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Transthyretin interacts with the lysosome-associated membrane protein (LAMP-1) in circulation
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| Zeitschriftentitel: | Biochemical Journal |
|---|---|
| Personen und Körperschaften: | , , , , , , |
| In: | Biochemical Journal, 382, 2004, 2, S. 481-489 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
Portland Press Ltd.
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| Schlagwörter: |
| author_facet |
CHANG, Melissa H. Y. HUA, Chi T. ISAAC, Elizabeth L. LITJENS, Tom HODGE, Greg KARAGEORGOS, Litsa E. MEIKLE, Peter J. CHANG, Melissa H. Y. HUA, Chi T. ISAAC, Elizabeth L. LITJENS, Tom HODGE, Greg KARAGEORGOS, Litsa E. MEIKLE, Peter J. |
|---|---|
| author |
CHANG, Melissa H. Y. HUA, Chi T. ISAAC, Elizabeth L. LITJENS, Tom HODGE, Greg KARAGEORGOS, Litsa E. MEIKLE, Peter J. |
| spellingShingle |
CHANG, Melissa H. Y. HUA, Chi T. ISAAC, Elizabeth L. LITJENS, Tom HODGE, Greg KARAGEORGOS, Litsa E. MEIKLE, Peter J. Biochemical Journal Transthyretin interacts with the lysosome-associated membrane protein (LAMP-1) in circulation Cell Biology Molecular Biology Biochemistry |
| author_sort |
chang, melissa h. y. |
| spelling |
CHANG, Melissa H. Y. HUA, Chi T. ISAAC, Elizabeth L. LITJENS, Tom HODGE, Greg KARAGEORGOS, Litsa E. MEIKLE, Peter J. 0264-6021 1470-8728 Portland Press Ltd. Cell Biology Molecular Biology Biochemistry http://dx.doi.org/10.1042/bj20031752 <jats:p>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.</jats:p> Transthyretin interacts with the lysosome-associated membrane protein (LAMP-1) in circulation Biochemical Journal |
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| title |
Transthyretin interacts with the lysosome-associated membrane protein (LAMP-1) in circulation |
| title_unstemmed |
Transthyretin interacts with the lysosome-associated membrane protein (LAMP-1) in circulation |
| title_full |
Transthyretin interacts with the lysosome-associated membrane protein (LAMP-1) in circulation |
| title_fullStr |
Transthyretin interacts with the lysosome-associated membrane protein (LAMP-1) in circulation |
| title_full_unstemmed |
Transthyretin interacts with the lysosome-associated membrane protein (LAMP-1) in circulation |
| title_short |
Transthyretin interacts with the lysosome-associated membrane protein (LAMP-1) in circulation |
| title_sort |
transthyretin interacts with the lysosome-associated membrane protein (lamp-1) in circulation |
| topic |
Cell Biology Molecular Biology Biochemistry |
| url |
http://dx.doi.org/10.1042/bj20031752 |
| publishDate |
2004 |
| physical |
481-489 |
| description |
<jats:p>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.</jats:p> |
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| author | CHANG, Melissa H. Y., HUA, Chi T., ISAAC, Elizabeth L., LITJENS, Tom, HODGE, Greg, KARAGEORGOS, Litsa E., MEIKLE, Peter J. |
| author_facet | CHANG, Melissa H. Y., HUA, Chi T., ISAAC, Elizabeth L., LITJENS, Tom, HODGE, Greg, KARAGEORGOS, Litsa E., MEIKLE, Peter J., CHANG, Melissa H. Y., HUA, Chi T., ISAAC, Elizabeth L., LITJENS, Tom, HODGE, Greg, KARAGEORGOS, Litsa E., MEIKLE, Peter J. |
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| description | <jats:p>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.</jats:p> |
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| imprint_str_mv | Portland Press Ltd., 2004 |
| institution | DE-Ch1, DE-L229, DE-D275, DE-Bn3, DE-Brt1, DE-Zwi2, DE-D161, DE-Gla1, DE-Zi4, DE-15, DE-Rs1, DE-Pl11, DE-105, DE-14 |
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| spelling | CHANG, Melissa H. Y. HUA, Chi T. ISAAC, Elizabeth L. LITJENS, Tom HODGE, Greg KARAGEORGOS, Litsa E. MEIKLE, Peter J. 0264-6021 1470-8728 Portland Press Ltd. Cell Biology Molecular Biology Biochemistry http://dx.doi.org/10.1042/bj20031752 <jats:p>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.</jats:p> Transthyretin interacts with the lysosome-associated membrane protein (LAMP-1) in circulation Biochemical Journal |
| spellingShingle | CHANG, Melissa H. Y., HUA, Chi T., ISAAC, Elizabeth L., LITJENS, Tom, HODGE, Greg, KARAGEORGOS, Litsa E., MEIKLE, Peter J., Biochemical Journal, Transthyretin interacts with the lysosome-associated membrane protein (LAMP-1) in circulation, Cell Biology, Molecular Biology, Biochemistry |
| title | Transthyretin interacts with the lysosome-associated membrane protein (LAMP-1) in circulation |
| title_full | Transthyretin interacts with the lysosome-associated membrane protein (LAMP-1) in circulation |
| title_fullStr | Transthyretin interacts with the lysosome-associated membrane protein (LAMP-1) in circulation |
| title_full_unstemmed | Transthyretin interacts with the lysosome-associated membrane protein (LAMP-1) in circulation |
| title_short | Transthyretin interacts with the lysosome-associated membrane protein (LAMP-1) in circulation |
| title_sort | transthyretin interacts with the lysosome-associated membrane protein (lamp-1) in circulation |
| title_unstemmed | Transthyretin interacts with the lysosome-associated membrane protein (LAMP-1) in circulation |
| topic | Cell Biology, Molecular Biology, Biochemistry |
| url | http://dx.doi.org/10.1042/bj20031752 |