Background: In SWAN, we showed that accelerated loss of bone mineral density (BMD) begins 1 year before the final menstrual period (FMP) to 2 years after the FMP and slows thereafter. However, the risk of fracture depends on both BMD and bone geometry. The hip structural analysis (HSA) measures important geometric properties of bone. Changes in HSA parameters across the menopausal transition have not been previously assessed.
Methods: The current analysis uses data from SWAN, 5 years before to 5 years after FMP (N = 900, Age (mean(SD)) = 46.85(2.60), 44% White). HSA parameters at the femoral narrow neck were obtained from 2D DXA scans and normalized to baseline values. FMP was determined from annual interviews. Changes in HSA were assessed over 3 periods, 5 to 2 years before FMP (pre-transmenopausal), 2 years before to 1 years after FMP (transmenopausal), 1 to 5 years after FMP (postmenopausal). Mixed linear models with random slopes were used to estimate the rate of change in HSA parameters relative to FMP.
Results: Loss of BMD, cross-sectional area (CSA), and section modulus (SM) and increases in outer diameter (OD) were greatest in the transmenopausal period (p for all<0.05). Changes continued in the postmenopausal period but were not statistically significant. The cumulative percentage changes over 10 years in BMD (-10.67%), CSA (-9.01), SM (-7.03) and OD (+1.95) were statistically significant.
Conclusion: Changes in hip geometry across the menopause transition parallel changes in BMD and provide insight into mechanisms that may increase risk of fragility fracture.
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http://dx.doi.org/10.1016/j.bone.2019.02.016 | DOI Listing |
Biomedicines
December 2024
Cardiovascular Pathophysiology Group, Institute of Biomedicine of Seville-IBiS, University of Seville/Hospital Universitario Virgen de Rocio/CSIC, 41013 Seville, Spain.
Unlabelled: Echocardiographic myocardial strain is crucial for early detection of anthracycline-induced cardiotoxicity, particularly in patients at moderate or high risk.
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ACS Appl Bio Mater
January 2025
Department of Chemistry, Indian Institute of Technology Palakkad, Palakkad, Kerala 678 623, India.
The aggregation of proteins, peptides and amino acids has been a keen subject of interest owing to their implications in metabolic disorders. In this work, we investigated the self-aggregation of the unmodified aromatic amino acid l-tryptophan (Trp) into unusual spherical microstructures. Using fluorescence spectroscopy and field emission scanning electron microscopy (FE-SEM), we detail the time-dependent transformation of monomeric tryptophan into spherical aggregates with distinct fluorescence characteristics (λ = 345 nm, λ = 430 nm) compared to the monomer.
View Article and Find Full Text PDFAm J Clin Exp Immunol
December 2024
Department of Internal Medicine, University of Michigan Ann Arbor, MI 48109, USA.
Since the COVID-19 pandemic, a significant number of pediatric leukemia patients have shown to have also contracted COVID-19 several weeks or months prior to the development of their cancer. Current research indicates the expression of MDA5, encoded by , is associated with increased immunity to COVID-19 in children. Children are also known to have a much lower risk of developing leukemia.
View Article and Find Full Text PDFJ Med Chem
January 2025
Department of Organic Chemistry and Technology, Budapest University of Technology and Economics, Műegyetem rkp. 3, H-1111Budapest, Hungary.
The binding ability of human serum albumin (HSA) on active pharmaceutical ingredients (APIs) is one of the most important parameters in the early stages of drug discovery. In this study, an immobilized HSA-based tool was developed for the rapid and easy in vitro screening of API binding. The work explored the serious incompleteness in the identification of HSA used for in vitro screening published in the last five years.
View Article and Find Full Text PDFArch Biochem Biophys
January 2025
Department of Biochemistry, J.N.M.C., Faculty of Medicine, Aligarh Muslim University, Aligarh 202002, U.P., India. Electronic address:
Glycation and aggregation of proteins have garnered more interest in recent years. Glycation leads to the formation of protein aggregates and advanced glycation ends (AGEs) that play crucial roles within several pathological conditions. The objective of our study is to gain a deeper understanding of the formation of AGEs and aggregates of human serum albumin (HSA) in the presence of methylglyoxal and the protective effects of the phytochemical berberine.
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