ORM-3819 promotes cardiac contractility through Ca2+ sensitization in combination with selective PDE III inhibition, a novel approach to inotropy

Autor: Ágnes Végh, István Édes, Tia Sorsa, Nagy Laszlo, Julius Gy. Papp, Jouko Levijoki, Attila Tóth, Zoltán Papp, Piero Pollesello, Heimo Haikala, Szabolcs Szilágyi

This study is the first pharmacological characterization of the novel chemical entity, ORM-3819 (L-6-{4-[N'-(4-Hydroxi-3-methoxy-2-nitro-benzylidene)-hydrazino]-phenyl}-5-methyl-4,5-dihydro-2H-pyridazin-3-one), focusing primarily on its cardiotonic e

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1796213fd1796066d34f2983fb3b5996

Conformations of the regulatory domain of cardiac troponin C examined by residual dipolar couplings

Autor: Piero Pollesello, Arto Annila, Sami Heikkinen, Torbjörn Drakenberg, Tia Sorsa, Perttu Permi, Ilkka Kilpeläinen, Carola Tilgmann, Kimmo Pääkkönen

Publikováno v: European Journal of Biochemistry. 267:6665-6672

Conformations of the regulatory domain of cardiac troponin C (cNTnC) were studied by means of residual dipolar couplings measured from samples dissolved in dilute liquid crystals. Changes in the main chain HN residual dipolar couplings revealed a con

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::fab5870187f041076a0003a1f486cb75
https://doi.org/10.1046/j.1432-1327.2000.01763.x

Solution Structure and Main Chain Dynamics of the Regulatory Domain (Residues 1–91) of Human Cardiac Troponin C

Autor: Piero Pollesello, Tia Sorsa, Piia Karisola, Torbjörn Drakenberg, Ismo Ulmanen, Ilkka Kilpeläinen, Kimmo Pääkkönen, Arto Annila, Carola Tilgmann

Publikováno v: Journal of Biological Chemistry. 273:15633-15638

The three-dimensional structure of calcium-loaded regulatory, i.e. N-terminal, domain (1-91) of human cardiac troponin C (cNTnC) was determined by NMR in water/trifluoroethanol (91:9 v/v) solution. The single-calcium-loaded cardiac regulatory domain

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f25d9a0128746db91a5c79434c79512a
https://doi.org/10.1074/jbc.273.25.15633

Interaction of levosimendan with cardiac troponin C in the presence of cardiac troponin I peptides

Autor: Ilkka Kilpeläinen, Tia Sorsa, Torbjörn Drakenberg, Perttu Permi, Piero Pollesello

Publikováno v: Journal of molecular and cellular cardiology. 35(9)

The interaction between troponin C (TnC) and troponin I (TnI) is essential for the regulation of muscle contraction. There are several binding sites for TnI on TnC that are differentially occupied depending on the phase of the contraction/relaxation

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::00a315a01c04c0a8dd080ae43515b691
https://pubmed.ncbi.nlm.nih.gov/12967622

Further evidence for the cardiac troponin C mediated calcium sensitization by levosimendan:Structure-response and binding analysis with analogs of levosimendan

Autor: Arto Annila, Jouko Levijoki, Piero Pollesello, Tia Sorsa, Ilkka Kilpeläinen, Heimo Haikala, Carola Tilgmann, Juha Kaivola

Publikováno v: Levijoki, J, Pollesello, P, Kaivola, J, Tilgmann, C, Sorsa, T, Annila, A, Kilpeläinen, I & Haikala, H 2000, ' Further evidence for the cardiac troponin C mediated calcium sensitization by levosimendan : Structure-response and binding analysis with analogs of levosimendan ', Journal of Molecular and Cellular Cardiology, vol. 32, no. 3, pp. 479-491 . https://doi.org/10.1006/jmcc.1999.1093

Levosimendan, an inodilatory drug discovered using troponin C as a target protein, has a cardiac effect deriving from the calcium sensitization of contractile proteins. The aim of this study was to give further evidence that levosimendan binds to car

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4fb308b99da8bdb193679b6ab7ac0ad8
https://cris.vtt.fi/en/publications/332f2059-7fa7-4b3f-aa23-c657d98a674c