Oligodendrocyte-myelin glycoprotein is present in lipid rafts and caveolin-1-enriched membranes.

The oligodendrocyte-myelin glycoprotein is a ligand of the neuronal Nogo receptor and a potent inhibitor of neurite outgrowth, but its physiological function remains to be elucidated. The oligodendrocyte-myelin glycoprotein is anchored solely in the outer leaflet of the plasma membrane via its glycosylphosphatidylinositol anchor, and through its leucine-rich repeat domain, it likely interacts with other proteins. In the present study, we compare its buoyancy and detergent solubility characteristics with those of other myelin proteins.

Redistribution of integrins in tubular epithelial cells during diabetic glycogen nephrosis.

Background/aims: Even though many aspects of glycogen nephrosis in diabetes have already been studied, adhesion interactions between the glycogen-accumulating clear cells and the tubular basement membranes have not been addressed. As integrins play key roles in cell-to-matrix interactions, we investigated the expression and distribution of alpha3-, alphaV-, beta1- and beta3-integrin subunits in renal tissues from streptozotocin-induced hyperglycemic rats (3 months old) and their age-matched controls as well as from streptozotocin-injected normoglycemic animals.

Methods: The levels and distribution of integrins were studied by immunocytochemistry and Western blot analysis.

Apoptosis of tubular epithelial cells in glycogen nephrosis during diabetes.

The important problem of the fate of glycogen-accumulating clear cells in glycogen nephrosis is still unsettled. In this study, we examine whether apoptosis plays a relevant role in the development of diabetic glycogen nephrosis and explore the involvement of the Fas/Fas-L system and the activation of the caspase cascade. Diabetes was induced in rats by streptozotocin injection.