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The demand for processing vast volumes of data has surged dramatically due to the advancement of machine learning technology. Large-scale data processing necessitates substantial computational resources, prompting individuals and enterprises to turn to cloud services. Accompanying this trend is a growing concern regarding data leakage and misuse. Homomorphic encryption (HE) is one solution for safeguarding data privacy, enabling encrypted data to be processed securely in the cloud. However, the encryption and decryption routines of some HE schemes require considerable computational resources, presenting non-trivial work for clients. In this paper, we propose an outsourced decryption protocol for the prevailing RLWE-based fully homomorphic encryption schemes. The protocol splits the original decryption into two routines, with the computationally intensive part executed remotely by the cloud. Its security relies on an invariant of the NTRU-search problem with a newly designed blinding key distribution. Cryptographic analyses are conducted to configure protocol parameters across varying security levels. Our experiments demonstrate that the proposed protocol achieves up to a 67% acceleration in the client-side computation, accompanied by a 50% reduction in space usage. [ABSTRACT FROM AUTHOR]

Background Statins are potent inhibitors of cholesterol biosynthesis and are clinically beneficial in preventing cardiovascular diseases, however, the therapeutic utility of these drugs is limited by myotoxicity. Here, we explored the mechanism of statin-mediated activation of ERK5 in the human endothelium with the goal of identifying compounds that confer endothelial protection but are nontoxic to muscle. Methods An ERK5-one hybrid luciferase reporter transfected into COS-7 cells with pharmacological and molecular manipulations dissected the signaling pathway leading to statin activation of ERK5. qRT-PCR of HUVEC cells documented the transcriptional activation of endothelial-protective genes. Lastly, morphological and cellular ATP analysis, and induction of atrogin-1 in C2C12 myotubes were used to assess statin-induced myopathy. Results Statin activation of ERK5 is dependent on the cellular reduction of GGPPs. Furthermore, we found that the combination of FTI-277 (inhibitor of farnesyl transferase) and GGTI-298 (inhibitor of geranylgeranyl transferase I) mimicked the statin-mediated activation of ERK5. FTI-277 and GGTI-298 together recapitulated the beneficial effects of statins by transcriptionally upregulating anti-inflammatory mediators such as eNOS, THBD, and KLF2. Finally, C2C12 skeletal myotubes treated with both FTI-277 and GGTI-298 evoked less morphological and cellular changes recognized as biomarkers of statin-associated myopathy. Conclusions Statin-induced endothelial protection and myopathy are mediated by distinct metabolic intermediates and co-inhibition of farnesyl transferase and geranylgeranyl transferase I confer endothelial protection without myopathy. General significance The combinatorial FTI-277 and GGTI-298 drug regimen provides a promising alternative avenue for endothelial protection without myopathy. [ABSTRACT FROM AUTHOR]