Hernandez M

References (6)

Title : Paraoxonase-1 activity in patients with cancer: A systematic review and meta-analysis - Arenas_2018_Crit.Rev.Oncol.Hematol_127_6
Author(s) : Arenas M , Rodriguez E , Sahebkar A , Sabater S , Rizo D , Pallise O , Hernandez M , Riu F , Camps J , Joven J
Ref : Crit Rev Oncol Hematol , 127 :6 , 2018
Abstract : PURPOSE: Paraoxonase-1 (PON1) is a lipolactonase implicated in the elimination of carcinogenic free radicals and in the scavenging mechanisms to maintain oxidative balance. The objective of the present systematic review and meta-analysis was to evaluate possible alterations in serum PON1 activity in patients with cancer. METHODS: A systematic search of the observational studies in humans published in the last 15 years was performed through Medline databases following the PRISMA and STARLITE statements. Further, a keyword-based computerized search with restrictions on publication date, and a meta-analysis of case-control studies was performed. RESULTS: In total, 23 studies were included most of which reported decreased PON1 activity in patients with cancer. This could indicate impaired defense ability against oxidative stress with potential implications in cell proliferation, promotion of genetic instability, and alterations in cellular sensitivity to chemotherapy. CONCLUSION: This systematic review and meta-analysis confirms a consistent association between cancer and decreased serum PON1 activities. These findings may open fruitful lines of research with clinical relevance, and an understanding of molecular alterations underlying carcinogenesis.
ESTHER : Arenas_2018_Crit.Rev.Oncol.Hematol_127_6
PubMedSearch : Arenas_2018_Crit.Rev.Oncol.Hematol_127_6
PubMedID: 29891113

Title : Immunohistochemical analysis of paraoxonases-1 and 3 in human atheromatous plaques - Marsillach_2011_Eur.J.Clin.Invest_41_308
Author(s) : Marsillach J , Camps J , Beltran-Debon R , Rull A , Aragones G , Maestre-Martinez C , Sabench F , Hernandez M , Castillo DD , Joven J , Mackness MI , Mackness B
Ref : European Journal of Clinical Investigation , 41 :308 , 2011
Abstract : BACKGROUND: The paraoxonase (PON) enzyme family comprising PON1, PON2 and PON3 are antioxidant enzymes that degrade bioactive oxidised lipids and are thus antiatherogenic. MATERIALS AND
METHODS: We investigated the localisation of the PON proteins during the development of atherosclerosis by immunohistochemical analysis.
RESULTS: In normal aortas, PON1 and PON3 were localised to smooth muscle cells (SMC) and endothelial cells. PON3 staining was stronger than that of PON1. During atherosclerosis development, SMC staining for PON1 and PON3 was greatly reduced, while macrophage staining for both proteins increased with PON1 predominating. Macrophage staining for PON1 and PON3 was significantly and positively related to the amount of aortic inflammation (both P<0.001).
CONCLUSIONS: Our data add support to the growing body of evidence for a cellular protective effect of PON1 and PON3 against the proinflammatory/proatherosclerotic effects of lipid peroxidation.
ESTHER : Marsillach_2011_Eur.J.Clin.Invest_41_308
PubMedSearch : Marsillach_2011_Eur.J.Clin.Invest_41_308
PubMedID: 20964682

