Structurally functional features of insulin and mechanism of its action

   
Prozorovskiy V.N.1, Lokhov P.G.1, Maslov D.L.1, Ipatova O.M.1

1. Institute of Biomedical Chemistry RAMS
Section: Experimental/Clinical Study
PubMed Id: 14569873
Year: 2003  Volume: 49  Issue: 1  Pages: 46-62
On the basis of analysis of own and literature data on insulin-receptor interaction two centers responsible for receptor binding were identified on 3D-structure of insulin with receptor. Two extracellular domains of insulin receptor interact with these centers on insulin molecule. The comparative analysis of primary structures of the protein disulfide isomerase thioredoxine domains and C-terminal domain of the receptor suggests existence of the thioredoxine domain in the insulin receptor. In this connection the role of the thiol disulfide an exchange reaction is discussed in terms of insulin interaction with receptor followed by subsequent conformational changes in the receptor molecule and activation of the intercellular tyrosine kinase domain. It is supposed, that besides known mechanism of receptor mediated insulin signal transduction and tyrosine kinase activation, there is other mechanism of insulin intracellular signal transduction realised via cytosolic insulin-binding proteins. Major components of intercellular insulin signal transduction include: protein disulfide isomerase and insulin degrading enzyme. The importance of change of the intracellular insulin degradation rate for insulin signal transduction is discussed.
Download PDF:
Citation:

Prozorovskiy, V. N., Lokhov, P. G., Maslov, D. L., Ipatova, O. M. (2003). Structurally functional features of insulin and mechanism of its action. Biomeditsinskaya khimiya, 49(1), 46-62.
References  
 2022 (vol 68)
 2021 (vol 67)
 2020 (vol 66)
 2019 (vol 65)
 2018 (vol 64)
 2017 (vol 63)
 2016 (vol 62)
 2015 (vol 61)
 2014 (vol 60)
 2013 (vol 59)
 2012 (vol 58)
 2011 (vol 57)
 2010 (vol 56)
 2009 (vol 55)
 2008 (vol 54)
 2007 (vol 53)
 2006 (vol 52)
 2005 (vol 51)
 2004 (vol 50)
 2003 (vol 49)