Podocyte flattening and disorder of glomerular basement membrane are associated with splitting of dystroglycan-matrix interaction
K Kojima, A Davidovits, H Poczewski… - Journal of the …, 2004 - journals.lww.com
The transmembrane component of the dystroglycan complex, a heterodimer of α-and β-
dystroglycan, was recently localized at the basal cell membrane domain of podocytes, and it
was speculated that it serves as a device of the podocyte for maintaining the complex
podocyte foot process architecture, and for regulating the exact position of its ligands, the
matrix proteins laminin and agrin, in the glomerular basement membrane (GBM). The
redistribution of dystroglycan in two experimental rat models of foot process flattening and …
dystroglycan, was recently localized at the basal cell membrane domain of podocytes, and it
was speculated that it serves as a device of the podocyte for maintaining the complex
podocyte foot process architecture, and for regulating the exact position of its ligands, the
matrix proteins laminin and agrin, in the glomerular basement membrane (GBM). The
redistribution of dystroglycan in two experimental rat models of foot process flattening and …