S-adenosylhomocysteine (SAH) hydrolase is a cytosolic enzyme present in the
kidney. Enzyme activities of SAH hydrolase were measured in the kidney in
isolated glomeruli and tubules. SAH hydrolase activity was 0.62 +/- 0.02 mU
/mg in the kidney, 0.32 +/- 0.03 mU/mg in the glomeruli, and 0.50 +/- 0.02
mU/mg in isolated tubules. Using immunohistochemical methods, we describe t
he localization of the enzyme SAH hydrolase in rat kidney with a highly spe
cific antibody raised in rabbits against purified SAH hydrolase from bovine
kidney. This antibody crossreacts to almost the same extent with the SAH h
ydrolase from different species such as rat, pig, and human. Using light mi
croscopy, SAH hydrolase was visualized by the biotin-streptavidin-alkaline
phosphatase immunohistochemical procedure. SAH hydrolase immunostaining was
observed in glomeruli and in the epithelium of the proximal and distal tub
ules. The collecting ducts of the cortex and medulla were homogeneously sta
ined. By using double immunofluorescence staining and two-channel immunoflu
orescence confocal laser scanning microscopy, we differentiated the glomeru
lar cells (endothelium, mesangium, podocytes) and found intensive staining
of podocytes. Our results show that the enzyme SAH hydrolase is found ubiqu
itously in the rat kidney. The prominent staining of SAH hydrolase in the p
odocytes may reflect high rates of transmethylation.