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22 results on '"Kalnina, Z."'

17. Effects of betahistine on patient-reported outcomes in routine practice in patients with vestibular vertigo and appraisal of tolerability: Experience in the OSVaLD study

Author

Benecke, H., Pérez-Garrigues, H., Bin Sidek, D., Uloziene, I., Kuessner, D., Sondag, E., Theeuwes, A., Boari, L., Chaves, A. G., Dorigueto, R. S., Ganança, F. F., Gonçalves, D. U., Hyppolito, M. A., Korn, G. P., Munhoz, M. S., Oliveira, J. A., Ajisafe, O., Angilleta, B., Bracalenti, I., Carlos, J. M., Dada, O., Ho, M., Kopyto, A., Laliberté, A., Lau, Y., Medina, X., Mercier, C., Nijmeh, P., Pietraszek, B., Roberge, C., Vincent, S., Zeitouni, A., Aras, I., Bencic, I., Bonifacic, M., Branica, S., Dovzak-Kokic, D., Drvis, P., Gortan, D., Grdinic, B., Grigic, J., Handzic, I., Ivkovic, M., Juros, V., Kovacic, J., Krstic, E., Lucin, Z., Maksimovic, Z., Maslovara, S., Rak, I., Resler Seks, A., Ries, M., Trotic, R., Rosenberg, A., Gaal, A., Badacsonyi, M., Balogh, G., Bandula, M., Baranya, E., Jeges, B., Brajnovits, T., Bucsai, A., Tubony, C., Csill, R., Czegledi, I., Olah, L., Draveczky, E., Vaszkun, L., Siro, E., Fain, A., Foth, A., Gerlinger, I., Gestelyi, G., Getachen, K., Ghayada, R., Gilincsek, L., Guth, I., Hegedus, E., Hegyi, I., Jofeju, E., Kerepesi, L., Krisan, I., Laszlo, K., Lorincz, T., Marisch, I., Mihalecz, K., Breznyan, M., Mori, I., Nagy, L., Manhalter, N., Pal, A., Papp, M., Peter, J., Prunk Eger, F., Radai, F., Szihalmy, I., Torma, E., Torok, K., Trencsenyi, G., Varga, E., Vincze, A., Vogel, R., Szakolczay, Z., Zsilinszky, Z., Rovo, Z., Tamas, L., Mester, B., Hudak, I., Toth, L., Merczel, A., Agarwal, V. K., Bhatia, R., Bhimani, B., Biswal, R. N., Biswas, A., Chowdary, V. S., Dhond, P., Dube, T. N., Gopakumar, G., Kansara, A., Khound, G., Kirtane, M. V., Mukherjee, A., Nagpal, T., Ravikumar, A., Reddy, V., Sampat, N., Shaikh, S., Sinha, S., Vaid, N., Valsangkar, S., Vasnoi, S., Vishwanathan, A., Blumberga, I., Bucina, B., Cakule, G., Demidova, L., Dolge, A., Dzirgause, M., Freimane, A., Fricbergs, J., Frolova, V., Ganus, I., Gavare, I., Grigs, V., Grusle, M., Levins, E., Veidule, I., Indrane, M., Saihulova, I., Jeca, A., Jegere, D., Ivanova, A., Kalitas, N., Kalnina, Z., Kanepe, K., Karlovska, M., Kokina, I., Krigere, R., Krisjane, D., Kukurane, S., Kundrate, G., Kukaine, S., Kukute, I., Lagzdina, L., Lapsa-Arenta, S., Madre, S., Matusevica, A., Mežale, I., Melnika, V., Mickevica, S., Morlata, N., Naudina, M. S., Nimroda, L., Norina, D., Opelte, V., Pavlovska, I., Priede, Z., Proskurna, T., Purina, J., Kamsa, I., Raumane, D., Kenina, V., Roska-Levina, D., Rozenbaha, A., Rozkalne, A., Ruta, A., Sendze, G., Silins, A., Skrupska, D., Skurule, I., Sokalska, A., Stepko, Z., Supe, I., Telezenko, I., Tretjaka, N., Turlaja, V., Uzbeka, I., Valucka, T., Vancans, J., Vasilevskis, U., Veinberga, V., Viba, Z., Vitkovska, M., Vitolina, A., Voitovica, L., Zigure, I., Zilite, I., Bakstiene, J., Balkaitiene, R., Basinskiene, V., Beinaraviciene, R., Bertasiene, Z., Bieliauskiene, I., Budrikiene, N., Butkus, A., Butkus, E., Butkus, R., Cholomskiene, V., Dainius, K., Degteriova, R., Deveikyte, A., Dirzauskiene, J., Einoriene, D., Gadeikis, E., Gircys, P., Grazeviciute, L., Ivaskevicius, A., Janciute, J., Jankauskiene, D., Jersova, J., Jociene, I., Jokimaitiene, J., Jukneliene, R., Kanapeckiene, V., Karaliene, V., Kazlauskas, A., Kicas, R., Kiskuniene, I., Kiudelis, A., Kizlaitiene, R., Kuriene, A., Lukaseviciene, N., Lukosaitis, A., Malikeniene, T., Markeleviciene, R., Mazonyte, S., Nadusauskiene, M., Narkeviciene, V., Naumcik, J., Navickiene, E., Pancyreva, I., Pavydyte, J., Persidskaja, O., Petkiniene, V. R., Petrileviciene, R., Petrosiute, B., Pliopliene, I., Puckiene, Z., Razukiene, J., Remeikiene, S., Rudzeviciene, E., Sceponaviciute, S., Scerbickiene, L., Sersniova, I., Sinkuniene, N., Skerneviciute, I., Snureviciute, V., Sostakiene, N., Tunkulas, E., Vitkauskiene, V., Zakarauskiene, R., Zorjan, N., Zurauskiene, R., Sani, A., Mohamad, A., Abdullah, A., Abdullah, B., Hassan, F., Selvarajah, G., See, G. B., Mann, G. S., Singh, H., Hj Ahmad, H. A., Hailani, I., Mohd Yusof, I., Gopalan Nair, K., Sathananthar, K. S., Singh, K., Saim, L., Abdul Ghani, M. H., Herg, M., Jalaludin, M. A., Md Daud, M. K., Khir Abdullah, M., Noor, N. H., Mohamed, N. R., Esa, N. K., Jusoh, N. M., Narayanan, P., Choo, P. K., Al Konee, R. A., Rajagopalan, R., Ismail, R., Mohd Hashim, S. S., Kumarasamy, S., Suan, T. L., Kamalden, T. M., Sang, T. T., Ambu, V. K., Leman, W. I., Abidin, Z. A., Salahuddin, Z., Yusof, Z., Burduk, P., Chmura, H., Czecior, E., Dabrowski, P., Diechota, L., Dietrich, G., Domagata, M., Durko, M., Frak, W., Franczuk-Gwiazda, M., Galbarczyk, D., Gaweowicz, J., Kabacinska, A., Kadej, G. Z., Kapuscinski, J., Kolebacz, B., Korpus-Kaminska, I., Lachowicz, M., Mielnik, E., Mihutka, S., Nilewski, J., Nouinska, E., Obzebowska-Karszania, Z., Oleksiak, M., Palasik, W., Paradowski, B., Paskal, J., Pospiech, L., Pres, K., Rynio, E., Schneider, K., Siger, M., Stoniewska-Piackus, M., Szczuto, J., Wilczynski, K., Wojcick, P., Woynowski, W., Tomasz