| Differential effects between amphoterin and advanced glycation end products on colon cancer cells. | |
| | |
MedLine Citation:
|
PMID: 12640679 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
|
Amphoterin is 1 ligand of the receptor for advanced glycation end products (RAGE). We studied expression of amphoterin and RAGE mRNA and proteins in colorectal carcinoma cells and investigated their associations with the invasive activities of cells exposed to advanced glycation end products (AGE). Expression of RAGE and amphoterin was examined in 4 colorectal carcinoma cell lines. All cell lines expressed both RAGE and amphoterin. The effects of RAGE and amphoterin on cell growth (MTT assay), migration (wound healing assay) and invasion (in vitro invasion assay) were tested by treatment of cells with RAGE and amphoterin antisense S-oligodeoxynucleotides (ODNs). Cell growth, migration and invasion were inhibited significantly in Colo320 and WiDr carcinoma cells treated with RAGE and amphoterin antisense S-ODNs compared with sense-treated cells. Differences in ligand activity between amphoterin and AGE were examined with AGE-bovine serum albumin (BSA). AGE-BSA decreased cell growth, migration and invasion of amphoterin antisense S-ODN-treated Colo320 and WiDr cells compared with those of cells treated with Colo320 conditioned medium. Phosphorylation of extracellular signal-regulated kinase-1/2, Rac1 and AKT and production of matrix metalloproteinase 9 were increased to a greater degree by amphoterin than by AGE-BSA. In contrast, production of inducible nitric oxide synthase and nuclear factor-kappaBp65 were increased to a greater degree by AGE-BSA than by amphoterin. |
| | |
Authors:
|
Hiroki Kuniyasu; Yoshitomo Chihara; Hideaki Kondo |
Related Documents
:
|
21352549 - Identification of a sub-population of b cells that proliferates after infection with ep... 12618009 - Using cell transplantation to investigate genes involved in aging. 2430819 - The in vitro lifespan of mrc-5 cells is shortened by 5-azacytidine-induced demethylation. 20647039 - Pathophysiology of vascular calcification: pivotal role of cellular senescence in vascu... 12645879 - Origin of late-onset autoimmune disease. 17697939 - Partial uncoupling of oxidative phosphorylation induces premature senescence in human f... 18728729 - Effects of in vitro brevetoxin exposure on apoptosis and cellular metabolism in a leuke... 14500569 - Thiocyanate induces cell necrosis and fibrosis in selenium- and iodine-deficient rat th... 20422129 - Dioscorin protects tight junction protein expression in a549 human airway epithelium ce... |
Publication Detail:
|
Type: Comparative Study; Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
|
Title: International journal of cancer. Journal international du cancer Volume: 104 ISSN: 0020-7136 ISO Abbreviation: Int. J. Cancer Publication Date: 2003 May |
Date Detail:
|
Created Date: 2003-03-17 Completed Date: 2003-05-12 Revised Date: 2011-10-27 |
Medline Journal Info:
|
Nlm Unique ID: 0042124 Medline TA: Int J Cancer Country: United States |
Other Details:
|
Languages: eng Pagination: 722-7 Citation Subset: IM |
Copyright Information:
|
Copyright 2003 Wiley-Liss, Inc. |
Affiliation:
|
Department of Oncological Pathology, Cancer Center, Nara Medical University, Kashihara, Japan. cooninh@zb4.so-net.ne.jp |
Export Citation:
|
APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
|
Animals Cattle Cell Division / drug effects Cell Movement / drug effects Colorectal Neoplasms / metabolism*, pathology Glycosylation End Products, Advanced / genetics*, metabolism, pharmacology HMGB1 Protein / genetics*, metabolism, pharmacology Humans Immunoblotting Ligands Matrix Metalloproteinase 9 / metabolism Mitogen-Activated Protein Kinase 1 / metabolism Mitogen-Activated Protein Kinase 3 Mitogen-Activated Protein Kinases / metabolism NF-kappa B / metabolism Neoplasm Invasiveness Nitric Oxide Synthase / metabolism Nitric Oxide Synthase Type II Oligodeoxyribonucleotides, Antisense / pharmacology* Phosphorylation Polymerase Chain Reaction Protein-Serine-Threonine Kinases* Proto-Oncogene Proteins / metabolism Proto-Oncogene Proteins c-akt RNA, Messenger / metabolism Receptors, Immunologic / genetics*, metabolism Serum Albumin, Bovine / genetics*, metabolism, pharmacology Tumor Cells, Cultured Wound Healing rac1 GTP-Binding Protein / metabolism |
| Chemical | |
Reg. No./Substance:
|
0/Glycosylation End Products, Advanced; 0/HMGB1 Protein; 0/Ligands; 0/NF-kappa B; 0/Oligodeoxyribonucleotides, Antisense; 0/Proto-Oncogene Proteins; 0/RNA, Messenger; 0/Receptors, Immunologic; 0/Serum Albumin, Bovine; 0/advanced glycation end products-bovine serum albumin; 0/advanced glycosylation end-product receptor; EC 1.14.13.39/NOS2 protein, human; EC 1.14.13.39/Nitric Oxide Synthase; EC 1.14.13.39/Nitric Oxide Synthase Type II; EC 2.7.1.37/AKT1 protein, human; EC 2.7.11.1/Protein-Serine-Threonine Kinases; EC 2.7.11.1/Proto-Oncogene Proteins c-akt; EC 2.7.11.24/Mitogen-Activated Protein Kinase 1; EC 2.7.11.24/Mitogen-Activated Protein Kinase 3; EC 2.7.11.24/Mitogen-Activated Protein Kinases; EC 3.4.24.35/Matrix Metalloproteinase 9; EC 3.6.5.2/rac1 GTP-Binding Protein |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
Previous Document: Suppression of EGFRvIII-mediated proliferation and tumorigenesis of breast cancer cells by ribozyme.
Next Document: Immunohistochemical analysis of p16INK4a, p14ARF, p18INK4c, p21CIP1, p27KIP1 and p73 expression in 2...