The role of tumor necrosis factor alpha in the pathophysiology of human multiple myeloma: therapeutic applications. Hideshima, T., Chauhan, D., Schlossman, R., Richardson, P., & Anderson, K., C. Oncogene, 20(33):4519-27, Nature Publishing Group, 7, 2001.
The role of tumor necrosis factor alpha in the pathophysiology of human multiple myeloma: therapeutic applications. [link]Website  abstract   bibtex   
In this study we demonstrate that tumor necrosis factor alpha (TNFalpha) triggers only modest proliferation, as well as p44/p42 mitogen-activated protein kinase (MAPK) and NF-kappaB activation, in MM.1S multiple myeloma (MM) cells. TNFalpha also activates NF-kappaB and markedly upregulates (fivefold) secretion of interleukin-6 (IL-6), a myeloma growth and survival factor, in bone marrow stromal cells (BMSCs). TNFalpha in both a dose and time dependent fashion induced expression of CD11a (LFA-1), CD54 (intercellular adhesion molecule-1, ICAM-1), CD106 (vascular cell adhesion molecule-1, VCAM-1), CD49d (very late activating antigen-4, VLA-4), and/or MUC-1 on MM cell lines; as well as CD106 (VCAM-1) and CD54 (ICAM-1) expression on BMSCs. This resulted in increased (2-4-fold) per cent specific binding of MM cells to BMSCs, with related IL-6 secretion. Importantly, the proteasome inhibitor PS-341 abrogated TNFalpha-induced NF-kappaB activation, induction of ICAM-1 or VCAM-1, and increased adhesion of MM cells to BMSCs. Agents which act to inhibit TNFalpha may therefore abrogate the paracrine growth and survival advantage conferred by MM cell adhesion in the BM microenvironment.
@article{
 title = {The role of tumor necrosis factor alpha in the pathophysiology of human multiple myeloma: therapeutic applications.},
 type = {article},
 year = {2001},
 identifiers = {[object Object]},
 keywords = {Antigens, CD,Antigens, CD: biosynthesis,Antigens, CD: genetics,Bone Marrow Cells,Bone Marrow Cells: cytology,Bone Marrow Cells: metabolism,Bone Marrow Cells: secretion,Boronic Acids,Boronic Acids: pharmacology,Cell Adhesion,Cell Division,Cell Division: drug effects,Cysteine Endopeptidases,Gene Expression Regulation, Neoplastic,Gene Expression Regulation, Neoplastic: drug effec,Humans,Integrin alpha4,Intercellular Adhesion Molecule-1,Intercellular Adhesion Molecule-1: biosynthesis,Intercellular Adhesion Molecule-1: genetics,Interleukin-6,Interleukin-6: secretion,Lymphocyte Function-Associated Antigen-1,Lymphocyte Function-Associated Antigen-1: biosynth,Lymphocyte Function-Associated Antigen-1: genetics,MAP Kinase Signaling System,MAP Kinase Signaling System: drug effects,Mitogen-Activated Protein Kinase 1,Mitogen-Activated Protein Kinase 1: biosynthesis,Mitogen-Activated Protein Kinase 1: genetics,Mitogen-Activated Protein Kinase 3,Mitogen-Activated Protein Kinases,Mitogen-Activated Protein Kinases: biosynthesis,Mitogen-Activated Protein Kinases: genetics,Models, Biological,Mucin-1,Mucin-1: biosynthesis,Mucin-1: genetics,Multienzyme Complexes,Multienzyme Complexes: antagonists & inhibitors,Multiple Myeloma,Multiple Myeloma: genetics,Multiple Myeloma: pathology,Multiple Myeloma: physiopathology,NF-kappa B,NF-kappa B: physiology,Neoplasm Proteins,Neoplasm Proteins: biosynthesis,Neoplasm Proteins: genetics,Neoplasm Proteins: physiology,Protease Inhibitors,Protease Inhibitors: pharmacology,Proteasome Endopeptidase Complex,Pyrazines,Pyrazines: pharmacology,Stromal Cells,Stromal Cells: cytology,Stromal Cells: metabolism,Stromal Cells: secretion,Tumor Cells, Cultured,Tumor Cells, Cultured: metabolism,Tumor Cells, Cultured: pathology,Tumor Necrosis Factor-alpha,Tumor Necrosis Factor-alpha: physiology,Vascular Cell Adhesion Molecule-1,Vascular Cell Adhesion Molecule-1: biosynthesis,Vascular Cell Adhesion Molecule-1: genetics},
 pages = {4519-27},
 volume = {20},
 websites = {http://www.nature.com/onc/journal/v20/n33/full/1204623a.html},
 month = {7},
 publisher = {Nature Publishing Group},
 day = {27},
 id = {36826c71-c6f4-3634-be8d-673dff62c57d},
 created = {2016-06-24T20:49:19.000Z},
 accessed = {2015-02-09},
 file_attached = {false},
 profile_id = {954a987f-819f-3985-95a4-2991e0cf0552},
 group_id = {8440dcff-74cc-3783-aef7-fe2749cfc7ef},
 last_modified = {2016-06-24T20:49:19.000Z},
 read = {false},
 starred = {false},
 authored = {false},
 confirmed = {true},
 hidden = {false},
 citation_key = {Hideshima2001},
 language = {en},
 abstract = {In this study we demonstrate that tumor necrosis factor alpha (TNFalpha) triggers only modest proliferation, as well as p44/p42 mitogen-activated protein kinase (MAPK) and NF-kappaB activation, in MM.1S multiple myeloma (MM) cells. TNFalpha also activates NF-kappaB and markedly upregulates (fivefold) secretion of interleukin-6 (IL-6), a myeloma growth and survival factor, in bone marrow stromal cells (BMSCs). TNFalpha in both a dose and time dependent fashion induced expression of CD11a (LFA-1), CD54 (intercellular adhesion molecule-1, ICAM-1), CD106 (vascular cell adhesion molecule-1, VCAM-1), CD49d (very late activating antigen-4, VLA-4), and/or MUC-1 on MM cell lines; as well as CD106 (VCAM-1) and CD54 (ICAM-1) expression on BMSCs. This resulted in increased (2-4-fold) per cent specific binding of MM cells to BMSCs, with related IL-6 secretion. Importantly, the proteasome inhibitor PS-341 abrogated TNFalpha-induced NF-kappaB activation, induction of ICAM-1 or VCAM-1, and increased adhesion of MM cells to BMSCs. Agents which act to inhibit TNFalpha may therefore abrogate the paracrine growth and survival advantage conferred by MM cell adhesion in the BM microenvironment.},
 bibtype = {article},
 author = {Hideshima, T and Chauhan, D and Schlossman, R and Richardson, P and Anderson, K C},
 journal = {Oncogene},
 number = {33}
}
Downloads: 0
About
Documentation
Keywords
Search
Users
Terms and Conditions of Use
Privacy Policy
Sitemap
© BibBase.org 2021