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1.
Magn Reson Imaging ; 111: 15-20, 2024 Sep.
Artículo en Inglés | MEDLINE | ID: mdl-38579974

RESUMEN

BACKGROUND: In patients who have difficulty holding their breath, a free breathing (FB) respiratory-triggered (RT) bSSFP cine technique may be used. However, this technique may have inferior image quality and a longer scan time than breath-hold (BH) bSSFP cine acquisitions. This study examined the effect of an audiovisual breathing guidance (BG) system on RT bSSFP cine image quality, scan time, and ventricular measurements. METHODS: This study evaluated a BG system that provides audiovisual instructions and feedback on the timing of inspiration and expiration to the patient during image acquisition using input from the respiratory bellows to guide them toward a regular breathing pattern with extended end-expiration. In this single-center prospective study in patients undergoing a clinical cardiac magnetic resonance examination, a ventricular short-axis stack of bSSFP cine images was acquired using 3 techniques in each patient: 1) FB and RT (FBRT), 2) BG system and RT (BGRT), and 3) BH. The 3 acquisitions were compared for image quality metrics (endocardial edge definition, motion artifact, and blood-to-myocardial contrast) scored on a Likert scale, scan time, and ventricular volumes and mass. RESULTS: Thirty-two patients (19 females; median age 21 years, IQR 18-32) completed the study protocol. For scan time, BGRT was faster than FBRT (163 s vs. 345 s, p < 0.001). Endocardial edge definition, motion artifact, and blood-to-myocardial contrast were all better for BGRT than FBRT (p < 0.001). Left ventricular (LV) end-systolic volume (ESV) was smaller (3%, p = 0.02) and LV ejection fraction (EF) was larger (0.5%, p = 0.003) with BGRT than with FBRT. There was no significant difference in LV end-diastolic volume (EDV), LV mass, right ventricular (RV) EDV, RV ESV, and RV EF. Scan times were shorter for BGRT compared to BH. Endocardial edge definition and blood-to-myocardial contrast were better for BH than BGRT. Compared to BH, the LV EDV, LV ESV, RV EDV, and RV ESV were mildly smaller (all differences <7%) for BGRT. CONCLUSIONS: The addition of a BG system to RT bSSFP cine acquisitions decreased the scan time and improved image quality. Further exploration of this BG approach is warranted in more diverse populations and with other free breathing sequences.


Asunto(s)
Imagen por Resonancia Cinemagnética , Humanos , Imagen por Resonancia Cinemagnética/métodos , Femenino , Masculino , Adulto , Estudios Prospectivos , Respiración , Persona de Mediana Edad , Técnicas de Imagen Sincronizada Respiratorias/métodos , Corazón/diagnóstico por imagen , Ventrículos Cardíacos/diagnóstico por imagen , Contencion de la Respiración , Artefactos , Reproducibilidad de los Resultados , Recursos Audiovisuales , Adulto Joven
2.
Sci Rep ; 11(1): 10794, 2021 05 24.
Artículo en Inglés | MEDLINE | ID: mdl-34031459

RESUMEN

Iron-sulfur (Fe-S) proteins play essential roles in all living organisms. The gastric pathogen Helicobacter pylori relies exclusively on the NIF system for biosynthesis and delivery of Fe-S clusters. Previously characterized components include two essential proteins, NifS (cysteine desulfurase) and NifU (scaffold protein), and a dispensable Fe-S carrier, Nfu. Among 38 proteins previously predicted to coordinate Fe-S clusters, two proteins, HP0207 (a member of the Nbp35/ApbC ATPase family) and HP0277 (previously annotated as FdxA, a member of the YfhL ferredoxin-like family) were further studied, using a bacterial two-hybrid system approach to identify protein-protein interactions. ApbC was found to interact with 30 proteins, including itself, NifS, NifU, Nfu and FdxA, and alteration of the conserved ATPase motif in ApbC resulted in a significant (50%) decrease in the number of protein interactions, suggesting the ATpase activity is needed for some ApbC-target protein interactions. FdxA was shown to interact with 21 proteins, including itself, NifS, ApbC and Nfu, however no interactions between NifU and FdxA were detected. By use of cross-linking studies, a 51-kDa ApbC-Nfu heterodimer complex was identified. Attempts to generate apbC chromosomal deletion mutants in H. pylori were unsuccessful, therefore indirectly suggesting the hp0207 gene is essential. In contrast, mutants in the fdxA gene were obtained, albeit only in one parental strain (26695). Taken together, these results suggest both ApbC and FdxA are important players in the H. pylori NIF maturation system.


Asunto(s)
Helicobacter pylori/metabolismo , Proteínas Hierro-Azufre/metabolismo , Proteínas Bacterianas/metabolismo , Fijación del Nitrógeno , Mapas de Interacción de Proteínas , Técnicas del Sistema de Dos Híbridos
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