Title : The genome sequence of taurine cattle: a window to ruminant biology and evolution - Elsik_2009_Science_324_522
Author(s) : Elsik CG , Tellam RL , Worley KC , Gibbs RA , Muzny DM , Weinstock GM , Adelson DL , Eichler EE , Elnitski L , Guigo R , Hamernik DL , Kappes SM , Lewin HA , Lynn DJ , Nicholas FW , Reymond A , Rijnkels M , Skow LC , Zdobnov EM , Schook L , Womack J , Alioto T , Antonarakis SE , Astashyn A , Chapple CE , Chen HC , Chrast J , Camara F , Ermolaeva O , Henrichsen CN , Hlavina W , Kapustin Y , Kiryutin B , Kitts P , Kokocinski F , Landrum M , Maglott D , Pruitt K , Sapojnikov V , Searle SM , Solovyev V , Souvorov A , Ucla C , Wyss C , Anzola JM , Gerlach D , Elhaik E , Graur D , Reese JT , Edgar RC , McEwan JC , Payne GM , Raison JM , Junier T , Kriventseva EV , Eyras E , Plass M , Donthu R , Larkin DM , Reecy J , Yang MQ , Chen L , Cheng Z , Chitko-McKown CG , Liu GE , Matukumalli LK , Song J , Zhu B , Bradley DG , Brinkman FS , Lau LP , Whiteside MD , Walker A , Wheeler TT , Casey T , German JB , Lemay DG , Maqbool NJ , Molenaar AJ , Seo S , Stothard P , Baldwin CL , Baxter R , Brinkmeyer-Langford CL , Brown WC , Childers CP , Connelley T , Ellis SA , Fritz K , Glass EJ , Herzig CT , Iivanainen A , Lahmers KK , Bennett AK , Dickens CM , Gilbert JG , Hagen DE , Salih H , Aerts J , Caetano AR , Dalrymple B , Garcia JF , Gill CA , Hiendleder SG , Memili E , Spurlock D , Williams JL , Alexander L , Brownstein MJ , Guan L , Holt RA , Jones SJ , Marra MA , Moore R , Moore SS , Roberts A , Taniguchi M , Waterman RC , Chacko J , Chandrabose MM , Cree A , Dao MD , Dinh HH , Gabisi RA , Hines S , Hume J , Jhangiani SN , Joshi V , Kovar CL , Lewis LR , Liu YS , Lopez J , Morgan MB , Nguyen NB , Okwuonu GO , Ruiz SJ , Santibanez J , Wright RA , Buhay C , Ding Y , Dugan-Rocha S , Herdandez J , Holder M , Sabo A , Egan A , Goodell J , Wilczek-Boney K , Fowler GR , Hitchens ME , Lozado RJ , Moen C , Steffen D , Warren JT , Zhang J , Chiu R , Schein JE , Durbin KJ , Havlak P , Jiang H , Liu Y , Qin X , Ren Y , Shen Y , Song H , Bell SN , Davis C , Johnson AJ , Lee S , Nazareth LV , Patel BM , Pu LL , Vattathil S , Williams RL, Jr. , Curry S , Hamilton C , Sodergren E , Wheeler DA , Barris W , Bennett GL , Eggen A , Green RD , Harhay GP , Hobbs M , Jann O , Keele JW , Kent MP , Lien S , McKay SD , McWilliam S , Ratnakumar A , Schnabel RD , Smith T , Snelling WM , Sonstegard TS , Stone RT , Sugimoto Y , Takasuga A , Taylor JF , Van Tassell CP , Macneil MD , Abatepaulo AR , Abbey CA , Ahola V , Almeida IG , Amadio AF , Anatriello E , Bahadue SM , Biase FH , Boldt CR , Carroll JA , Carvalho WA , Cervelatti EP , Chacko E , Chapin JE , Cheng Y , Choi J , Colley AJ , de Campos TA , De Donato M , Santos IK , de Oliveira CJ , Deobald H , Devinoy E , Donohue KE , Dovc P , Eberlein A , Fitzsimmons CJ , Franzin AM , Garcia GR , Genini S , Gladney CJ , Grant JR , Greaser ML , Green JA , Hadsell DL , Hakimov HA , Halgren R , Harrow JL , Hart EA , Hastings N , Hernandez M , Hu ZL , Ingham A , Iso-Touru T , Jamis C , Jensen K , Kapetis D , Kerr T , Khalil SS , Khatib H , Kolbehdari D , Kumar CG , Kumar D , Leach R , Lee JC , Li C , Logan KM , Malinverni R , Marques E , Martin WF , Martins NF , Maruyama SR , Mazza R , McLean KL , Medrano JF , Moreno BT , More DD , Muntean CT , Nandakumar HP , Nogueira MF , Olsaker I , Pant SD , Panzitta F , Pastor RC , Poli MA , Poslusny N , Rachagani S , Ranganathan S , Razpet A , Riggs PK , Rincon G , Rodriguez-Osorio N , Rodriguez-Zas SL , Romero NE , Rosenwald A , Sando L , Schmutz SM , Shen L , Sherman L , Southey BR , Lutzow YS , Sweedler JV , Tammen I , Telugu BP , Urbanski JM , Utsunomiya YT , Verschoor CP , Waardenberg AJ , Wang Z , Ward R , Weikard R , Welsh TH, Jr. , White SN , Wilming LG , Wunderlich KR , Yang J , Zhao FQ
Ref : Science , 324 :522 , 2009
Abstract : To understand the biology and evolution of ruminants, the cattle genome was sequenced to about sevenfold coverage. The cattle genome contains a minimum of 22,000 genes, with a core set of 14,345 orthologs shared among seven mammalian species of which 1217 are absent or undetected in noneutherian (marsupial or monotreme) genomes. Cattle-specific evolutionary breakpoint regions in chromosomes have a higher density of segmental duplications, enrichment of repetitive elements, and species-specific variations in genes associated with lactation and immune responsiveness. Genes involved in metabolism are generally highly conserved, although five metabolic genes are deleted or extensively diverged from their human orthologs. The cattle genome sequence thus provides a resource for understanding mammalian evolution and accelerating livestock genetic improvement for milk and meat production.
ESTHER : Elsik_2009_Science_324_522
PubMedSearch : Elsik_2009_Science_324_522
PubMedID: 19390049
Gene_locus related to this paper: bovin-2neur , bovin-a0jnh8 , bovin-a5d7b7 , bovin-ACHE , bovin-balip , bovin-dpp4 , bovin-dpp6 , bovin-e1bi31 , bovin-e1bn79 , bovin-est8 , bovin-f1mbd6 , bovin-f1mi11 , bovin-f1mr65 , bovin-f1n1l4 , bovin-g3mxp5 , bovin-q0vcc8 , bovin-q2kj30 , bovin-q3t0r6 , bovin-thyro

