Document Detail


The structure of P-glycoprotein and the secretion of lysosomal enzymes in multidrug-resistant cells.
MedLine Citation:
PMID:  7805188     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
We have previously demonstrated that multidrug-resistant cells have a lower content of lysosomal enzymes, a consequence of an increased rate of secretion. The question was therefore to know whether an intact functional P-glycoprotein was necessary for expression of this property. Control NIH3T3 and mdr1-gene-transfected cells (pHaMDR1) were used together with 2 variants either lacking 23 amino acids at the carboxyl terminal (pHaMDRC 23) or in which 4 extra amino acids are inserted (pHaMDRBL2). Transfected and variant cells exhibited reduced uptake of [3H]-vinblastine and [3H]-daunomycin, a finding consistent with their drug resistance. By contrast, only pHaMDR1 cells had a reduced level of N-acetyl glucosaminidase that paralleled an increased rate of secretion of the same enzyme. The mutant cells secreted lysosomal enzyme at the same rate and had the same intracellular lysosomal enzyme content as NIH3T3 cells. Abnormal behavior of lysosomal enzymes in multidrug-resistant cells therefore seemed to require an intact P-glycoprotein molecule. Although sequestration in lysosomes and then secretion of drugs may possibly contribute to protection, it would not be an essential component of multidrug resistance.
Authors:
L Warren; A Malarska; J C Jardillier
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Cancer chemotherapy and pharmacology     Volume:  35     ISSN:  0344-5704     ISO Abbreviation:  Cancer Chemother. Pharmacol.     Publication Date:  1995  
Date Detail:
Created Date:  1995-02-02     Completed Date:  1995-02-02     Revised Date:  2007-11-15    
Medline Journal Info:
Nlm Unique ID:  7806519     Medline TA:  Cancer Chemother Pharmacol     Country:  GERMANY    
Other Details:
Languages:  eng     Pagination:  267-9     Citation Subset:  IM    
Affiliation:
Wistar Institute of Anatomy and Biology, Philadelphia, PA 19104.
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MeSH Terms
Descriptor/Qualifier:
3T3 Cells
Acetylglucosaminidase / secretion*
Amino Acid Sequence
Animals
Daunorubicin / metabolism
Drug Resistance, Multiple* / genetics,  physiology
Lysosomes / enzymology*
Mice
Molecular Sequence Data
Mutagenesis, Insertional
P-Glycoprotein / chemistry*,  genetics
Protein Engineering
Transfection
Vinblastine / metabolism
Grant Support
ID/Acronym/Agency:
CA 10815/CA/NCI NIH HHS; CA 19130/CA/NCI NIH HHS
Chemical
Reg. No./Substance:
0/P-Glycoprotein; 20830-81-3/Daunorubicin; 865-21-4/Vinblastine; EC 3.2.1.52/Acetylglucosaminidase

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


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