title: Differentially expressed proteins in nitric oxide-stimulated NIH/3T3 fibroblasts: implications for inhibiting cancer development.
abstract: OBJECTIVE
  Recent evidence shows that nitric oxide (NO) may exhibit both pro-cancer and anti-cancer activities. The present study aimed to determine the differentially expressed proteins in NO-treated NIH/3T3 fibroblasts in order to investigate whether NO induces proteins with pro-cancer or anti-cancer effects.
  
  
  METHODS
  The cells were treated with 300 μM of an NO donor 3,3-bis-(aminoethyl)-1-hydroxy-2-oxo-1-triazene (NOC-18) for 12 h. The changed protein patterns, which were separated by two-dimensional electrophoresis using pH gradients of 4-7, were conclusively identified by matrix-assisted laser desorption/ionization-time of flight mass spectrometry (MALDI-TOF MS) analysis of the peptide digests.
  
  
  RESULTS
  Seventeen differentially expressed proteins were identified in NOC-18-treated cells. Nine proteins [vinculin protein, keratin 19, ubiquitous tropomodulin, F-actin capping protein (α1 subunit), tropomyosin 3, 26S proteasome-associated pad1 homolog, T-complex protein 1 (ε subunit) N(G)-dimethylarginine dimethylaminohydrolase, and heat shock protein 90] were increased and eight proteins (heat shock protein 70, glucosidase II, lamin B1, calreticulin, nucleophosmin 1, microtubule-associated protein retinitis pigmentosa/end binding family member 1, 150 kD oxygen-regulated protein precursor, and heat shock 70-related protein albino or pale green 2) were decreased by NOC-18 in the cells. Thirteen proteins are related to the suppression of cancer cell proliferation, invasion, and metastasis while two proteins (heat shock protein 90 and N(G)-dimethylarginine dimethylaminohydrolase) are related to carcinogenesis. The functions of 150 kD oxygen-regulated protein precursor and T-complex protein 1 (ε subunit) are unknown in relation to carcinogenesis.
  
  
  CONCLUSIONS
  Most proteins differentially expressed by NOC-18 are involved in inhibiting cancer development.
authors: Department of Pharmacology, College of Medicine, Yonsei University, Seoul, Korea.
authors: Dong Hwi
authors: DH
authors: Shim
authors: Department of Food and Nutrition, Brain Korea 21 PLUS Project, College of Human Ecology, Yonsei University, Seoul, Korea. jwlim11@yonsei.ac.kr.
authors: Joo Weon
authors: JW
authors: Lim
authors: Department of Pharmacology, College of Medicine, Yonsei University, Seoul, Korea.; Department of Food and Nutrition, Brain Korea 21 PLUS Project, College of Human Ecology, Yonsei University, Seoul, Korea. kim626@yonsei.ac.kr.
authors: Hyeyoung
authors: H
authors: Kim
mesh_terms: D000818:Animals; D015180:Electrophoresis, Gel, Two-Dimensional / Q000379:methods*; D005347:Fibroblasts / Q000378:metabolism* / Q000473:pathology; D018840:HSP70 Heat-Shock Proteins; D006801:Humans; D051379:Mice; D041681:NIH 3T3 Cells; D009369:Neoplasms / Q000378:metabolism* / Q000473:pathology; D020030:Nitric Oxide Donors; D009603:Nitroso Compounds; D000090243:Nucleophosmin; D011506:Proteins / Q000032:analysis / Q000378:metabolism*; D040901:Proteomics / Q000379:methods*; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
chemical_list: D018840:HSP70 Heat-Shock Proteins; C093285:NOC 18; D020030:Nitric Oxide Donors; D009603:Nitroso Compounds; C000715570:Npm1 protein, mouse; D011506:Proteins; C050087:oxygen-regulated proteins; D000090243:Nucleophosmin
keywords: NIH/3T3 cells; Nitric oxide; cancer; proteomic analysis