Free Ig light chains interact with sphingomyelin and are found on the surface of myeloma plasma cells in an aggregated form
Free κ L chains (FκLCs) are expressed on the surface of myeloma cells and are being assessed as a therapeutic target for the treatment of multiple myeloma. Despite its clinical potential, the mechanism by which FκLCs interact with membranes remains unresolved. In this study, we show that FκLCs assoc...
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| Published in | The Journal of immunology (1950) Vol. 185; no. 7; pp. 4179 - 4188 |
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| Main Authors | , , , , , , , , , |
| Format | Journal Article |
| Language | English |
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United States
01.10.2010
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| Abstract | Free κ L chains (FκLCs) are expressed on the surface of myeloma cells and are being assessed as a therapeutic target for the treatment of multiple myeloma. Despite its clinical potential, the mechanism by which FκLCs interact with membranes remains unresolved. In this study, we show that FκLCs associate with sphingomyelin on the plasma membrane of myeloma cells. Moreover, membrane-bound FκLCs are aggregated, suggesting that aggregation is required for intercalation with membranes. Finally, we propose a model where the binding of FκLCs with sphingomyelin on secretory vesicle membranes is stabilized by self-aggregation, with aggregated FκLCs exposed on the plasma membrane after exocytosis. Although it is well known that protein aggregates bind membranes, this is only the second example of an aggregate being found on the surface of cells that also secrete the protein in its native form. We postulate that many other aggregation-prone proteins may associate with cell membranes by similar mechanisms. |
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| AbstractList | Free κ L chains (FκLCs) are expressed on the surface of myeloma cells and are being assessed as a therapeutic target for the treatment of multiple myeloma. Despite its clinical potential, the mechanism by which FκLCs interact with membranes remains unresolved. In this study, we show that FκLCs associate with sphingomyelin on the plasma membrane of myeloma cells. Moreover, membrane-bound FκLCs are aggregated, suggesting that aggregation is required for intercalation with membranes. Finally, we propose a model where the binding of FκLCs with sphingomyelin on secretory vesicle membranes is stabilized by self-aggregation, with aggregated FκLCs exposed on the plasma membrane after exocytosis. Although it is well known that protein aggregates bind membranes, this is only the second example of an aggregate being found on the surface of cells that also secrete the protein in its native form. We postulate that many other aggregation-prone proteins may associate with cell membranes by similar mechanisms. Free L chains (FLCs) are expressed on the surface of myeloma cells and are being assessed as a therapeutic target for the treatment of multiple myeloma. Despite its clinical potential, the mechanism by which FLCs interact with membranes remains unresolved. In this study, we show that FLCs associate with sphingomyelin on the plasma membrane of myeloma cells. Moreover, membrane-bound FLCs are aggregated, suggesting that aggregation is required for intercalation with membranes. Finally, we propose a model where the binding of FLCs with sphingomyelin on secretory vesicle membranes is stabilized by self-aggregation, with aggregated FLCs exposed on the plasma membrane after exocytosis. Although it is well known that protein aggregates bind membranes, this is only the second example of an aggregate being found on the surface of cells that also secrete the protein in its native form. We postulate that many other aggregation-prone proteins may associate with cell membranes by similar mechanisms. |
| Author | Yuriev, Elizabeth Hutchinson, Andrew T Agostino, Mark Bockhorni, Vanessa Raison, Robert L Lund, Maria E Edmundson, Allen B Ramsland, Paul A Jones, Darren R Jennings, Cameron V |
| Author_xml | – sequence: 1 givenname: Andrew T surname: Hutchinson fullname: Hutchinson, Andrew T email: andrew.hutchinson@uts.edu.au organization: Department of Medical and Molecular Biosciences, University of Technology Sydney, Ultimo, New South Wales, Australia. andrew.hutchinson@uts.edu.au – sequence: 2 givenname: Paul A surname: Ramsland fullname: Ramsland, Paul A – sequence: 3 givenname: Darren R surname: Jones fullname: Jones, Darren R – sequence: 4 givenname: Mark surname: Agostino fullname: Agostino, Mark – sequence: 5 givenname: Maria E surname: Lund fullname: Lund, Maria E – sequence: 6 givenname: Cameron V surname: Jennings fullname: Jennings, Cameron V – sequence: 7 givenname: Vanessa surname: Bockhorni fullname: Bockhorni, Vanessa – sequence: 8 givenname: Elizabeth surname: Yuriev fullname: Yuriev, Elizabeth – sequence: 9 givenname: Allen B surname: Edmundson fullname: Edmundson, Allen B – sequence: 10 givenname: Robert L surname: Raison fullname: Raison, Robert L |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/20817866$$D View this record in MEDLINE/PubMed |
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| Snippet | Free κ L chains (FκLCs) are expressed on the surface of myeloma cells and are being assessed as a therapeutic target for the treatment of multiple myeloma.... Free L chains (FLCs) are expressed on the surface of myeloma cells and are being assessed as a therapeutic target for the treatment of multiple myeloma.... |
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| SubjectTerms | Blotting, Western Cell Line, Tumor Cell Membrane - chemistry Cell Membrane - immunology Cell Membrane - metabolism Cell Separation Electrophoresis, Polyacrylamide Gel Enzyme-Linked Immunosorbent Assay Flow Cytometry Humans Immunoglobulin Light Chains - metabolism Multiple Myeloma - metabolism Multiple Myeloma - pathology Multiprotein Complexes Plasma Cells - metabolism Plasma Cells - pathology Receptor Aggregation - physiology Sphingomyelins - metabolism Transfection |
| Title | Free Ig light chains interact with sphingomyelin and are found on the surface of myeloma plasma cells in an aggregated form |
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