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https://hdl.handle.net/2440/7704
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dc.contributor.author | Meikle, P. | - |
dc.contributor.author | Yan, M. | - |
dc.contributor.author | Ravenscroft, E. | - |
dc.contributor.author | Isaac, E. | - |
dc.contributor.author | Hopwood, J. | - |
dc.contributor.author | Brooks, D. | - |
dc.date.issued | 1999 | - |
dc.identifier.citation | Molecular Genetics and Metabolism, 1999; 66(3):179-188 | - |
dc.identifier.issn | 1096-7192 | - |
dc.identifier.issn | 1096-7206 | - |
dc.identifier.uri | http://hdl.handle.net/2440/7704 | - |
dc.description.abstract | The lysosome-associated membrane protein (LAMP-1) is elevated in the cells and plasma from lysosomal storage disorder-affected individuals; however, the mechanism of this elevation is not well defined. In this study we have investigated the synthesis, glycoprocessing, trafficking, and turnover of LAMP-1 in human skin fibroblasts from Pompe disease patients and control individuals. There were similar levels of LAMP-1 synthesis in both cell types, but glycoprocessing was retarded in Pompe (T1/2 = 25 min) compared to control (T1/2 = 17 min) fibroblasts. There was also a marked delay in trafficking of LAMP-1 to lysosomes of Pompe (T1/2 = 200 min) compared to control (T1/2 = 100 min) cells. A proportion of newly synthesized LAMP-1 (5.4% in Pompe and 8.5% in controls) was trafficked out of the cell (T1/2 = 3.5 h in controls) and, although significantly smaller than the lysosomal form, still had a transmembrane domain and cytoplasmic tail. In contrast, a soluble lysosomal pool of LAMP-1 had no tail sequence, suggesting that it had been clipped from the membrane. In turnover studies, LAMP-1 was more stable in Pompe (T1/2 = 4.9 days) compared to control (T1/2 = 1. 6 days) cells, implying either reduced proteolysis or lysosomal function, in Pompe cells. These results indicate altered traffic and turnover of LAMP-1 in storage disorders and identify different intracellular and extracellular pools of soluble LAMP-1, suggesting alternative trafficking pathways. | - |
dc.language.iso | en | - |
dc.publisher | ACADEMIC PRESS INC | - |
dc.source.uri | http://dx.doi.org/10.1006/mgme.1998.2800 | - |
dc.subject | Cell Line | - |
dc.subject | Lysosomes | - |
dc.subject | Fibroblasts | - |
dc.subject | Skin | - |
dc.subject | Humans | - |
dc.subject | Glycogen Storage Disease Type II | - |
dc.subject | Membrane Glycoproteins | - |
dc.subject | Antigens, CD | - |
dc.subject | Amino Acid Sequence | - |
dc.subject | Biological Transport | - |
dc.subject | Molecular Sequence Data | - |
dc.subject | Lysosome-Associated Membrane Glycoproteins | - |
dc.title | Altered trafficking and turnover of LAMP-1 in Pompe disease-affected cells | - |
dc.type | Journal article | - |
dc.identifier.doi | 10.1006/mgme.1998.2800 | - |
pubs.publication-status | Published | - |
dc.identifier.orcid | Brooks, D. [0000-0001-9098-3626] | - |
Appears in Collections: | Aurora harvest 4 Paediatrics publications |
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