Uptake by neuroblastoma cells of glucosylceramide, glucosylceramide glucosidase, its stimulator protein, and phosphatidylserine
dc.contributor.author | Datta, Subhash C. | en_US |
dc.contributor.author | Snider, R. Michael | en_US |
dc.contributor.author | Radin, Norman S. | en_US |
dc.date.accessioned | 2006-04-07T19:28:25Z | |
dc.date.available | 2006-04-07T19:28:25Z | |
dc.date.issued | 1986-07-18 | en_US |
dc.identifier.citation | Datta, Subhash C., Snider, R. Michael, Radin, Norman S. (1986/07/18)."Uptake by neuroblastoma cells of glucosylceramide, glucosylceramide glucosidase, its stimulator protein, and phosphatidylserine." Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism 877(3): 387-398. <http://hdl.handle.net/2027.42/26097> | en_US |
dc.identifier.uri | http://www.sciencedirect.com/science/article/B6T1X-47F7DT6-D9/2/7130575f55b9bf5cdb40d2427d32dee7 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/26097 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=3730407&dopt=citation | en_US |
dc.description.abstract | Serum-free cultured neuroblastoma cells (clone NIE-115) have been shown to absorb emulsified glucosylceramide, glucosylceramide glucosidase, an activator protein for the enzyme, and phosphatidylserine from a synthetic medium. Uptake of the enzyme was augmented by phosphatidylserine, and vice versa. Uptake of the enzyme-lipid complex was further augmented by the activator protein. It appears likely that the activator forms a complex only with the enzyme-lipid complex, not with the individual components. Two uptake mechanisms for the enzyme seem to be involved, one of which (the complex with activator proteins and acidic lipid) is sensitive to mannosyl phosphate groups. Hydrolysis of absorbed glucosylceramide was slow unless the medium was supplemented with the acidic phospholipid or glucosidase. The most rapid disappearance of stored glycolipid took place when the ternary mixture was added to the cell medium, enzyme + activator protein + phosphatidylserine. These findings may be relevant to enzyme replacement therapy for Gaucher disease. | en_US |
dc.format.extent | 1115557 bytes | |
dc.format.extent | 3118 bytes | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | text/plain | |
dc.language.iso | en_US | |
dc.publisher | Elsevier | en_US |
dc.title | Uptake by neuroblastoma cells of glucosylceramide, glucosylceramide glucosidase, its stimulator protein, and phosphatidylserine | en_US |
dc.type | Article | en_US |
dc.rights.robots | IndexNoFollow | en_US |
dc.subject.hlbsecondlevel | Materials Science and Engineering | en_US |
dc.subject.hlbsecondlevel | Chemistry | en_US |
dc.subject.hlbsecondlevel | Chemical Engineering | en_US |
dc.subject.hlbtoplevel | Science | en_US |
dc.subject.hlbtoplevel | Engineering | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | Mental Health Research Institute, University of Michigan, Ann Arbor, MI 48109, U.S.A. | en_US |
dc.contributor.affiliationum | Mental Health Research Institute, University of Michigan, Ann Arbor, MI 48109, U.S.A. | en_US |
dc.contributor.affiliationum | Mental Health Research Institute, University of Michigan, Ann Arbor, MI 48109, U.S.A. | en_US |
dc.identifier.pmid | 3730407 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/26097/1/0000173.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1016/0005-2760(86)90204-3 | en_US |
dc.identifier.source | Biochimica et Biophysica Acta | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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