Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P50583 (asymmetrical)
 12,197 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

[Purpose] The main aim of this study was to identify the short-term effects of Kinesio taping (KT) on the static body alignment and overall balance function presented by the coordinate and foot balance in stroke patients. [Subjects and Methods] Thirty-eight stroke subjects were randomly allocated into the study groups. The kinematic analysis measured deviation or changes from standard body alignment and foot pressure by the human anatomy-based coordinates were examined using the Shisei Innovation System PA200 ver.9.0. [Results] The glabellas on the front view, larynx on the front view, rt. greater tubercle of the humerus (vertical changes), lt. greater tubercle of the humerus (vertical changes), posterior superior iliac spine, and greater trochanter (horizontal changes) showed statistically significant decreases, indicating dislocation from the axis center, after taping. [Conclusion] The clinical use of KT for stroke patients who have asymmetrical and imbalanced body posture could be an optimal therapeutic approach. Since more evidence based practices are needed, future studies should include large numbers of subjects and examine diverse KT application patterns.
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PMID:Immediate effects of kinesio taping on fixed postural alignment and foot balance in stroke patients. 2669 33

Senescence is accompanied with histones level alteration; however, the roles and the mechanisms of histone reduction in cellular senescence are largely unknown. Protein arginine methyltransferase 1 (PRMT1) is the major enzyme that generates monomethyl and asymmetrical dimethyl arginine. Here we showed that abrogation of PRMT1-mediated senescence was accompanied with decreasing histone H4 level. Consistently, under multiple classic senescence models, H4 decreasing was also been found prior to the other 3 core histones. Noticeably, asymmetric demethylation of histone H4 at arginine 3 (H4R3me2as), catalyzed by PRMT1, was decreased prior to histone H4. In addition, we showed that the PRMT1-mediated H4R3me2as maintained H4 stability. Reduction of H4R3me2as level increased the interaction between proteasome activator PA200 and histone H4, which catalyzes the poly-ubiquitin-independent degradation of H4. Moreover, H4 degradation promoted nucleosome decomposition, resulting in increased senescence-associated genes transcription. Significantly, H4 was restored by 3 well-informed anti-aging drugs (metformin, rapamycin, and resveratrol) much earlier than other senescence markers detected under H2O2-induced senescence. Thus, we uncovered a novel function of H4R3me2as in modulation of cellular senescence via regulating H4 stability. This finding also points to the value of histone H4 as a senescence indicator and a potential anti-aging drug screening marker.
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PMID:Arginine hypomethylation-mediated proteasomal degradation of histone H4-an early biomarker of cellular senescence. 3244 47