PHOSPHOHEXOSYL RECOGNITION IS A GENERAL CHARACTERISTIC OF PINOCYTOSIS OF LYSOSOMAL GLYCOSIDASES BY HUMAN FIBROBLASTS
PHOSPHOHEXOSYL RECOGNITION IS A GENERAL CHARACTERISTIC OF PINOCYTOSIS OF LYSOSOMAL GLYCOSIDASES BY HUMAN FIBROBLASTS
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DOI:
10.1172/jci108860
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发表时间:
1977-01-01
影响因子:
15.9
通讯作者:
SLY, W
中科院分区:
文献类型:
--
作者:
KAPLAN, A;FISCHER, D;SLY, W
Data was presented showing that mannose-6-phosphate was a potent competitive inhibitor of pinocytosis of human platelet .beta.-glucuronidase, and that treatment of high-uptake forms of the enzyme with alkaline phosphatase destroyed the high-uptake property of the enzyme without diminishing its catalytic activity. These data indicated that phosphate was a necessary component of the recognition marker on the enzyme for pinocytosis by human fibroblasts, and suggested that the phosphate on high-uptake forms of the enzyme was present as a phosphohexosyl moiety. Results presented here showed that mannose-6-phosphate was also a potent inhibitor of pinocytosis of the following enzyme preparations: .beta.-glucuronidase from human spleen, liver, placenta and urine; .beta.-hexosaminidase and .beta.-galactosidase from human platelets; and .beta.-hexosaminidase from human fibroblast secretions. Alkaline phosphatase treatment of all of these enzymes except .beta.-galactosidase, which was unstable to the incubation conditions and could not be tested, greatly diminished the uptake activity of the enzymes without diminishing their catalytic activity. These results suggested that phosphohexosyl recognition was a general characteristic of pinocytosis of lysosomal glycosidases.