Please use this identifier to cite or link to this item: http://dx.doi.org/10.25673/120463
Title: Hyperthermia augments the H1-histamine receptor-mediated force in the human atrium
Author(s): Pham, Thanh Hoai
Grundig, Peter
Hofmann, BrittLook up in the Integrated Authority File of the German National Library
Kirchhefer, UweLook up in the Integrated Authority File of the German National Library
Neumann, JoachimLook up in the Integrated Authority File of the German National Library
Gergs, UlrichLook up in the Integrated Authority File of the German National Library
Issue Date: 2025
Type: Article
Language: English
Abstract: It was unknown whether hyperthermia increased the efficacy of histamine to raise the force of cardiac contractions via human H1-histamine receptors. To that end, we measured the force in isolated human atrial preparations (HAPs) excised from the right atrium of patients who underwent cardiac surgery due to severe two- or three-vessel coronary heart disease. For comparison, we also measured the force in paced (1 Hz) left and spontaneously beating right atrial preparations of transgenic mice overexpressing cardiac human H1-histamine receptors (H1-TG). Histamine (100 µM) was less efficient in raising the force in left atrial preparations from H1 TG mouse atria under hyperthermia than under hypothermia. Oppositely, histamine was more efficient in augmenting force during hyperthermia than during hypothermia in isolated electrically stimulated (1 Hz) HAPs. In sum, the contractile response to activation of H1-histamine receptor in H1-TG mice and in HAPs are opposite with regard to hyperthermia dependence. In patients with fever, histamine might thus be important, to preserve cardiac contractile function as a compensatory mechanism.
URI: https://opendata.uni-halle.de//handle/1981185920/122419
http://dx.doi.org/10.25673/120463
Open Access: Open access publication
License: (CC BY 4.0) Creative Commons Attribution 4.0(CC BY 4.0) Creative Commons Attribution 4.0
Journal Title: International journal of molecular sciences
Publisher: Molecular Diversity Preservation International
Publisher Place: Basel
Volume: 26
Issue: 14
Original Publication: 10.3390/ijms26146842
Appears in Collections:Open Access Publikationen der MLU

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