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PMID: 2850797 Published · ppublish English Journal Article

Subcellular localization of the enzymes that dephosphorylate myo-inositol polyphosphates in human platelets.

The Biochemical journal ·Vol. 255 ·No. 3 ·1988-11-01 ·Pages 795-800

Molina Y Vedia L, Nolan RD, Lapetina EG

Abstract

The phosphatase-induced hydrolysis of [3H]inositol 1,4-bisphosphate [Ins(1,4)P2)] and [3H]inositol 1,4,5-trisphosphate [Ins(1,4,5)P3] was studied in platelet subcellular fractions. The activity that hydrolyses Ins(1,4)P2 is cytosolic, whereas the activity that hydrolyses Ins(1,4,5)P3 is present in both particulate and cytosolic fractions. The cytosolic Ins(1,4)P2 phosphatase hydrolyses the 1-phosphate of Ins(1,4)P2, whereas the cytosolic and membrane-bound Ins(1,4,5)P3 phosphatases hydrolyse the 5-phosphate of Ins(1,4,5)P3. In the presence of ATP, it is possible to observe a cytosolic Ins(1,4,5)P3 3-kinase that phosphorylates Ins(1,4,5)P3 to inositol 1,3,4,5-tetrakisphosphate. Apparent Km values for the particulate and the cytosolic Ins(1,4,5)P3 phosphatases are 100 microM and 40 microM respectively. A large proportion of the membrane-associated Ins(1,4,5)P3 phosphatase can be extracted with 1 M-NaCl, and the Mr of this enzyme, as determined by hydrodynamic studies, is 49,000, whereas that of the cytosolic enzyme is 59,000. The Km values for the cytosolic Ins(1,4)P2 phosphatase is 40 microM; this enzyme has an Mr of 49,000. The highest specific activity of the Ins(1,4,5)P3 phosphatase is present in a highly purified plasma-membrane fraction.

MeSH Terms
Blood Platelets/enzymology Chromatography, High Pressure Liquid Cytosol/enzymology Humans Hydrolysis Inositol 1,4,5-Trisphosphate Inositol Phosphates/blood Inositol Polyphosphate 5-Phosphatases Phosphoric Monoester Hydrolases/blood Subcellular Fractions/enzymology Sugar Phosphates/blood
Chemicals
Inositol Phosphates Sugar Phosphates inositol 1,4-bis(phosphate) Inositol 1,4,5-Trisphosphate Phosphoric Monoester Hydrolases Inositol Polyphosphate 5-Phosphatases inositol-1,4-bisphosphate 1-phosphatase
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Molina Y Vedia L
Molecular Biology Department, Burroughs Wellcome Co., Research Triangle Park, NC 27709.
Nolan R D
Lapetina E G
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Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
DOI
10.1042/bj2550795
Published
1988-11-01
Pages
795-800
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1135311
Subset
IM
External Links
PubMed source DOI: 10.1042/bj2550795 PMC Full Text View journal details
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