The structure of the normal human glomerular basement membrane. Ultrastructural localization of type IV collagen and laminin.
Structural models of the glomerular basement membrane (GBM) have been based solely on the localization of antigens in animal kidneys. These models depict a type IV collagen lattice as the structural skeleton along the central portion of the membrane, with the glycoprotein laminin attached predominantly in the laminae rarae where it is thought to be involved with endothelial and visceral epithelial cell attachment. The human GBM is also known to contain type IV collagen and laminin. The present study localizes both of these structural antigens in normal human GBM using the ultrastructural immunogold technique. Type IV collagen is situated in the sub-endothelial third of the GBM and is continuous with the type IV collagen within the mesangial matrix. Laminin is localized throughout the entire thickness of the GBM and mesangial matrix. These results indicate that the structure of human GBM is significantly different from that proposed in animal models. A structure for the normal human GBM is discussed, depicting a thin type IV collagen lattice which is asymmetrically placed in the sub-endothelial third of the membrane, with laminin distributed as an integral component of the membrane in addition to its role in cell attachment.
Smith
P S
PS
Division of Tissue Pathology, University of Adelaide.
Fanning
J C
JC
Aarons
I
I
D001485:Basement Membrane / Q000378:metabolism / Q000648:ultrastructure; D003094:Collagen / Q000378:metabolism*; D006801:Humans; D007150:Immunohistochemistry; D007678:Kidney Glomerulus / Q000378:metabolism / Q000648:ultrastructure*; D007797:Laminin / Q000378:metabolism*; D008854:Microscopy, Electron; D012016:Reference Values; D014018:Tissue Distribution
D007797:Laminin; D003094:Collagen