Zatonski, Ziolkowska-Kochan, M., Zygadlo, E. N., Alaicescu, M., Augustin, A., Bădescu, A., Baltag, D., Bărbos, C., Becuşi, T., Bucan, L., Călăraşu, R., Cămpeanu, A., Chirileanhu, R. D., Comşa, G. I., Constantinescu, D., Cotulbea, S., Cozma, S., Cucoş, L., Docu, A. A., Dulămea, A., Enache, N., Ene, A., Fischer, T. S., Floare, L., Frăsineanu, A., Geană, I., Georgescu, E., Georgescu, M., Georgescu, M. J., Gherman, E., Hăncu, A., Iliescu, I., Ionescu-Mihăiţă, E. R., Ionita, E., Ionita, I., Iovănescu, D., Ladea, M., Loghin, V., Marceanu, L., Mărginean, I., Mariam, G., Marin, M., Mariş, C., Mârţu, D., Matcău, L., Muhlfay, G., Muică, L., Naconecinîi, D., Nirestean, A., Niţă, A., Niţu, L., Oană, N., Oancea, A., Oşanu, M., Panea, N., Pascu, A., Pastia, M., Pavel, R., Pendefunda, L., Petrutiu, S., Plăviţu, I., Poenaru, M., Popa, G. C., Popa, G., Popi, S., Popovivci, A., Prelipceanu, D., Radu, L., Rădulescu, L., Roceanu, A., Rusu, A., Sabău, M. S., Safta, D., Sarafoleanu, D., Stanciu, M., Stănciulescu, R., Ştefanache, F., Stefanescu, E. H., Szatmari, S., Szocs, Tomescu, L., Tudorache, B., Tudose, C., Ursu, C., Vasilescu, L., Vasu, I., Vioreanu, M., Zaboş, D., Zaharia, C., Zainea, V., Zarie, G., Alekseeva, N., Amelin, A., Artemova, I., Batysheva, T., Bobyreva, S., Boyko, A., Buldakova, N., Ganzhula, P., Gaponova, O., Hanevich, T., Hozova, A., Isachenkova, O., Ismailov, A., Zhuravleva, E., Kostenko, E., Lilenko, S., Lisenker, L., Makarova, G., Manevich, T., Matsnev, E., Melnikov, O., Morozova, S., Nesterova, O., Nikulina, I., Otcheskaya, O., Pivovarova, V., Rotor, L., Rylskiy, A., Shalabanova, I., Shinkarev, S., Sorokoumov, V., Vdovichenko, T., Vinetskiy, Y., Vostricova, I., Zadorozhnaya, T., Breznik Farkas, B., Felbabic, J., Geczy Buljovcic, B., Grad, A., Hoenigman, B., Kurent, Z., Krek, B. P., Rok, B., Spindler, M., Vatovec, J., Zorn, A., Zupan, L., Aguila, A. A., Caballero, B. M., Garcia, V. C., Cruellas, T. F., Munoz, P. C., Domenech, J. I., Donderis, S. J., Estevez, G. M., Pallas, P. E., Grani, M. F., Gonzalez, C. F., Galindo, O. J., Garcia, A. A., Garcia, G. B., Gonzalez, G. I., Hernandez Ade, S., Hijano, E. R., Lopez, E. J., Saiz, A. J., Izquierdo, L. J., Perez, L. L., Paya, P. L., Mesa, M. M., Molina, P. M., Navarrete, A. L., Marti, G. L., Melgarejo, M. F., Orts, A. M., Suarez, G. P., Perez, M. P., Perez, G. H., Perez, G. V., Rodriguez, R. S., Santos, P. S., Soto, V. A., Malluguiza, C. J., Ramirez, L. R., Jimenez, M. R., Barona Guzmán, R., Escamilla, C. Y., Saiz, M. V., Gisbert, A. F., Provedo, P. C., Pardo, S. E., Alemán, L. O., Martin, S. E., and Marco, A. J.

