Ultrastructural immunocytochemistry of collagenous and non-collagenous proteins in fast-frozen, freeze-substituted, and low-temperature-embedded renal tissue in Alport syndrome.

This paper describes the ultrastructural immunolocalization of the alpha 2 chain of collagen IV, laminin, and the amino terminal propeptide of collagen I (N-Pro I) in glomeruli of rapidly frozen, freeze-substituted, and low-temperature-embedded renal biopsy specimens from two cases of Alport disease and from normal kidneys. The alpha 2 chain of collagen IV is present in the whole thickness of the basement membrane in glomeruli of Alport patients, while it is limited to the subendothelial portion of the basement membrane of normal glomeruli. Laminin has the same distribution in both normal and Alport glomeruli, but is apparently more concentrated along the basement membrane of normal glomeruli. N-Pro I is localized in mesangial areas and in the basement membrane in Alport cases, while it is not detected in normal glomeruli. These data suggest complex rearrangements of major constituents of the glomerular basement membrane network and demonstrate early deposition of fibrillary collagen proteins in the matrix before the appearance of banded collagen fibres. This finding could be an indicator of early evolution towards glomerulosclerosis.