Glycosyl-phosphatidylinositol (GPI)-anchored renal dipeptidase is released by a phospholipase C in vivo.
The release mechanism of the glycosyl-phosphatidylinositol (GPI)-anchored renal dipeptidase (EC 3.4.13.19) in vivo has been investigated. Triton X-114 phase separation indicated that the dipeptidase is exclusively present as a hydrophilic form in urine from porcine, rat, rabbit and human. Western blot analysis of human and porcine purified dipeptidase and the urine concentrates with anti-(cross-reacting determinant) serum demonstrated the presence of inositol 1,2-cyclic monophosphate indicating that the renal dipeptidase had been released from the membrane by the action of a phospholipase C. This is the first direct evidence for cleavage of a human GPI-anchored protein by a responsible phospholipase C in vivo.
Park
Sung Wook
SW
College of Pharmacy, Hormone Research Center, Chonnam National University, Kwangju, Korea.
Choi
Kyong
K
Lee
Hwanghee Blaise
HB
Park
Sung Kwang
SK
Turner
Anthony J
AJ
Hooper
Nigel M
NM
Park
Haeng Soon
HS
D000818:Animals; D004150:Dipeptidases / Q000737:chemistry / Q000378:metabolism* / Q000652:urine; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D007295:Inositol Phosphates / Q000032:analysis; D007668:Kidney / Q000201:enzymology; D011817:Rabbits; D051381:Rats; D013552:Swine; D010738:Type C Phospholipases / Q000502:physiology*; D014867:Water
D007295:Inositol Phosphates; D014867:Water; C010199:inositol cyclic phosphate; D010738:Type C Phospholipases; D004150:Dipeptidases; C038937:dipeptidase