Accelerating HE Operations from Key Decomposition Technique

Lattice-based homomorphic encryption (HE) schemes are based on the noisy encryption technique, where plaintexts are masked with some random noise for security. Recent advanced HE schemes rely on a decomposition technique to manage the growth of noise, which involves a conversion of a ciphertext entry into a short vector followed by multiplication with an evaluation key. Prior to this work, the decomposition procedure turns out to be the most time-consuming part, as it requires discrete Fourier transforms (DFTs) over the base ring for efficient polynomial arithmetic. In this paper, an expensive decomposition operation over a large modulus is replaced with relatively cheap operations over a ring of integers with a small bound. Notably, the cost of DFTs is reduced from quadratic to linear with the level of a ciphertext without any extra noise growth. We demonstrate the implication of our approach by applying it to the key-switching procedure. Our experiments show that the new key-switching method achieves a speedup of 1.2--2.3 or 2.1--3.3 times over the previous method, when the dimension of a base ring is $2^{15}$ or $2^{16}$, respectively

Potential role and mechanism of IFN-gamma inducible protein-10 on receptor activator of nuclear factor kappa-B ligand (RANKL) expression in rheumatoid arthritis

Introduction IFN-gamma inducible protein-10 (CXCL10), a member of the CXC chemokine family, and its receptor CXCR3 contribute to the recruitment of T cells from the blood stream into the inflamed joints and have a crucial role in perpetuating inflammation in rheumatoid arthritis (RA) synovial joints. Recently we showed the role of CXCL10 on receptor activator of nuclear factor kappa-B ligand (RANKL) expression in an animal model of RA and suggested the contribution to osteoclastogenesis. We tested the effects of CXCL10 on the expression of RANKL in RA synoviocytes and T cells, and we investigated which subunit of CXCR3 contributes to RANKL expression by CXCL10. Methods Synoviocytes derived from RA patients were kept in culture for 24 hours in the presence or absence of TNF-α. CXCL10 expression was measured by reverse transcriptase polymerase chain reaction (RT-PCR) of cultured synoviocytes. Expression of RANKL was measured by RT-PCR and western blot in cultured synoviocytes with or without CXCL10 and also measured in Jurkat/Hut 78 T cells and CD4+ T cells in the presence of CXCL10 or dexamethasone. CXCL10 induced RANKL expression in Jurkat T cells was tested upon the pertussis toxin (PTX), an inhibitor of Gi subunit of G protein coupled receptor (GPCR). The synthetic siRNA for Gαi2 was used to knock down gene expression of respective proteins. Results CXCL10 expression in RA synoviocytes was increased by TNF-α. CXCL10 slightly increased RANKL expression in RA synoviocytes, but markedly increased RANKL expression in Jurkat/Hut 78 T cell or CD4+ T cell. CXCL10 augmented the expression of RANKL by 62.6%, and PTX inhibited both basal level of RANKL (from 37.4 ± 16.0 to 18.9 ± 13.0%) and CXCL10-induced RANKL expression in Jurkat T cells (from 100% to 48.6 ± 27.3%). Knock down of Gαi2 by siRNA transfection, which suppressed the basal level of RANKL (from 61.8 ± 17.9% to 31.1 ± 15.9%) and CXCL10-induced RANKL expression (from 100% to 53.1 ± 27.1%) in Jurkat T cells, is consistent with PTX, which inhibited RANKL expression. Conclusions CXCL10 increased RANKL expression in CD4+ T cells and it was mediated by Gαi subunits of CXCR3. These results indicate that CXCL10 may have a potential role in osteoclastogenesis of RA synovial tissue and subsequent joint erosion

Environmental Impacts of Prefabricated Construction: CO2 Emissions Comparison of Precast and Cast-In-Place Concrete Case Study

Thesis (Master's)--University of Washington, 2020Construction activities are one of the major contributors to climate change by greenhouse gas emissions. While the use of prefabrication has certain advantages in terms of environmental impacts through material and time efficiency, it is not clear nor has enough data for the quantities and factors comparing the conventional methods. This study aims to review the characteristics of prefabricated construction and to find environmental impacts through the case study. The methodology is the analysis by comparing the carbon emissions of precast concrete which is one of the major prefabricated structures and cast-in-place concrete which is conventional methods. The case study data is based on residential buildings which were built by prefabricated structures in South Korea. The comparison is conducted focused on several scenarios according to the criteria for precast concrete construction such as loss rate of materials, delivery distance, vehicle capacity, equipment types and installation hours. The outcomes are found that the amount of carbon emissions of precast and cast-in-place concrete for the studied residential buildings. Based on the research findings, it is recommended to adopt precast concrete in building construction in terms of environmental impacts during the product stage and construction stage. However, these averages can be a significant variation among individual projects. The far distance, small vehicle capacity and low efficiency of equipment with a loss of material can adversely affect the environment. The building industry should consider the carbon reduction as a benefit of implementing prefabricated construction after considering the characteristics of the location, distance, transportation method, and installation efficiency

