Sandbox Reserved 1645: Difference between revisions

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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.
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.


Role in the [https://en.wikipedia.org/wiki/Cytokine cytokine]:
Role in the [https://en.wikipedia.org/wiki/Cytokine cytokine] and '''growth factor regulation''':


This protein plays an important role in the '''cytokine''' and growth factor regulation. For example, fibrillin-1 can modulate the bioavailability of TGFβ1, which is a cytokine that regulates cell survival. Changed TGFβ signaling is a significant factor in the development of certain diseases.  A fibrillin-1 segment encoded by exons 44-49 triggers the release of TGFβ1 and consequently stimulates TGFβ receptor-mediated Smad2 signaling. Thereby, specific gene activation or repression can be induced. <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> <ref> Shazia S. Chaudhry, Stuart A. Cain, Amanda Morgan, Sarah L. Dallas, C. Adrian Shuttleworth, Cay M. Kielty; Fibrillin-1 regulates the bioavailability of TGFβ1. J Cell Biol 29 January 2007; 176 (3): 355–367. doi: https://doi.org/10.1083/jcb.200608167</ref>
This protein plays an important role in the cytokine and growth factor regulation. For example, fibrillin-1 can modulate the bioavailability of TGFβ1, which is a cytokine that regulates cell survival. Changed TGFβ signaling is a significant factor in the development of certain diseases.  A fibrillin-1 segment encoded by exons 44-49 triggers the release of TGFβ1 and consequently stimulates TGFβ receptor-mediated Smad2 signaling. Thereby, specific gene activation or repression can be induced. <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> <ref> Shazia S. Chaudhry, Stuart A. Cain, Amanda Morgan, Sarah L. Dallas, C. Adrian Shuttleworth, Cay M. Kielty; Fibrillin-1 regulates the bioavailability of TGFβ1. J Cell Biol 29 January 2007; 176 (3): 355–367. doi: https://doi.org/10.1083/jcb.200608167</ref>


'''Fetal''' '''cardiovascular''' development :
'''Fetal''' '''cardiovascular''' development :
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