Sandbox Reserved 1645: Difference between revisions
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== Biological Function == | == Biological Function == | ||
Fibrillin-1 is a ubiquitous protein mostly expressed in muscles in its monomeric form. The monomers then polymerize to form the 10 to 12nm of diameter '''microfibrils'''. In the microfibrils the fibrillin-1 is associated to various proteins such as [[MAGP-1]], [[MAGP-2]], [[fibulin 2]] and [[fibulin 5]], [[elastin]], [[versicane]] and [[LTBP-1]]. Those microfibrils constitute the elastic and non-elastic human connective tissues such as the dermis or the organs. This protein plays an important role in the [https://en.wikipedia.org/wiki/Cytokine cytokine] and growth factor regulation. <ref> | Fibrillin-1 is a ubiquitous protein mostly expressed in muscles in its monomeric form. The monomers then polymerize to form the 10 to 12nm of diameter '''microfibrils'''. In the microfibrils the fibrillin-1 is associated to various proteins such as [[MAGP-1]], [[MAGP-2]], [[fibulin 2]] and [[fibulin 5]], [[elastin]], [[versicane]] and [[LTBP-1]]. Those microfibrils constitute the elastic and non-elastic human connective tissues such as the dermis or the organs. This protein plays an important role in the [https://en.wikipedia.org/wiki/Cytokine cytokine] and growth factor regulation. <ref>Robert N. Ono, Gerhard Sengle, Noe L. Charbonneau, Valerie Carlberg, Hans Peter Bächinger, Takako Sasaki, Sui Lee-Arteaga, Lior Zilberberg, Daniel B. Rifkin, Francesco Ramirez, Mon-LiChu, Lynn Y.Sakai. (2009). Latent Transforming Growth Factor β-binding Proteins and Fibulins Compete for Fibrillin-1 and Exhibit Exquisite Specificities in Binding Sites. ''Journal of Biological Chemistry'', volume (284). https://www.sciencedirect.com/science/article/pii/S0021925818665056</ref> | ||
== Diseases caused by mutation == | == Diseases caused by mutation == | ||
