Document Detail

Biosynthesis, processing, and intracellular transport of lysosomal acid phosphatase in rat hepatocytes.
MedLine Citation:
PMID:  1699935     Owner:  NLM     Status:  MEDLINE    
The biosynthesis, processing, and intracellular transport of lysosomal acid phosphatase was studied using an in vitro cell-free translation system, pulse-chase experiments with primary cultured rat hepatocytes and subcellular fractionation techniques of rat liver after pulse-labeling with [35S]methionine in vivo. The single polypeptide of 45 kDa translated in the cell-free system from membrane-bound polysomal RNAs was converted to the 64 kDa form when the translation was carried out in the presence of microsomal vesicles. Pulse-chase experiments using cultured rat hepatocytes showed that acid phosphatase is initially synthesized as an endo-beta-N-acetylglucosaminidase H (Endo H)-sensitive form of 64 kDa, and processed via an Endo H-sensitive intermediate form of 62 kDa to an Endo H-resistant form with a 67 kDa mass. Phase separation with Triton X-114 showed that both the 64 and 67 kDa forms have hydrophobic properties. Treatment of the cells with chloroquine or tunicamycin, drugs which enhance the secretion of lysosomal hydrolases, had no effect on the normal transport of acid phosphatase to lysosomes. Acid phosphatase did not contain the phosphorylated high mannose type of oligosaccharide chains observed in cathepsin D. Subcellular fractionation experiments in conjunction with pulse-labeling in vivo showed that the acid phosphatase of the 67 kDa form was present in the Golgi heavy fraction (GF3) and the Golgi light fraction (GF1+2) enriched in cis and trans Golgi elements, respectively, at 30 min after the administration of [35S]methionine. Simultaneously, this polypeptide was also found in the lysosomal membrane fraction, thereby indicating that acid phosphatase is delivered to lysosomes in a membrane-bound form, immediately after reaching the trans-Golgi region.(ABSTRACT TRUNCATED AT 250 WORDS)
Y Tanaka; R Harada; M Himeno; K Kato
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Publication Detail:
Type:  In Vitro; Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Journal of biochemistry     Volume:  108     ISSN:  0021-924X     ISO Abbreviation:  J. Biochem.     Publication Date:  1990 Aug 
Date Detail:
Created Date:  1990-12-27     Completed Date:  1990-12-27     Revised Date:  2007-12-19    
Medline Journal Info:
Nlm Unique ID:  0376600     Medline TA:  J Biochem     Country:  JAPAN    
Other Details:
Languages:  eng     Pagination:  278-86     Citation Subset:  IM    
Division of Physiological Chemistry, Faculty of Pharmaceutical Sciences, Kyushu University.
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MeSH Terms
Acid Phosphatase / biosynthesis*,  metabolism
Blotting, Northern
Cell-Free System
Cells, Cultured
Electrophoresis, Polyacrylamide Gel
Endoplasmic Reticulum / enzymology
Glycoside Hydrolases / metabolism
Horseradish Peroxidase / diagnostic use
Liver / cytology,  enzymology*
Lysosomes / enzymology*
Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase
Neuraminidase / diagnostic use
Poly A / metabolism
Polyethylene Glycols / diagnostic use
Precipitin Tests
RNA / isolation & purification
Rats, Inbred Strains
Reticulocytes / metabolism
Subcellular Fractions / enzymology
Reg. No./Substance:
0/Polyethylene Glycols; 24937-83-5/Poly A; 63231-63-0/RNA; 9036-19-5/Nonidet P-40; EC 1.11.1.-/Horseradish Peroxidase; EC Phosphatase; EC 3.2.1.-/Glycoside Hydrolases; EC; EC Endo-beta-N-Acetylglucosaminidase

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

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