Heme oxygenase-l (HO-l) exhibits cyt oprotective effects in many different cell types and is induced by nicotine exposure in human gingival fibroblasts‘ However‘ therole of HO- l in cancer cells exposed to nicotine has not previously been descnbed We investigated the effects of nicotine on HO-l protein expression and cell viability in immortalized (IHOK) and malignant (HN12) human ora l keratinocyte cells using the MTT assay and Western blotting. We al so examined the involvement of t he phosphoinosit ide-3-0H- kinase (PI3K), mitogen-acti vated protein kinase (MAPK) , and nucJear factor-κ B (NF-κ B) signaling pathways in nicotine-induced cytotoxicity and HO- l levels in IHOK and HN12 cell s‘ Nicotine induced HO- l pro ducti on and had cytotoxic effects on cells in both a concentration- and time-dependent manner. Nicotine-induced cytotox icity and accumulation of HO- l were greater in JJ-IOK cells than in HN12 cells Molecular inhibitors of the ERK, p38 MAP kinase, PI3K, and NF-κ B signaling pathways blocked the cytotoxic effects and induction of J-IO-l expression by nicotine. Treatmen t with an t ioxida nts (bil irubin, N-acetyl cysteine) protected cells against nicotine-induced cytotoxicity and blocked the upregula tion of J-IO- l, the effects of which were more pronounced in II-IOK cells than in HN12 cells Collecti vely, these results suggest that J-IO- l plays a principal role in the protective response to nicotine in oral cancel and immortalized keratinocytes. Moreover, the addition of exogenous antioxidants may help to protect oral epithelial cells as chemopreventive agents against nicotine-induced oxidative stress.

Heme oxygenase-l (HO-l) exhibits cyt oprotective effects in many different cell types and is induced by nicotine exposure in human gingival fibroblasts‘ However‘ therole of HO- l in cancer cells exposed to nicotine has not previously been descnbed We investigated the effects of nicotine on HO-l protein expression and cell viability in immortalized (IHOK) and malignant (HN12) human ora l keratinocyte cells using the MTT assay and Western blotting. We al so examined the involvement of t he phosphoinosit ide-3-0H- kinase (PI3K), mitogen-acti vated protein kinase (MAPK) , and nucJear factor-κ B (NF-κ B) signaling pathways in nicotine-induced cytotoxicity and HO- l levels in IHOK and HN12 cell s‘ Nicotine induced HO- l pro ducti on and had cytotoxic effects on cells in both a concentration- and time-dependent manner. Nicotine-induced cytotox icity and accumulation of HO- l were greater in JJ-IOK cells than in HN12 cells Molecular inhibitors of the ERK, p38 MAP kinase, PI3K, and NF-κ B signaling pathways blocked the cytotoxic effects and induction of J-IO-l expression by nicotine. Treatmen t with an t ioxida nts (bil irubin, N-acetyl cysteine) protected cells against nicotine-induced cytotoxicity and blocked the upregula tion of J-IO- l, the effects of which were more pronounced in II-IOK cells than in HN12 cells Collecti vely, these results suggest that J-IO- l plays a principal role in the protective response to nicotine in oral cancel and immortalized keratinocytes. Moreover, the addition of exogenous antioxidants may help to protect oral epithelial cells as chemopreventive agents against nicotine-induced oxidative stress.

Although substance P (SP). a potent pro-inflammatory peptide, is involved in inflammation and immune responses, the effect of SP 011 the expression of macl'ophage inJlammatol'Y protein 3a (MIP-3a. CCL20) in periodontal ligament (PDL) cells a l'e unknown Equally as enigmatic is the link between SP. the stress protein heme oxygenase-l (HO-l) , and CCL20 product ion. We investigated whether SP induces the release of chemokine CCL20 from irrunortalized POL (IPDL) cells. and further claif’y SP mediated pathways . We also exarnined the relationship between HO-l and CCL20 by treating POL cells with SP Incubating IPOL cells with SP incl'eased ex pl'ession of CCL20 mRNA and CCL20 protein in a dose-time dependent manner. Highly selective p38 and ERKl/2 inhibitors abl'ogated SP-induced expression of CCL20 lD IPOL cells SP is also responsible fo l' ini tiating phosphorylation of I/( B‘ degl'adation of IK B. and activation of NF-/( B. SP induced expression of HO-l in both a concentration- and time-dependent manner. and CCL20 refl ected similal' patterns. The inductive effects of SP on HO-l and CCL20 were enhanced by HO- l inducer hemin and the membrane-permea ble cGMP analog 8-bromo-cGMP Conversely, this pathway was inhi bited by the HO-l inhibitor zinc Pl'otoporphyrin IX (ZnPP IX) and the selective inhibitor of guanylate cyclase‘ 1H- [1. 2. 4]uxad iazole[4, 3-alquinoxal i n- 1-one (ODQ) We report hel'ein the pathway that connects SP a long with other modulators 0 1' neuroimmunoregulationto the induction of HO-1 and the inflanunatol'y mediatol' MIP- 3a /CCL20 in IPDL cel ls. which play an impol'tant role in the development 0 1' pe- I'iodontitis or inflammation during ol'thodontic tooth movement

Al t hough substance P(SP) , a potent pro- inflammatory peptide, is involved in inflammation and immune responses‘ t he eff'ect of SP on t he expression of macrophage inflammatory protein 3a (MIP- 3α CCL20) in periodontal liga ment(PDL) cell s a re unknown, Equally as enigmatic is the link between SP, t he stress protein heme oxygenase- l(HO-l) ‘ and CCL20 procluction, We investigated whether SP induces the release of chemokine CCL20 from immortal ized PDL(IPDL) ceJJ s‘ and fur ther c l a꺼 SP mediated pathways, We also examined the relationship between HO-l a ncl CCL20 by t reating PDL cells with SP, Incubating IPDL cells with SP increased expression of CCL20 mRNA a nd CCL20 protein in a dose-time dependent manner Highly selective p38 and ERKl/2 inhibitors abrogated SP-induced expression of CCL20 in IPDL cell s, SP is a lso responsible for ini t iating phosphorylation of I/C B, degradation of Iκ B‘ ancl activat ion of NF'-/C B, SP induced expression of HO-l in both a concentration- and time-dependent man nel ‘ and CCL20 refl ected s imilar patterns, The inductive effects o[ SP on HO- l and CCL20 wer e enhanced by HO- j inducer hemin and the membrane-permeable cGMP analog 8-bromo-cGMP, Conversely, this pathway was inJübited by t he 1-10난 inhi bitor zinc protoporphyrin IX(ZnPP IX) and the selective inl뼈itor of guanylate cyc1ase‘ lH-[l , 2, 4Joxad iazole[4‘ 3-aJquinoxal in-l-one (ODQ) , We report herein the pathway that connects SP along with other modulators 。f neuroimmunoregulationto the induction of HO-l and t he inflammatory mediator MIP-3a /CCL20 in IPDL cell s‘ which play an important role in the development 01' periodontitis or inflamrnation during orthodontic tooth movem

From 120 soil and activated sludge, the strains able to grow on Benzoate and m-Toluate have been isolated after selective enrichment which were later identified as Psudomonas sp. according to its morphological and biochemical characteristics. Ben-2 strain contained two plasmid DNA having about 120 Kb and below 2.0 Kb by agarose gel electrophoresis. Form the comparative investigation of catechol 1,2-oxygenase and catechol 2,3-oxygenase activities in Ben-2 strain and its cured strain, Ben-2 strain has both of these two enzymes while cured strain has catechol 1,2-oxygenase only.