Title : Characterization of the 5-hydroxytryptamine receptors mediating contraction in the pig isolated intravesical ureter - Hernandez_2003_Br.J.Pharmacol_138_137
Author(s) : Hernandez M , Barahona MV , Simonsen U , Recio P , Rivera L , Martinez AC , Garcia-Sacristan A , Orensanz LM , Prieto D
Ref : British Journal of Pharmacology , 138 :137 , 2003
Abstract : 1 This study was designed to investigate the effect of 5-hydroxytryptamine (5-HT) and to characterize the 5-HT receptors involved in 5-HT responses in the pig intravesical ureter. 2 5-HT (0.01-10 microM) concentration-dependently increased the tone of intravesical ureteral strips, whereas the increases in phasic contractions were concentration-independent. The 5-HT(2) receptor agonist alpha-methyl 5-HT, mimicked the effect on tone whereas weak or no response was obtained with 5-CT, 8-OH-DPAT, m-chlorophenylbiguanide and RS 67333, 5-HT(1), 5-HT(1A), 5-HT(3) and 5-HT(4) receptor agonists, respectively. 5-HT did not induce relaxation of U46619-contracted ureteral preparations. Pargyline (100 microM), a monoaminooxidase A/B activity inhibitor, produced leftward displacements of the concentration-response curves for 5-HT. 3 5-HT-induced tone was reduced by the 5-HT(2) and 5-HT(2A) receptor antagonists ritanserine (0.1 microM) and spiperone (0.2 microM), respectively. However, 5-HT contraction was not antagonized by cyanopindolol (2 microM), SDZ-SER 082 (1 microM), Y-25130 (1 microM) and GR 113808 (0.1 microM), which are respectively, 5-HT(1A/1B), 5-HT(2B/2C), 5-HT(3), and 5-HT(4) selective receptor antagonists. 4 Removal of the urothelium did not modify 5-HT-induced contractions. Blockade of neuronal voltage-activated sodium channels, alpha-adrenergic receptors and adrenergic neurotransmission with tetrodotoxin (1 microM), phentolamine (0.3 microM) and guanethidine (10 microM), respectively, reduced the contractions to 5-HT. However, physostigmine (1 microM), atropine (0.1 microM) and suramin (30 microM), inhibitors of cholinesterase activity, muscarinic- and purinergic P(2)-receptors, respectively, failed to modify the contractions to 5-HT. 5 These results suggest that 5-HT increases the tone of the pig intravesical ureter through 5-HT(2A) receptors located at the smooth muscle. Part of the 5-HT contraction is indirectly mediated via noradrenaline release from sympathetic nerves.
ESTHER : Hernandez_2003_Br.J.Pharmacol_138_137
PubMedSearch : Hernandez_2003_Br.J.Pharmacol_138_137
PubMedID: 12522083

