ABSTRACT
The review summarizes recent achievements in biochemistry of basal lamina which is highly specialized structural element of extracellular matrix. Structural and functional characteristics of main basal lamina proteins are reviewed including collagen type IV, laminin, nidogen, and heparan sulfate-containing proteoglycans. Special attention is paid to characteristics of structure and biochemical composition of renal glomerular basal lamina which is one of the main components of renal filtration barrier. Possible methods of investigation and characterization of new basal lamina proteins are discussed which help in understanding of biochemical composition of this structure.
Subject(s)
Basement Membrane/metabolism , Extracellular Matrix Proteins/metabolism , Extracellular Matrix Proteins/chemistry , Structure-Activity RelationshipABSTRACT
The protein composition of various structural divisions of human kidney was studied using two-dimensional electrophoresis. Two-dimensional electrophoregrams of the cortical substance of human kidney revealed 165 polypeptide fractions within the pH range of 4.5-7.5, having molecular masses of 10 to 330 kDa. Electrophoresis of glomerular proteins gave 155 fractions with M(r) = 15-300 kDa, whereas fractionation of glomerular basement membrane proteins gave 40 fractions with M(r) = 30-330 kDa within the same range of pH. The M(r) values for all fractions and the relative electrophoretic mobility in the forward direction were determined. A comparative analysis of the electrophoregrams was conducted. The data obtained were used to construct two-dimensional maps of the cortical substance and glomerular proteins of human kidney.
Subject(s)
Kidney Cortex/metabolism , Kidney Glomerulus/metabolism , Proteins/metabolism , Electrophoresis, Gel, Two-Dimensional , Humans , Isoelectric FocusingABSTRACT
A technique was developed for analysis of basal membrane proteins from rat kidney glomerulus using two-dimensional electrophoresis by O'Farrell. Basal membranes were isolated from the glomerulus by means of detergent treatment. Various procedures of basal membrane solubilization were studied. About 25 protein fractions with molecular mass from 25 kDa to 330 kDa were detected in the basal membrane after single-dimensional electrophoresis in presence of sodium dodecyl-sulfate. Two-dimensional electrophoresis of the basal membrane proteins and staining of gels with silver nitrate enabled to detect approximately 50 polypeptide fractions with molecular mass from 25 kDa up to 250 kDa at pH 5-7.