19. High-Affinity NIR-Fluorescent Inhibitors for Tumor Imaging via Carbonic Anhydrase IX.

Author

Žvinys G, Petrosiute A, Zakšauskas A, Zubrienė A, Ščerbavičienė A, Kalnina Z, Čapkauskaitė E, Juozapaitienė V, Mickevičiu Tė A, Shubin K, Grincevičienė Š, Raišys S, Tars K, Matulienė J, and Matulis D

Subjects
Humans, Animals, Mice, HeLa Cells, Neoplasms diagnostic imaging, Mice, Nude, Sulfonamides chemistry, Infrared Rays, Carbonic Anhydrases metabolism, Optical Imaging methods, Carbonic Anhydrase IX metabolism, Carbonic Anhydrase IX antagonists & inhibitors, Fluorescent Dyes chemistry, Carbonic Anhydrase Inhibitors chemistry, Carbonic Anhydrase Inhibitors pharmacology, Carbonic Anhydrase Inhibitors therapeutic use, Antigens, Neoplasm metabolism, Antigens, Neoplasm analysis
Abstract

Tumor imaging and delivery of therapeutic agents may be achieved by designing high-affinity and high-selectivity compounds recognizing a tumor cell-expressing biomarker, such as carbonic anhydrase IX (CA IX). The CAIX, overexpressed in many hypoxic solid tumors, helps adjust to the energy requirements of the hypoxic environment, reduces intracellular acidification, and participates in the metastatic invasion of adjacent tissues. Here, we designed a series of sulfonamide compounds bearing CAIX-recognizing, high-affinity, and high-selectivity groups conjugated via a PEG linker to near-infrared (NIR) fluorescent probes used in the clinic for optically guided cancer surgery. We determined compound affinities for CAIX and other 11 catalytically active CA isozymes by the thermal shift assay and showed that the affinity K d value of CAIX was in the subnanomolar range, hundred to thousand-fold higher than those of other CA isozymes. Similar affinities were also observed for CAIX expressed on the cancer cell surface in live HeLa cell cultures, as determined by the competition assay. The NIR-fluorescent compounds showed excellent properties in visualizing CAIX-positive tumors but not CAIX-negative knockout tumors in a nude mice xenograft model. These compounds would therefore be helpful in optically guided cancer surgery and could potentially be developed for anticancer treatment by radiotherapy.

Published
2024
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20. Bacteriophage-Derived Double-Stranded RNA Exerts Anti-SARS-CoV-2 Activity In Vitro and in Golden Syrian Hamsters In Vivo.

Author

Vaivode K, Verhovcova I, Skrastina D, Petrovska R, Kreismane M, Lapse D, Kalnina Z, Salmina K, Rubene D, and Pjanova D

Abstract

Bacteriophage-derived dsRNA, known as Larifan, is a nationally well-known broad-spectrum antiviral medication. This study aimed to ascertain the antiviral activity of Larifan against the novel SARS-CoV-2 virus. Larifan's effect against SARS-CoV-2 in vitro was measured in human lung adenocarcinoma (Calu3) and primary human small airway epithelial cells (HSAEC), and in vivo in the SARS-CoV-2 infection model in golden Syrian hamsters. Larifan inhibited SARS-CoV-2 replication both in vitro and in vivo. Viral RNA copy numbers and titer of infectious virus in the supernatant of Calu3 cells dropped significantly: p = 0.0296 and p = 0.0286, respectively. A reduction in viral RNA copy number was also observed in HSAEC, especially when Larifan was added before infection ( p = 0.0218). Larifan markedly reduced virus numbers in infected hamsters' lungs post-infection, with a more pronounced effect after intranasal administration ( p = 0.0032). The administration of Larifan also reduced the amount of infections virus titer in the lungs ( p = 0.0039). Improvements in the infection-induced pathological lesion severity in the lungs of animals treated with Larifan were also demonstrated. The inhibition of SARS-CoV-2 replication in vitro and the reduction in the viral load in the lungs of infected hamsters treated with Larifan alongside the improved lung histopathology suggests a potential use of Larifan in also controlling the COVID-19 disease in humans., Competing Interests: The authors declare no conflict of interest.

Published
2022
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21. DNA damage causes TP53-dependent coupling of self-renewal and senescence pathways in embryonal carcinoma cells.

Author

Jackson TR, Salmina K, Huna A, Inashkina I, Jankevics E, Riekstina U, Kalnina Z, Ivanov A, Townsend PA, Cragg MS, and Erenpreisa J

Subjects
Antineoplastic Agents, Phytogenic pharmacology, Aurora Kinase B, Aurora Kinases, Autophagy, Cell Line, Tumor, Checkpoint Kinase 2, Cyclin-Dependent Kinase Inhibitor p16 biosynthesis, Cyclin-Dependent Kinase Inhibitor p21 biosynthesis, Cyclin-Dependent Kinase Inhibitor p21 genetics, Embryonal Carcinoma Stem Cells metabolism, Etoposide pharmacology, Female, G2 Phase Cell Cycle Checkpoints drug effects, Histones biosynthesis, Humans, Octamer Transcription Factor-3 biosynthesis, Octamer Transcription Factor-3 genetics, Ovarian Neoplasms, Phosphorylation, Protein Serine-Threonine Kinases biosynthesis, RNA Interference, RNA, Small Interfering, Rad51 Recombinase biosynthesis, Tumor Suppressor Protein p53 genetics, Up-Regulation, beta-Galactosidase biosynthesis, Cellular Senescence physiology, DNA Damage genetics, DNA Repair physiology, Tumor Suppressor Protein p53 metabolism
Abstract

