Laminines in the structure of glomerular basement membrane
Abstract
Laminines are high weighted glycosylated proteins that communicate with each other and forming at least 15 heterotrimeric macromolecules. Laminin-521 is one of the key molecules in the glomerular basal membrane and is synthesized by podocytes and endothelial cells. The majority of laminins form a cruciform structure, short globular processes of which (LN-domains) are responsible for laminin interaction in the extracellular environment. This interaction leads to polymerization of laminin, underlying the formation of the basal membrane. Polymerization of laminins forms a mesh crystalloid structure. Moreover, the polymerization of laminins in vivo does not occur in liquids, this process requires the connection of laminins with cellular receptors. Domains LG1-3 laminine are associated primarily with integrins, and LG4-5 - with α-dystroglycan (a-DG), heparan sulfate and sulfated glycolipids (sulfatide). The research of laminin mutations in the laboratory allows to study in details its probable role in the development of glomerulopathy and glomerular membrane remodeling in pathological processes.
About the Authors
M. M. Batiushin
Rostov State Medical University
Russian Federation
Russian Federation
D. G. Pasechnic
Rostov State Medical University
Russian Federation
Russian Federation
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Review
For citations:
Batiushin M.M., Pasechnic D.G. Laminines in the structure of glomerular basement membrane. Nephrology (Saint-Petersburg). 2016;20(5):9-15. (In Russ.)
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