TY - GEN ED - Szabó, Ádám ED - Tasiné Csúcs, Ildikó Mária / Interviewed person ED - Pál, József / Interviewed person ED - Hannus, István / Interviewed person ED - Wollemann, Mária / Interviewed person ED - Kapronczay, Károly / Interviewed person AU - Visinger, István TI - Akinek nevét a paprikával és a C-vitaminnal együtt emlegetjük ET - 0 PY - 2018 UR - https://m2.mtmt.hu/api/publication/30312021 ID - 30312021 LA - Hungarian DB - MTMT ER - TY - JOUR AU - Zádor, Ferenc AU - Wollemann, Mária TI - Receptome: Interactions between three pain-related receptors or the "Triumvirate" of cannabinoid, opioid and TRPV1 receptors JF - PHARMACOLOGICAL RESEARCH J2 - PHARMACOL RES VL - 102 PY - 2015 SP - 254 EP - 263 PG - 10 SN - 1043-6618 DO - 10.1016/j.phrs.2015.10.015 UR - https://m2.mtmt.hu/api/publication/2998296 ID - 2998296 N1 - Admin megjegyzés-25229264 tblcategory: (Category) ('JOUR\n\nReview') #Jelleg Megjegyzés-25258453 Hiányzó Jelleg: 'JOUR\n\nReview' Admin megjegyzés-25258453 tblcategory: (Category) ('JOUR\n\nReview') #Jelleg Funding Agency and Grant Number: National Research Development and Innovation Office (NKFIH) [OTKA 108518] Funding text: This study was supported by the National Research Development and Innovation Office (NKFIH), grant number: OTKA 108518. The authors would like to thank Dr. Sandor Benyhe, Prof. Anna Borsodi and Dr. Maria Szucs for the critical reading of the manuscript. The authors are also very grateful to Dr. Erna Zador, Dr. Ferenc Otvos and Dr. Istvan Katona for their help, ideas and for reviewing the manuscript. Export Date: 17 August 2020 CODEN: PHMRE Cited By :18 Export Date: 25 May 2021 CODEN: PHMRE Correspondence Address: Zádor, F.; Institute of Biochemistry, Temesvári krt. 62, Hungary; email: zador.ferenc@gmail.com AB - A growing amount of data demonstrates the interactions between cannabinoid, opioid and the transient receptor potential (TRP) vanilloid type 1 (TRPV1) receptors. These interactions can be bidirectional, inhibitory or excitatory, acute or chronic in their nature, and arise both at the molecular level (structurally and functionally) and in physiological processes, such as pain modulation or perception. The interactions of these three pain-related receptors may also reserve important and new therapeutic applications for the treatment of chronic pain or inflammation. In this review, we summarize the main findings on the interactions between the cannabinoid, opioid and the TRPV1 receptor regarding to pain modulation. (C) 2015 Elsevier Ltd. All rights reserved. LA - English DB - MTMT ER - TY - JOUR AU - Bocsik, Alexandra AU - Darula, Zsuzsanna AU - Tóth, Géza AU - Deli, Mária Anna AU - Wollemann, Mária TI - Transfer of opiorphin through a blood-brain barrier culture model JF - ARCHIVES OF MEDICAL RESEARCH J2 - ARCH MED RES VL - 46 PY - 2015 IS - 6 SP - 502 EP - 506 PG - 5 SN - 0188-4409 DO - 10.1016/j.arcmed.2015.06.009 UR - https://m2.mtmt.hu/api/publication/2915571 ID - 2915571 LA - English DB - MTMT ER - TY - JOUR AU - Benyhe, Z AU - Tóth, Géza AU - Wollemann, Mária AU - Borsodi, Anna AU - Helyes, Zsuzsanna AU - Rougeot, C AU - Benyhe, Sándor TI - Effects of synthetic analogues of human opiorphin on rat brain opioid receptors. JF - JOURNAL OF PHYSIOLOGY AND PHARMACOLOGY J2 - J PHYSIOL PHARMACOL VL - 65 PY - 2014 IS - 4 SP - 525 EP - 530 PG - 6 SN - 0867-5910 UR - https://m2.mtmt.hu/api/publication/2731289 