Document Detail


Stimulation by lysosomal enzymes and mannose-6-phosphate of a phosphoprotein phosphatase activity associated with the lysosomal enzyme binding receptor protein from monkey brain.
MedLine Citation:
PMID:  8394096     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Previously we have isolated a lysosomal enzyme binding receptor protein from monkey brain that exhibits protein kinase activity and undergoes phosphorylation on serine and tyrosine residues. Using the 32P-labelled receptor protein, we have found that the lysosomal enzyme fucosidase and mannose-6-phosphate, which are ligands for the receptor, stimulated a protein phosphatase activity associated with the receptor protein. Stimulation of protein phosphatase activity using the 32P-labelled receptor protein was demonstrated both by the loss in radioactivity of the receptor and by the release of 32P-phosphate. There was no stimulation by a non-lysosomal glycoprotein enzyme, or by the sugars mannose or glucose. Both serine-phosphate and tyrosine-phosphate residues were dephosphorylated. Stimulation of protein phosphatase activity by fucosidase and mannose-6-phosphate was also demonstrated using as substrate histone 32P-labelled, on serine/threonine or tyrosine residues. Insulin-like growth factor II, another known ligand for the lysosomal enzyme binding receptor, did not show any significant effect, either on the phosphorylation or dephosphorylation of the receptor protein. Our previous and present results suggest that a phosphorylation/dephosphorylation mechanism may be operative in the ligand binding and functions of the receptor.
Authors:
K Panneerselvam; A S Balasubramanian
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Cellular signalling     Volume:  5     ISSN:  0898-6568     ISO Abbreviation:  Cell. Signal.     Publication Date:  1993 May 
Date Detail:
Created Date:  1993-09-16     Completed Date:  1993-09-16     Revised Date:  2009-11-19    
Medline Journal Info:
Nlm Unique ID:  8904683     Medline TA:  Cell Signal     Country:  ENGLAND    
Other Details:
Languages:  eng     Pagination:  269-77     Citation Subset:  IM    
Affiliation:
Department of Neurological Sciences, Christian Medical College Hospital, Vellore, India.
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MeSH Terms
Descriptor/Qualifier:
Animals
Brain Chemistry*
Carbohydrates / pharmacology
Enzyme Activation / drug effects
Haplorhini / metabolism
Histones / metabolism
Insulin-Like Growth Factor II / pharmacology
Ligands
Lysosomes / enzymology*
Mannosephosphates / pharmacology*
Nitrophenols / pharmacology
Organophosphorus Compounds / pharmacology
Phosphoprotein Phosphatases / metabolism*
Phosphorylation / drug effects
Protein Processing, Post-Translational / drug effects
Protein-Serine-Threonine Kinases / metabolism*
Protein-Tyrosine Kinases / metabolism*
Receptors, Cell Surface / metabolism*
Receptors, Cytoplasmic and Nuclear*
Sodium Fluoride / pharmacology
Stimulation, Chemical
Vanadates / pharmacology
alpha-L-Fucosidase / pharmacology*
Chemical
Reg. No./Substance:
0/Carbohydrates; 0/Histones; 0/Ligands; 0/Mannosephosphates; 0/Nitrophenols; 0/Organophosphorus Compounds; 0/Receptors, Cell Surface; 0/Receptors, Cytoplasmic and Nuclear; 0/Vanadates; 0/cation-dependent mannose-6-phosphate receptor; 330-13-2/nitrophenylphosphate; 3672-15-9/mannose-6-phosphate; 67763-97-7/Insulin-Like Growth Factor II; 7681-49-4/Sodium Fluoride; EC 2.7.10.1/Protein-Tyrosine Kinases; EC 2.7.11.1/Protein-Serine-Threonine Kinases; EC 3.1.3.16/Phosphoprotein Phosphatases; EC 3.2.1.51/alpha-L-Fucosidase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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