Recent studies have highlighted an apparently paradoxical link between self-renewal and senescence triggered by DNA damage in certain cell types. In addition, the finding that TP53 can suppress senescence has caused a re-evaluation of its functional role in regulating these outcomes. To investigate these phenomena and their relationship to pluripotency and senescence, we examined the response of the TP53-competent embryonal carcinoma (EC) cell line PA-1 to etoposide-induced DNA damage. Nuclear POU5F1/OCT4A and P21CIP1 were upregulated in the same cells following etoposide-induced G 2M arrest. However, while accumulating in the karyosol, the amount of OCT4A was reduced in the chromatin fraction. Phosphorylated CHK2 and RAD51/γH2AX-positive nuclear foci, overexpression of AURORA B kinase and moderate macroautophagy were evident. Upon release from G 2M arrest, cells with repaired DNA entered mitoses, while the cells with persisting DNA damage remained at this checkpoint or underwent mitotic slippage and gradually senesced. Reduction of TP53 using sh- or si-RNA prevented the upregulation of OCT4A and P21CIP1 and increased DNA damage. Subsequently, mitoses, micronucleation and senescence were all enhanced after TP53 reduction with senescence confirmed by upregulation of CDKN2A/P16INK4A and increased sa-β-galactosidase positivity. Those mitoses enhanced by TP53 silencing were shown to be multicentrosomal and multi-polar, containing fragmented and highly deranged chromosomes, indicating a loss of genome integrity. Together, these data suggest that TP53-dependent coupling of self-renewal and senescence pathways through the DNA damage checkpoint provides a mechanism for how embryonal stem cell-like EC cells safeguard DNA integrity, genome stability and ultimately the fidelity of self-renewal.

Published
2013
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22. Alterations of pre-mRNA splicing in cancer.

Author

Kalnina Z, Zayakin P, Silina K, and Linē A

Subjects
Exons, Humans, Introns, RNA Precursors metabolism, RNA Splicing
Abstract

Recent genomewide analyses of alternative splicing (AS) indicate that up to 70% of human genes may have alternative splice forms, suggesting that AS together with various posttranslational modifications plays a major role in the production of proteome complexity. Splice-site selection under normal physiological conditions is regulated in the developmental stage in a tissue type-specific manner by changing the concentrations and the activity of splicing regulatory proteins. Whereas spliceosomal errors resulting in the production of aberrant transcripts rarely occur in normal cells, they seem to be an intrinsic property of cancer cells. Changes in splice-site selection have been observed in various types of cancer and may affect genes implicated in tumor progression (for example, CD44, MDM2, and FHIT) and in susceptibility to cancer (for example, BRCA1 and APC). Splicing defects can arise from inherited or somatic mutations in cis-acting regulatory elements (splice donor, acceptor and branch sites, and exonic and intronic splicing enhancers and silencers) or variations in the composition, concentration, localization, and activity of regulatory proteins. This may lead to altered efficiency of splice-site recognition, resulting in overexpression or down-regulation of certain splice variants, a switch in splice-site usage, or failure to recognize splice sites correctly, resulting in cancer-specific splice forms. At least in some cases, changes in splicing have been shown to play a functionally significant role in tumorigenesis, either by inactivating tumor suppressors or by gain of function of proteins promoting tumor development. Moreover, cancer-specific splicing events may generate novel epitopes that can be recognized by the host's immune system as cancer specific and may serve as targets for immunotherapy. Thus, the identification of cancer-specific splice forms provides a novel source for the discovery of diagnostic or prognostic biomarkers and tumor antigens suitable as targets for therapeutic intervention., ((c) 2005 Wiley-Liss, Inc.)

Published
2005
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