Protective protein as an endogenous endothelin degradation enzyme in human tissues.
An enzyme hydrolyzing the carboxyl terminus of endothelin-1 was detected in control human tissues but was deficient in tissues from a patient with galactosialidosis, a metabolic disease caused by the protective protein gene mutation. It was proportional to the amount of immunologically estimated mature protective protein. An antibody against the lysosomal protective protein/beta-galactosidase complex precipitated the enzyme activity almost completely. Transfection of the human cDNA for protective protein resulted in high expression of the enzyme activity in transformed fibroblasts from a galactosialidosis patient. These results indicated that the mature protective protein is a major soluble endogenous endothelin degradation enzyme in human tissues.
Itoh
K
K
Department of Clinical Genetics, Tokyo Metropolitan Institute of Medical Science, Japan.
Kase
R
R
Shimmoto
M
M
Satake
A
A
Sakuraba
H
H
Suzuki
Y
Y
D001921:Brain / Q000201:enzymology; D002268:Carboxypeptidases / Q000235:genetics / Q000378:metabolism*; D043402:Cathepsin A; D018076:DNA, Complementary; D016232:Endothelins / Q000378:metabolism*; D006023:Glycoproteins / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D007668:Kidney / Q000201:enzymology; D008099:Liver / Q000201:enzymology; D008168:Lung / Q000201:enzymology; D016464:Lysosomal Storage Diseases / Q000201:enzymology; D011233:Precipitin Tests; D001616:beta-Galactosidase / Q000235:genetics / Q000378:metabolism
D018076:DNA, Complementary; D016232:Endothelins; D006023:Glycoproteins; D001616:beta-Galactosidase; D002268:Carboxypeptidases; C468629:CTSA protein, human; D043402:Cathepsin A