Document Detail


Binding receptors for alpha-L-fucosidase in human B-lymphoid cell lines.
MedLine Citation:
PMID:  1327338     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
An established mechanism for directing newly made acid hydrolases to lysosomes involves acquisition of mannose 6-phosphate residues by the carbohydrate portion of acid hydrolases followed by binding to specific membrane-bound transport receptors and delivery to lysosomes. Two distinct phosphomannosyl receptors (CI-MPR and CD-MPR) have been identified. Alternative mechanisms for trafficking acid hydrolases exist. This report examines means for the possible receptor-mediated intracellular transport of alpha-L- fucosidase in lymphoid cells. The binding of alpha-L-fucosidase to intact cells and to total cell membrane preparations, in conjunction with immunoassays of solubilized membrane preparations, revealed the presence of CI-MPR and CD-MPR on human lymphoid and fibroblast cell lines. The mean level of CD-MPR in nine lymphoid cell lines was 7.2-fold greater than CI-MPR. The mean level of CI-MPR in two fibroblast lines was 3.8-fold greater than CD-MPR. The mean content of CI-MPR was 19.5-fold greater in the fibroblasts than in the lymphoid cells. The CD-MPR content of fibroblasts and lymphoid cells was nearly equivalent. Among these cell lines were a fibroblast and a lymphoid line from the same individual. These results indicate that human B-lymphoid cells are deficient in CI-MPR and suggest that modulation of expression of CI-MPR and CD-MPR in lymphoid cells differs from that in fibroblasts, including cell lines with identical genomes. No specific receptor capable of binding alpha-L-fucosidase independent of mannose 6-phosphate was demonstrable, despite published results that support the existence of a mannose 6-phosphate independent trafficking mechanism in lymphoid cells for this enzyme.
Authors:
R A Dicioccio; A L Miller
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Glycoconjugate journal     Volume:  9     ISSN:  0282-0080     ISO Abbreviation:  Glycoconj. J.     Publication Date:  1992 Feb 
Date Detail:
Created Date:  1992-11-06     Completed Date:  1992-11-06     Revised Date:  2008-08-22    
Medline Journal Info:
Nlm Unique ID:  8603310     Medline TA:  Glycoconj J     Country:  ENGLAND    
Other Details:
Languages:  eng     Pagination:  56-62     Citation Subset:  IM    
Affiliation:
Department of Gynaecologic Oncology, Roswell Park Cancer Institute, Buffalo, NY 14263.
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MeSH Terms
Descriptor/Qualifier:
B-Lymphocytes / metabolism*
Carrier Proteins*
Cell Line
Cell Membrane / metabolism
Humans
Immunoassay
Mucolipidoses / enzymology*
Receptors, Cell Surface / analysis*
Receptors, Cytoplasmic and Nuclear*
Reference Values
alpha-L-Fucosidase / isolation & purification,  metabolism*
Grant Support
ID/Acronym/Agency:
DK32161/DK/NIDDK NIH HHS; NS12138/NS/NINDS NIH HHS
Chemical
Reg. No./Substance:
0/Carrier Proteins; 0/Receptors, Cell Surface; 0/Receptors, Cytoplasmic and Nuclear; 0/cation-dependent mannose-6-phosphate receptor; EC 3.2.1.51/alpha-L-Fucosidase

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