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   <subfield code="a">Binding receptors for α- l -fucosidase in human B-lymphoid cell lines</subfield>
   <subfield code="h">[Elektronische Daten]</subfield>
   <subfield code="c">[Richard Dicioccio, Arnold Miller]</subfield>
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   <subfield code="a">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 α-l-fucosidase in lymphoid cells. The binding of α-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 α-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.</subfield>
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   <subfield code="a">Chapman and Hall, 1992</subfield>
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   <subfield code="a">α- l -Fucosidase</subfield>
   <subfield code="2">nationallicence</subfield>
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   <subfield code="a">phosphomannosyl receptors</subfield>
   <subfield code="2">nationallicence</subfield>
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   <subfield code="a">B-lymphoid cells</subfield>
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   <subfield code="a">Dicioccio</subfield>
   <subfield code="D">Richard</subfield>
   <subfield code="u">Department of Gynaecologic Oncology, Roswell Park Cancer Institute, 14263, Buffalo, NY, USA</subfield>
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   <subfield code="u">Department of Neurosciences, M-024, University of California, San Diego, School of Medicine, 90093, La Jolla, CA, USA</subfield>
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   <subfield code="t">Glycoconjugate Journal</subfield>
   <subfield code="d">Kluwer Academic Publishers</subfield>
   <subfield code="g">9/1(1992-02-01), 56-62</subfield>
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   <subfield code="q">9:1&lt;56</subfield>
   <subfield code="1">1992</subfield>
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   <subfield code="t">Glycoconjugate Journal</subfield>
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   <subfield code="a">Metadata rights reserved</subfield>
   <subfield code="b">Springer special CC-BY-NC licence</subfield>
   <subfield code="2">nationallicence</subfield>
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