To select congenial pairs between donor-pig and recipient-human for the future xenotransplantation, the levels of xeno-IgM natural antibodies (NAb) were analyzed in healthy subjects and hemodialysis patients by ELISA tests, which target swine-derived crude endothelial cells (P16N) or proteins (thyroglobulin; TG). The total IgM concentration was lower in hemodialysis patients than in healthy subjects, but there was no difference in IgM NAb titer between the two groups. Individuals with non-B blood types (A, O) exibited significantly higher IgM NAb titer compared with those with B blood types (B, AB). A blood type individuals showed higher killing activity against P16N than those with B, AB or O types with a statistical significance. Sera from A blood type, after being absorbed with red blood cells (RBC) from B blood type, decreased their IgM titer against TG to the level of sera from B blood type. Meanwhile, sera from A blood type significantly decreased hemagglutinin titer against B-RBC after passage through a TG-coated affinity column. We conclude that human anti-B-RBC and anti-Pig xeno NAb have certain common binding epitopes, which might be a branched B carbohydrate structure.
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J Med Internet Res
January 2025
Department of Internal Medicine, Hospital Clinic, Institut d'Investigacio Biomèdica August Pi i Sunyer, Barcelona, Spain.
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PTC Therapeutics Germany GmbH, Frankfurt, Germany.
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View Article and Find Full Text PDFDiabetes Care
February 2025
Division of Blood Disorders and Public Health Genomics, Centers for Disease Control and Prevention, Atlanta, GA.
Objective: The goal of this study was to assess the additive value of considering type 2 diabetes (T2D) polygenic risk score (PRS) in addition to family history for T2D prediction.
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Anesthesiology
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Anesthesia and critical care department, Amiens Hospital University, F-80054 Amiens, France.
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View Article and Find Full Text PDFSci Adv
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Laboratory of Mitochondrial Biology and Metabolism, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD, USA.
Although lipid-derived acetyl-coenzyme A (CoA) is a major carbon source for histone acetylation, the contribution of fatty acid β-oxidation (FAO) to this process remains poorly characterized. To investigate this, we generated mitochondrial acetyl-CoA acetyltransferase 1 (ACAT1, distal FAO enzyme) knockout macrophages. C-carbon tracing confirmed reduced FA-derived carbon incorporation into histone H3, and RNA sequencing identified diminished interferon-stimulated gene expression in the absence of ACAT1.
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