ID - 2731289 N1 - Export Date: 27 January 2024; CODEN: JPHPE AB - Human opiorphin (Gln-Arg-Phe-Ser-Arg; QRFSR-peptide) is a physiological inhibitor of enkephalin-inactivating peptidases. We previously demonstrated that opiorphin can substitute for the classic mixture of peptidase inhibitors and greatly improves the specific binding and affinity of the enkephalin-related peptide [(3)H]MERF (Tyr-Gly-Gly-Phe-Met-Arg-Phe; YGGFMRF) for rat brain opioid receptors. To extend the metabolic stability of opiorphin in human plasma two functional derivatives were designed, i.e., Cys-[(CH2)6]-QRF-[Ser-O-octanoyl]-R peptide (monomeric CC6-opiorphin) and its cystine-dipeptide (dimeric CC6-opiorphin) derivative. We found that, in homologous competition experiments, the affinity of [(3)H]MERF for rat brain opioid receptors was significantly increased in the presence of monomeric and dimeric CC6-opiorphin, compared to control-Tris buffer. In addition ten times lower concentrations (5 muM) than those required for native opiorphin (50 muM) were sufficient. In heterologous competition experiments, using unlabeled dynorphin(1-10), affinity increases were also observed: increases in binding were similar with either monomeric or dimeric CC6-opiorphin. Surprisingly, these opiorphin analogues displayed weak competitive effects on [(3)H]MERF binding to rat brain opioid receptors in the absence of unlabeled MERF, effects never observed for the native opiorphin. In conclusion, CC6-opiorphin compounds are certainly more potent than the native opiorphin in increasing the binding and the affinity of homologous and heterologous competition, but the binding enhancement occurs only at temperatures much higher than 0 degrees C, specifically at 24 degrees C. LA - English DB - MTMT ER - TY - JOUR AU - Wollemann, Mária AU - Tóth, Fanni AU - Benyhe, Sándor TI - Protein kinase C inhibitor BIM suspended TRPV1 effect on mu-opioid receptor JF - BRAIN RESEARCH BULLETIN J2 - BRAIN RES BULL VL - 90 PY - 2013 SP - 114 EP - 117 PG - 4 SN - 0361-9230 DO - 10.1016/j.brainresbull.2012.10.008 UR - https://m2.mtmt.hu/api/publication/2223828 ID - 2223828 N1 - Funding Agency and Grant Number: Hungarian Research Foundation (OTKA)Orszagos Tudomanyos Kutatasi Alapprogramok (OTKA) [CK 78566] Funding text: The study was supported by a grant from the Hungarian Research Foundation (OTKA) CK 78566. The authors wish to thank Mrs. Katalin Horvath Pappne for her excellent technical assistance. Export Date: 17 August 2020 CODEN: BRBUD AB - The purpose of the present study was to elucidate the role of protein kinase A and C in the mechanism of capsaicin inhibition on mu-opiate receptors. H89, a protein kinase A inhibitor and BIM (bisindolylmaleimide), a protein kinase C inhibitor were used for this purpose. BIM suspended the inhibition of capsaicin in endomorphin-1 competition binding. The addition of BIM alone had no effect itself on this reaction. H89 however, exerted a strong inhibitory effect on the endomorphin-1 binding. We can conclude that protein kinase C certainly plays a role in the inhibition of capsaicin. The role of protein kinase A in this reaction could not be established, owing to the blocking effect of H89 on the mu-opioid receptors. (c) 2012 Elsevier Inc. All rights reserved. LA - English DB - MTMT ER - TY - JOUR AU - Tóth, Fanni AU - Tóth, Géza AU - Benyhe, Sándor AU - Rougeot, C AU - Wollemann, Mária TI - Opiorphin highly improves the specific binding and affinity of MERF and MEGY to rat brain opioid receptors JF - REGULATORY PEPTIDES J2 - REGUL PEPTIDES VL - 178 PY - 2012 IS - 1-3 SP - 71 EP - 75 PG - 5 SN - 0167-0115 DO - 10.1016/j.regpep.2012.06.011 UR - https://m2.mtmt.hu/api/publication/2110516 ID - 2110516 AB - Endogenously occurring opioid peptides are rapidly metabolized by different ectopeptidases. Human opiorphin is a recently discovered natural inhibitor of the enkephalin-inactivating neutral endopeptidase (NEP) and aminopeptidase-N (AP-N) (Wisner et al., 2006). To date, in vitro receptor binding experiments must be performed either in the presence of a mixture of peptidase inhibitors and/or at low temperatures, to block peptidase activity. Here we demonstrate that, compared to classic inhibitor cocktails, opiorphin dramatically increases the binding of [H-3]MERF and [H-3]MEGY ligands to rat brain membrane preparations. We found that at 0 degrees C the increase in specific binding is as high as 40-60% and at 24 degrees C this rise was even higher. In contrast, the binding of the control [H-3]endomorphin-1, which is relatively slowly degraded in rat brain membrane preparations, was not enhanced by opiorphin compared to other inhibitors. In addition, in homologous binding displacement experiments, the IC50 affinity values measured at 24 degrees C were also significantly improved using opiorphin compared to the inhibitor cocktail. In heterologous binding experiments the differences were less obvious, but still pronounced using [H-3]MERF and MEGY compared to dynorphin(1-11), or naloxone and DAGO competitor ligands. (C) 2012 Elsevier B.V. All rights reserved. LA - English DB - MTMT ER - TY - JOUR AU - Wollemann, Mária TI - Recent developments in the molecular biology of the pain JF - ACTA BIOLOGICA SZEGEDIENSIS J2 - ACTA BIOL SZEGED VL - 55 PY - 2011 IS - 1 SP - 1 EP - 6 PG - 6 SN - 1588-385X UR - https://m2.mtmt.hu/api/publication/1921822 ID - 1921822 N1 - Export Date: 13 February 2020 CODEN: ABSCC Correspondence Address: Wollemann, M.; Institute of Biochemistry, Biological Research Center, Hungarian Academy of Sciences, Szeged, Hungary LA - English DB - MTMT ER - TY - JOUR AU - Csabafi, Krisztina AU - Jászberényi, Miklós AU - Bagosi, Zsolt AU - Tóth, Géza AU - Wollemann, Mária AU - Telegdy, Gyula TI - The action of a synthetic derivative of Met(5)-enkephalin-Arg(6)-Phe(7) on behavioral and endocrine responses JF - PEPTIDES J2 - PEPTIDES VL - 32 PY - 2011 IS - 8 SP - 1656 EP - 1660 PG - 5 SN - 0196-9781 DO - 10.1016/j.peptides.2011.05.029 UR - https://m2.mtmt.hu/api/publication/1886257 ID - 1886257 LA - English DB - MTMT ER - TY - JOUR AU - Wollemann, Mária TI - A TRP termoszenzoros és fájdalomérzékelő receptorok molekuláris szerkezete és funkciója JF - BIOKÉMIA: A MAGYAR BIOKÉMIAI EGYESÜLET FOLYÓIRATA J2 - BIOKÉMIA VL - 33 PY - 2009 IS - 2 SP - 19 EP - 28 PG - 10 SN - 0133-8455 UR - https://m2.mtmt.hu/api/publication/1920949 ID - 1920949 LA - Hungarian DB - MTMT ER - TY - JOUR AU - Wollemann, Mária AU - Ioja, Enikő AU - Benyhe, Sándor TI - Capsaicin inhibits the in vitro binding of peptides selective for mu- and kappa-opioid, and nociceptin-receptors JF - BRAIN RESEARCH BULLETIN J2 - BRAIN RES BULL VL - 77 PY - 2008 IS - 2-3 SP - 136 EP - 142 PG - 7 SN - 0361-9230 DO - 10.1016/j.brainresbull.2008.06.003 