@article{oai:niigata-u.repo.nii.ac.jp:00006533,
 author = {Nishi, Shinichi and Arakawa, Masaaki},
 issue = {1},
 journal = {Acta medica et biologica, Acta medica et biologica},
 month = {Mar},
 note = {Recent studies have revealed highly differentiated structures and functions of glomerular basement membrane (GBM). The most specific feature of the GBM is a three-layer structure, i.e. a lamina densa and two laminae rarae. The GBM consists of various components, such as type IV collagen, laminin and proteoglycans, in forming its three-dimensional network structure. This structure is thought to result from a self-assembling of each component and binding each other. The subclasses of the components have been differentiated and their distributions have been proved to be heterogeneous with the GBM. These structural characteristics are supposed to be related to the function of the GBM as a sieving membrane and as a base for cellular attachment. The mechanism of pathological damage to the structure and function of the GBM has been elucidated in various renal diseases with advances in the basic studies on the GBM. Matrix metalloprotainase (MMP) is considered to be important in GBM injuries of IgA nephropathy. Glycosylation of GBM components is suggested to be one of the causes of thickening of the GBM. A genetic mutation in α5(IV) chain of type IV collagen has been confirmed in Alport's syndrome.},
 pages = {1--9},
 title = {Recent Advances in Basic and Clinical Studies of Glomerular Basement Membrane (GBM)},
 volume = {41},
 year = {1993}
}