TY - BOOK AU - Árva, Hédi AU - Huliák, Ildikó AU - Szűcs, Gergő AU - Csont, Tamás Bálint AU - Matejka, Zsombor AU - Csontné Kiricsi, Mónika TI - A TRIGLICERID, ILLETVE A FENOFIBRÁT KEZELÉS HATÁSÁNAK VIZSGÁLATA AORTA-VENA CAVA SHUNTTEL KIALAKÍTOTT VOLUMENTERHELÉSES PATKÁNY SZÍV MODELLBEN PY - 2024 SN - 9786156457523 UR - https://m2.mtmt.hu/api/publication/35431401 ID - 35431401 LA - Hungarian DB - MTMT ER - TY - JOUR AU - Rónavári, Andrea AU - Ochirkhuyag, Altantuya AU - Igaz, Nóra AU - Szerencsés, Bettina AU - Ballai, Gergő AU - Huliák, Ildikó AU - Bocz, Csenge AU - Kovács, Ákos AU - Pfeiffer, Ilona AU - Csontné Kiricsi, Mónika AU - Kónya, Zoltán TI - Preparation, characterization and in vitro evaluation of the antimicrobial and antitumor activity of MnOx nanoparticles JF - COLLOIDS AND SURFACES A : PHYSICOCHEMICAL AND ENGINEERING ASPECTS J2 - COLLOID SURFACE A VL - 688 PY - 2024 SN - 0927-7757 DO - 10.1016/j.colsurfa.2024.133528 UR - https://m2.mtmt.hu/api/publication/34687262 ID - 34687262 LA - English DB - MTMT ER - TY - JOUR AU - Kovács, Ferenc AU - Huliák, Ildikó AU - Árva, Hédi AU - Csontné Kiricsi, Mónika AU - Erdős, Dóra AU - Kocsis, Marianna AU - Takács, Gergely AU - Balogh, György Tibor AU - Nagyné Frank, Éva TI - Medicinal-Chemistry-Driven Approach to 2-Substituted Benzoxazole–Estradiol Chimeras: Synthesis, Anticancer Activity, and Early ADME Profile JF - CHEMMEDCHEM J2 - CHEMMEDCHEM VL - 18 PY - 2023 IS - 22 PG - 9 SN - 1860-7179 DO - 10.1002/cmdc.202300352 UR - https://m2.mtmt.hu/api/publication/34147665 ID - 34147665 N1 - Department of Molecular and Analytical Chemistry, University of Szeged, Dóm tér 7–8, Szeged, 6720, Hungary Department of Biochemistry and Molecular Biology, Doctoral School of Biology, University of Szeged, Közép fasor 52, Szeged, 6726, Hungary Department of Chemical and Environmental Process Engineering, Budapest University of Technology and Economics, Műegyetem rkp. 3, Budapest, 1111, Hungary Mcule.com Kft., Bartók Béla út 105–113, Budapest, 1115, Hungary Department of Pharmaceutical Chemistry, Semmelweis University, Hőgyes E. 9, Budapest, 1085, Hungary Export Date: 13 October 2023 CODEN: CHEMG Correspondence Address: Frank, É.; Department of Molecular and Analytical Chemistry, Dóm tér 7–8, Hungary; email: frank@chem.u-szeged.hu Correspondence Address: Balogh, G.T.; Department of Chemical and Environmental Process Engineering, Műegyetem rkp. 3, Hungary; email: balogh.gyorgy.tibor@semmelwies.hu AB - The efficient synthesis of novel estradiol‐based A‐ring‐fused oxazole derivatives, which can be considered as benzoxazole‐steroid domain‐integrated hybrids containing a common benzene structural motif, is described. The target compounds were prepared from steroidal 2‐aminophenol precursors by heterocycle formation or functional group interconversion (FGI) strategies. According to 2D projection‐based t‐distributed stochastic neighbor embedding (t‐SNE), the novel molecules were proved to represent a new chemical space among steroid drugs. They were characterized based on critical physicochemical parameters using in silico and experimental data. The performance of the compounds to inhibit cell proliferation was tested on four human cancer cell lines and non‐cancerous cells. Further examinations were performed to reveal IC50 and lipophilic ligand efficiency (LLE) values, cancer cell selectivity, and apoptosis‐triggering features. Pharmacological tests and LLE metric revealed that some derivatives, especially the 2‐(4‐ethylpiperazin‐1‐yl)oxazole derivative exhibit strong anticancer activity and trigger the apoptosis of cancer cells with relatively low promiscuity risk similarly to the structurally most closely‐related and intensively studied anticancer agent, 2‐methoxy‐estradiol. LA - English DB - MTMT ER - TY - JOUR AU - Nagy, Ferenc István AU - Gopisetty, Mohana Krishna AU - Huliák, Ildikó AU - Nagyné Frank, Éva AU - Csontné Kiricsi, Mónika