Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
|
pubmed:dateCreated |
1992-11-6
|
pubmed:abstractText |
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.
|
pubmed:grant | |
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cell Surface,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cytoplasmic and Nuclear,
http://linkedlifedata.com/resource/pubmed/chemical/alpha-L-Fucosidase,
http://linkedlifedata.com/resource/pubmed/chemical/cation-dependent...
|
pubmed:status |
MEDLINE
|
pubmed:month |
Feb
|
pubmed:issn |
0282-0080
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:volume |
9
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
56-62
|
pubmed:dateRevised |
2008-8-22
|
pubmed:meshHeading |
pubmed-meshheading:1327338-B-Lymphocytes,
pubmed-meshheading:1327338-Carrier Proteins,
pubmed-meshheading:1327338-Cell Line,
pubmed-meshheading:1327338-Cell Membrane,
pubmed-meshheading:1327338-Humans,
pubmed-meshheading:1327338-Immunoassay,
pubmed-meshheading:1327338-Mucolipidoses,
pubmed-meshheading:1327338-Receptors, Cell Surface,
pubmed-meshheading:1327338-Receptors, Cytoplasmic and Nuclear,
pubmed-meshheading:1327338-Reference Values,
pubmed-meshheading:1327338-alpha-L-Fucosidase
|
pubmed:year |
1992
|
pubmed:articleTitle |
Binding receptors for alpha-L-fucosidase in human B-lymphoid cell lines.
|
pubmed:affiliation |
Department of Gynaecologic Oncology, Roswell Park Cancer Institute, Buffalo, NY 14263.
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
|