![]() ![]() ![]() However, compared to unpurified myoblasts, CD34 +/CD90 − cells expressed greater amounts of endothelium-specific mRNAs and were, therefore, selected for transplantation experiments. Skeletal muscle biopsies obtained from 39 patients were sorted by flow cytometry which generated three populations (CD90 +/CD34 −, CD34 +/CD90 −, CD90 −/CD34 −) expressing similar levels of cardiac (Nkx2.5, cTn-T, cTn-I, Cx43) and skeletal muscle (Myf-5, MyoD, myogenin) mRNAs, as assessed by quantitative reverse transcriptase–PCR. Since murine skeletal muscle was reported to harbor cardiac precursor cells, we assessed whether similar cells exist in man. PMID 31588002.The limited plasticity of adult muscle- or bone marrow– derived stem cells intended for cardiac regeneration impedes their conversion into cardiomyocytes. "Neuronal O-GlcNAcylation Improves Cognitive Function in the Aged Mouse Brain". ^ Wheatley EG, Albarran E, White CW 3rd, Bieri G, Sanchez-Diaz C, Pratt K, Snethlage CE, Ding JB, Villeda SA (2019)."Protein O-GlcNAcylation in diabetes and diabetic complications". "Cross talk between O-GlcNAcylation and phosphorylation: roles in signaling, transcription, and chronic disease". ^ a b c d Hart GW, Slawson C, Ramirez-Correa G, Lagerlof O (2011)."N-Acetylglucosamine Inhibits T-helper 1 (Th1)/T-helper 17 (Th17) Cell Responses and Treats Experimental Autoimmune Encephalomyelitis". ^ Grigorian A, Araujo L, Naidu NN, Place DJ, Choudhury B, Demetriou M (2011)."Inhibition of elastase enzyme release from human polymorphonuclear leukocytes by N-acetyl-galactosamine and N-acetyl-glucosamine". Wheat germ agglutinin, a plant lectin that binds to this substrate.When O-GlcNAcylation was increased in the hippocampus of aged mice, spatial learning and memory improved. O-GlcNAcylation decline in the brain with age is associated with cognitive decline. Increased O-GlcNAcylation due to hyperglycemia is evidently a dysfunctional form of O-GlcNAcylation. Hyperglycemia increases O-GlcNAcylation, leading to insulin resistance. O-GlcNAcylation most often occurs on chromatin proteins, and is often seen as a response to stress. In fact, O-GlcNAcylation and phosphorylation often compete for the same serine/threonine sites. Comparable to phosphorylation, addition or removal of N-acetylglucosamine is a means of activating or deactivating enzymes or transcription factors. O-GlcNAcylation is the process of adding a single N-acetylglucosamine sugar to the serine or threonine of a protein. It has been proposed as a treatment for autoimmune diseases and recent tests have claimed some success. GlcNAc has been reported to be an inhibitor of elastase release from human polymorphonuclear leukocytes (range 8–17% inhibition), however this is much weaker than the inhibition seen with N-acetylgalactosamine (range 92–100%). Polymerized with glucuronic acid, it forms hyaluronan. It is the main component of the radulas of mollusks, the beaks of cephalopods, and a major component of the cell walls of most fungi. GlcNAc is the monomeric unit of the polymer chitin, which forms the exoskeletons of arthropods like insects and crustaceans. This layered structure is called peptidoglycan (formerly called murein). It is part of a biopolymer in the bacterial cell wall, which is built from alternating units of GlcNAc and N-acetylmuramic acid (MurNAc), cross-linked with oligopeptides at the lactic acid residue of MurNAc. It is significant in several biological systems. It is a secondary amide between glucosamine and acetic acid. N-Acetylglucosamine (GlcNAc) is an amide derivative of the monosaccharide glucose. ![]()
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