]] and [[integrin]].&lt;/div&gt;</summary>
		<author><name>FuzzyBot</name></author>
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