Laminin: Difference between revisions
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Laminin is the fundamental protein that assemble the basal lamina or the basement membrane. Laminin molecules are the first moleules to be formed in the early stage of the basal lamina. In terms of composition, three long polypeptide chains: alpha, beta and gamma chains, form the protein laminin. These chains twist and turn via | Laminin is the fundamental protein that assemble the [[Basal lamina|basal lamina]] or the basement membrane. Laminin [[molecules|molecules]] are the first moleules to be formed in the early stage of the basal lamina. In terms of composition, three long [[Polypeptide|polypeptide chains]]: alpha, beta and gamma chains, form the protein laminin. These chains twist and turn via [[Disulphide_bond|disulphide bonds]] give rise to the asymmetric shape of the protein. Due to the presence of [[isoform|isoforms]] of each chains, different combinations of these isoforms can be produced. Hence, each combinations create different set of laminin, each with different functions, structures and characteristic <ref>Alberts, A., Johnson, A., Lewis, J., Raff, M., Roberts, K. and Walter, P. (2008) Molecular Biology of The Cell, 5th Edition, New York: Garland Science.</ref>.<br> | ||
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Latest revision as of 07:12, 23 October 2012
Laminin is the fundamental protein that assemble the basal lamina or the basement membrane. Laminin molecules are the first moleules to be formed in the early stage of the basal lamina. In terms of composition, three long polypeptide chains: alpha, beta and gamma chains, form the protein laminin. These chains twist and turn via disulphide bonds give rise to the asymmetric shape of the protein. Due to the presence of isoforms of each chains, different combinations of these isoforms can be produced. Hence, each combinations create different set of laminin, each with different functions, structures and characteristic [1].
Reference
- ↑ Alberts, A., Johnson, A., Lewis, J., Raff, M., Roberts, K. and Walter, P. (2008) Molecular Biology of The Cell, 5th Edition, New York: Garland Science.