UR - https://m2.mtmt.hu/api/publication/1918055 ID - 1918055 N1 - Megjegyzés-20891859 FU: National Office for Research and Technology (NKTH), Budapest, Hungary ; : Del-Alfoldi Regionalis Tudaskozpont [RET-2004-DNT] FX: This study was supported by funds from the National Office for Research : and Technology (NKTH), Budapest, Hungary; grant number: RET-2004-DNT : (Del-Alfoldi Regionalis Tudaskozpont). The authors thank Dr. Maria : Szucs for critical reading of the manuscript and Mrs. Katalin Horvath : Pappne for her excellent technical assistance. Capsaicin was a generous : gift of Prof. Gabor Jancso, Department of Physiology, University of : Szeged Medical School. Megjegyzés-22120088 DI: 10.1016/j.brainresbull.2008.06.003 Megjegyzés-22130226 DI: 10.1016/j.brainresbull.2008.06.003 Megjegyzés-22152746 DI: 10.1016/j.brainresbull.2008.06.003 Megjegyzés-22186306 DI: 10.1016/j.brainresbull.2008.06.003 Megjegyzés-22209986 DI: 10.1016/j.brainresbull.2008.06.003 Funding Agency and Grant Number: National Office for Research and Technology (NKTH), Budapest, HungaryNational Office for Research and Technology; Del-Alfoldi Regionalis Tudaskozpont [RET-2004-DNT] Funding text: This study was supported by funds from the National Office for Research and Technology (NKTH), Budapest, Hungary; grant number: RET-2004-DNT (Del-Alfoldi Regionalis Tudaskozpont). The authors thank Dr. Maria Szucs for critical reading of the manuscript and Mrs. Katalin Horvath Pappne for her excellent technical assistance. Capsaicin was a generous gift of Prof. Gabor Jancso, Department of Physiology, University of Szeged Medical School. Export Date: 17 August 2020 CODEN: BRBUD AB - Capsaicin inhibited the equilibrium specific binding of endogenous opioid-like peptide ligands such as endomorphin-1, nociceptin, and dynorphin((1-17)) in rat brain membrane preparations. We studied the in vitro effect of capsaicin (1-10 mu M) on homologous and heterologous competitive binding of opioid ligands, using unlabeled synthetic peptides and the following tritiated compounds: [H-3]endomorphin-1, 1[H-3]endomorphin-2,[H-3]nociceptin((1-17)) and [H-3]dynorphin((1-17)). Capsaicin-dependent inhibition was also observed in [S-35]GTP gamma S stimulation assays in the presence of certain opioid peptides. The inhibition of opioid binding was further investigated using other synthetic and natural mu-opioid ligands such as [D-Ala(2),(NMe)Phe(4),Gly(5)-ol]enkephalin (DAMGO), morphine and naloxone. The decrease in opioid ligand affinity upon capsaicin treatments was most apparent with endomorphin-1, followed by nociceptin and dynorphin. The binding of other investigated opioids were not affected in the presence of capsaicin. In [H-3]endomorphin-1 binding assays, capsazepine antagonized the inhibitory effect of capsaicin in rat brain membranes suggesting the involvement of TRPV1 receptors. In Chinese hamster ovary (CHO) cells stably expressing mu-opioid receptors, but lacking vanilloid receptors, the inhibition by capsaicin on the binding of [H-3]endomorphin-1 was not present. It is concluded that the inhibitory effect of capsaicin on the receptor binding affinity of endogenous opioid peptides in brain membrane preparations seems not to be a direct effect, it is rather a negative feedback interaction with opioid receptors. (C) 2008 Elsevier Inc. All rights reserved. LA - English DB - MTMT ER -