TI - Semi-synthetic dihydrotestosterone derivatives modulate inherent multidrug resistance and sensitize colon cancer cells to chemotherapy JF - FEBS OPEN BIO J2 - FEBS OPEN BIO VL - 13 PY - 2023 IS - S2 SP - 66 EP - 66 PG - 1 SN - 2211-5463 UR - https://m2.mtmt.hu/api/publication/34070423 ID - 34070423 LA - English DB - MTMT ER - TY - JOUR AU - Nagy, Ferenc István AU - Adamecz, Dóra Izabella AU - Baji, Ádám AU - Kiricsi, Ágnes AU - Huliák, Ildikó AU - Rónavári, Andrea AU - Kónya, Zoltán AU - Nagyné Frank, Éva AU - Gopisetty, Mohana Krishna AU - Csontné Kiricsi, Mónika TI - Semi-Synthetic Dihydrotestosterone Derivatives Modulate Inherent Multidrug Resistance and Sensitize Colon Cancer Cells to Chemotherapy JF - PHARMACEUTICS J2 - PHARMACEUTICS VL - 15 PY - 2023 IS - 2 PG - 22 SN - 1999-4923 DO - 10.3390/pharmaceutics15020584 UR - https://m2.mtmt.hu/api/publication/33634274 ID - 33634274 AB - Multidrug resistance (MDR) is a serious hurdle to successful cancer therapy. Here, we examined the efficiency of novel semi-synthetic dihydrotestosterone derivatives, more specifically androstano-arylpyrimidines in inhibiting the efflux activity of ATP-binding cassette (ABC) transporters and sensitizing inherently MDR colon cancer cells to various chemotherapy drugs. Using the Rhodamine123 accumulation assay, we evaluated the efflux activity of cancer cells following treatments with androstano-arylpyrimidines. We found that acetylated compounds were capable of attenuating the membrane efflux of inherently MDR cells; however, deacetylated counterparts were ineffective. To delineate the possible molecular mechanisms underlying these unique activities of androstano-arylpyrimidines, the degree of apoptosis induction was assessed by AnnexinV-based assays, both upon the individual as well as by steroid and chemotherapy agent combination treatments. Five dihydrotestosterone derivatives applied in combination with Doxorubicin or Epirubicin triggered massive apoptosis in MDR cells, and these combinations were more efficient than chemotherapy drugs together with Verapamil. Furthermore, our results revealed that androstano-arylpyrimidines induced significant endoplasmic reticulum stress (ER stress) but did not notably modulate ABC transporter expression. Therefore, ER stress triggered by acetylated androstano-arylpyrimidines is probably involved in the mechanism of efflux pump inhibition and drug sensitization which can be targeted in future drug developments to defeat inherently multidrug-resistant cancer. LA - English DB - MTMT ER - TY - BOOK AU - Árva, Hédi AU - Huliák, Ildikó AU - Leprán, István AU - Csontné Kiricsi, Mónika TI - METABOLIKUS SZABÁLYOZÓ GÉNEK EXPRESSZIÓS VIZSGÁLATA PATKÁNYMODELLBEN PY - 2022 SN - 9786158205481 UR - https://m2.mtmt.hu/api/publication/35431263 ID - 35431263 LA - Hungarian DB - MTMT ER - TY - THES AU - Huliák, Ildikó TI - Tumor-asszociált miofibroblasztok genetikai, epigenetikai, transzkripciós és funkcionális jellemzői [Genetic, epigenetic, transcriptional and functional comparison of tumor-associated and adjacent normal myofibroblasts] PB - Szegedi Tudományegyetem (SZTE) PY - 2021 SP - 95 DO - 10.14232/phd.10787 UR - https://m2.mtmt.hu/api/publication/32474165 ID - 32474165 LA - Hungarian DB - MTMT ER - TY - JOUR AU - Huliák, Ildikó AU - Bodai, László AU - Czepán, Mátyás AU - Kovács, Dávid AU - Szabó, Anikó AU - Tiszlavicz, László AU - Lázár, György ifj AU - Rakonczay, Zoltán AU - Hegyi, Péter AU - Boros, Imre Miklós AU - Csontné Kiricsi, Mónika TI - Genetic, epigenetic and transcriptional comparison of esophagus tumor‑associated and adjacent normal myofibroblasts JF - ONCOLOGY REPORTS J2 - ONCOL REP VL - 41 PY - 2019 IS - 2 SP - 839 EP - 852 PG - 14 SN - 1021-335X DO - 10.3892/or.2018.6909 UR - https://m2.mtmt.hu/api/publication/30350391 ID - 30350391 N1 - Department of Biochemistry and Molecular Biology, University of Szeged, Közép fasor 