Title : Regulation of lipid metabolism and gene expression by fenofibrate in hamsters. -
Author(s) : Guo Q , Wang PR , Milot DP , Ippolito MC , Hernandez M , Burton CA , Wright SD , Chao Y
Ref : Biochimica & Biophysica Acta , 1533 :220 , 2001
PubMedID: 11731332

Title : Histochemical and functional evidence for a cholinergic innervation of the equine ureter - Prieto_1994_J.Autonom.Nerv.Syst_47_159
Author(s) : Prieto D , Simonsen U , Martin J , Hernandez M , Rivera L , Lema L , Garcia P , Garcia-Sacristan A
Ref : Journal of the Autonomic Nervous System , 47 :159 , 1994
Abstract : The distribution of acetylcholinesterase (AChE)-positive nerve fibers and cells, as well as the effects of acetylcholine (ACh) on ureteral smooth muscle and small resistance arteries were investigated in the equine ureter by means of histochemical, classic organ baths and myograph techniques. AChE-positive nerve fibers were widely distributed throughout the ureteral wall forming muscular, subepithelial and perivascular nerve plexuses, whose density was highest at the intravesical ureter. AChE-positive nerve cells were also identified grouped as adventitial or intramural ganglia. ACh increased concentration-dependently both the frequency of phasic contractile activity and basal tone of the isolated intravesical ureter, the pD2 values being 6.31 +/- 0.18 and 6.59 +/- 0.13, respectively. The ACh-induced motor effects in ureteral smooth muscle were blocked by atropine, giving pIC50 values of 8.58 +/- 0.08 and 9.68 +/- 0.05 for phasic activity and tone, respectively. Hexamethonium only inhibited ACh-evoked contractile activity at the highest concentration used. ACh elicited a potent endothelium-dependent relaxation of equine ureteral resistance arteries precontracted with 40 mM K-PSS, the pD2 value being 7.94 +/- 0.07. This relaxant response was abolished in the presence of the nitric oxide (NO) inhibitor, NG-nitro-L-arginine (L-NNA), the blockade being reversed by subsequent incubation with the NO exogenous substrate, L-arginine. The ACh-induced relaxation was competitively antagonized by atropine (pA2 = 10.05 +/- 0.18). The present results suggest the existence of a rich cholinergic innervation in the equine ureter which controls both ureteral smooth muscle and resistance arteries motor activity through the muscarinic effects of ACh. In addition, the ACh relaxant response in the ureteral resistance arteries seems to be mediated by NO.
ESTHER : Prieto_1994_J.Autonom.Nerv.Syst_47_159
PubMedSearch : Prieto_1994_J.Autonom.Nerv.Syst_47_159
PubMedID: 7912246