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https://hdl.handle.net/2440/7012
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Type: | Journal article |
Title: | Transthyretin interacts with the lysosome-associated membrane protein (LAMP-1) in circulation |
Author: | Chang, M. Hua, C. Isaac, E. Litjens, T. Hodge, G. Karageorgos, L. Meikle, P. |
Citation: | Biochemical Journal, 2004; 382(2):481-489 |
Publisher: | Portland Press |
Issue Date: | 2004 |
ISSN: | 0264-6021 1470-8728 |
Abstract: | LAMP-1 (lysosome-associated membrane protein), a major glycoprotein present in the lysosomal membrane, constitutes up to 50% of total membrane proteins. LAMP-1, expressed at the plasma membrane, is reported to be the major molecule expressing the sialyl-Lewis X antigen. Two forms of LAMP-1 exist; the full-length LAMP-1 [LAMP-1 (+Tail)] has a highly glycosylated lumenal domain, a membrane-spanning domain and a short cytoplasmic tail, and the truncated LAMP-1 [LAMP-1 (-Tail)] contains only the lumenal domain. Soluble LAMP-1 (+/-Tail) has been reported in circulation. LAMP-1 at the cell surface has been shown to interact with E-selectin and galectin and is proposed to function in cell-cell interactions. However, the functional role(s) of soluble LAMP-1 in circulation is unclear. To investigate the functional role of soluble LAMP-1 in circulation, recombinant LAMP-1 (-Tail) and LAMP-1 (+Tail) were produced in HT1080 cells. Two immune-quantification assays were developed to distinguish between the LAMP-1 forms. The interaction and aggregation properties of the different LAMP-1 forms were investigated using the immune-quantification assays. Only LAMP-1 (+Tail) was found to aggregate and interact with plasma proteins. Plasma proteins that interact with LAMP-1 were isolated by affinity chromatography with either the recombinant LAMP-1 (-Tail) or a synthesized peptide consisting of the 14 amino acids of the LAMP-1 cytoplasmic tail. Transthyretin was found to interact with the cytoplasmic tail of LAMP-1. Transthyretin exists as a homotetramer in plasma, as such may play a role in the aggregation of LAMP-1 in circulation. |
Keywords: | Cell Line, Tumor Humans Fibrosarcoma Cholic Acids Prealbumin Blood Proteins Protein Isoforms Recombinant Proteins Antigens, CD Gene Expression Regulation, Neoplastic Alternative Splicing Lysosome-Associated Membrane Glycoproteins |
DOI: | 10.1042/BJ20031752 |
Published version: | http://dx.doi.org/10.1042/bj20031752 |
Appears in Collections: | Aurora harvest Paediatrics publications |
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