52, Szeged, H-6726, Hungary First Department of Medicine, University of Szeged, Szeged, H-6720, Hungary Institute of Biochemistry, Biological Research Center of the Hungarian Academy of Sciences, Szeged, H-6726, Hungary Department of Pathology, University of Szeged, Szeged, H-6720, Hungary Department of Surgery, University of Szeged, Szeged, H-6720, Hungary Department of Pathophysiology, University of Szeged, Szeged, H-6720, Hungary MTA-SZTE Lendület Translational Gastroenterology Research Group, Szeged, H-6720, Hungary Cited By :4 Export Date: 26 January 2024 CODEN: OCRPE Correspondence Address: Kiricsi, M.; Department of Biochemistry and Molecular Biology, Közép fasor 52, Hungary; email: kiricsim@bio.u-szeged.hu AB - Myofibroblasts (MFs) are present in healthy tissues and are also key components of the tumor microenvironment. In the present study a comparative analysis of MFs obtained from various gastrointestinal tumor tissues and from tumor‑adjacent normal tissues of cancer patients was performed, with the aim to evaluate differences in MF morphology, gene expression profile and function. The goal was to correlate the observed morphological and functional variations with the underlying genetic and epigenetic backgrounds. The mutation frequency of MFs was assessed by next generation sequencing. The transcript levels of cancer‑specific genes were determined by TaqMan array and quantitative polymerase chain reaction. Epigenetic modifications were analyzed by immunocytochemistry and western blotting. The migratory capacity of MFs was assessed by scratch assay, whereas matrix metalloproteinase expression and activity were obtained by quantitative polymerase chain reaction and zymography. The results of the present study demonstrate that MFs were present in an increased number and with altered morphology in tumor samples compared with the healthy tissue. Although the detected number of mutations in tumor‑associated and normal tissue‑derived MFs did not differ markedly, shifts in the level of specific acetylated and methylated histone proteins, namely decreased levels of trimethylated H3K9 and acetylated H4K16 were demonstrated in tumor‑associated MFs. Transcript levels of several tumor‑specific genes involved in metastasis, regulation of cellular growth, apoptosis, as well as in hypoxia‑angiogenesis were altered in tumor‑derived MF cultures. Increased mRNA levels were obtained and activity of matrix metalloproteases in tumor‑derived MFs and these cells also exhibited a higher migratory capacity compared with the normal MFs. In summary, the results of the present study indicate that tumor‑associated MFs display an altered phenotype compared with healthy tissue derived counterparts. The results imply that epigenetic rather than genetic alterations are associated with the development of the distinct expressional and functional features, which define this MF phenotype in the tumor microenvironment. LA - English DB - MTMT ER - TY - CONF AU - Borsos, Barbara Nikolett AU - Huliák, Ildikó AU - Majoros, Hajnalka AU - Újfaludi, Zsuzsanna AU - Gyenis, Ákos AU - Pukler, Peter AU - Boros, Imre Miklós AU - Pankotai, Tibor TI - Human p53 interacts with the elongating RNAPII complex and is required for the release of actinomycin D induced transcription blockage T2 - 9th Central European Genome Stability and Dynamics Meeting C1 - Varsó PY - 2018 PG - 1 UR - https://m2.mtmt.hu/api/publication/3414115 ID - 3414115 LA - English DB - MTMT ER - TY - CONF AU - Borsos, Barbara Nikolett AU - Majoros, Hajnalka AU - Huliák, Ildikó AU - Újfaludi, Zsuzsanna AU - Boros, Imre Miklós AU - Pankotai, Tibor ED - N, Stankovic ED - J, Schweiggert ED - A, Flotho TI - Beyond Initiation: Human P53 Plays Role in Transcription Elongation T2 - Ubiquitin and SUMO: From molecular mechanisms to system-wide responses PY - 2017 SP - 95 UR - https://m2.mtmt.hu/api/publication/3333842 ID - 3333842 LA - English DB - MTMT ER -