Gq protein mediates UVB-induced cyclooxygenase-2 expression by stimulating HB-EGF secretion from HaCaT human keratinocytes

Ultraviolet (UV) radiation induces cyclooxygenase-2 expression to produce cellular responses including aging and carcinogenesis in skin. We hypothesised that heterotrimeric G proteins mediate UV-induced COX-2 expression by stimulating secretion of soluble HB-EGF (sHB-EGF). In this study, we aimed to elucidate the role and underlying mechanism of the a subunit of Gq protein (G alpha q) in UVB-induced HB-EGF secretion and COX-2 induction. We found that expression of constitutively active G alpha q (G alpha qQL) augmented UVB-induced HB-EGF secretion. which was abolished by knockdown of G alpha q with shRNA in HaCaT human keratinocytes. G alpha q was found to mediate the UVB-induced HB-EGF secretion by sequential activation of phospholipase C (PLC), protein kinase C delta (PKC delta), and matrix metaloprotease-2 (MMP-2). Moreover, G alpha qQL mediated UVB-induced COX-2 expression in an HH-EGF-, EGFR-, and p38-dependent manner. From these results, we concluded that G alpha q mediates UV-induced COX-2 expression through activation of EGFR by HB-EGF, of which ectodomain shedding was stimulated through sequential activation of PLC, PKC delta and MMP-2 in HaCaT cells. (C) 2010 Elsevier Inc. All rights reserved.Beltran AE, 2009, J HYPERTENS, V27, P142, DOI 10.1097/HJH.0b013e328317a730Dong KK, 2008, EXP DERMATOL, V17, P1037, DOI 10.1111/j.1600-0625.2008.00747.xHsieh HL, 2008, BBA-MOL CELL RES, V1783, P1563, DOI 10.1016/j.bbamcr.2008.03.016Kim Y, 2008, J BIOL CHEM, V283, P22513, DOI 10.1074/jbc.M708319200Pham H, 2008, BBA-GENE REGUL MECH, V1779, P408, DOI 10.1016/j.bbagrm.2008.05.004Rundhaug JE, 2008, PHOTOCHEM PHOTOBIOL, V84, P322, DOI 10.1111/j.1751-1097.2007.00261.xKim SY, 2008, J BIOL CHEM, V283, P1350, DOI 10.1074/jbc.M702344200Huang W, 2008, DIGEST DIS SCI, V53, P163, DOI 10.1007/s10620-007-9838-9Seo MR, 2007, J BIOL CHEM, V282, P24720Zhou WL, 2007, AM J PHYSIOL-HEART C, V292, pH2773, DOI 10.1152/ajpheart.01018.2006Chun KS, 2007, CANCER RES, V67, P2015, DOI 10.1158/0008-5472.CAN-06-3617Nagase H, 2006, CARDIOVASC RES, V69, P562, DOI 10.1016/j.cardiores.2005.12.002Pakozdi A, 2006, ARTHRITIS RES THER, V8, DOI 10.1186/ar2021Husain S, 2005, INVEST OPHTH VIS SCI, V46, P1706, DOI 10.1167/iovs.04-0993Lucchesi PA, 2004, CIRCULATION, V110, P3587, DOI 10.1161/01.CIR.0000148780.36121.47Woo CH, 2004, J IMMUNOL, V173, P6973Deo DD, 2004, J BIOL CHEM, V279, P3497, DOI 10.1074/jbc.M304497200Le Gall SM, 2003, J BIOL CHEM, V278, P45255, DOI 10.1074/jbc.M307745200Zaczynska E, 2003, INFLAMMATION, V27, P307Tsai CH, 2003, ORAL SURG ORAL MED O, V95, P710, DOI 10.1067/moe.2003.121Takenobu H, 2003, J BIOL CHEM, V278, P17255, DOI 10.1074/jbc.M211835200Slice LW, 2003, J CELL PHYSIOL, V194, P127, DOI 10.1002/jcp.10195Bachelor MA, 2002, ONCOGENE, V21, P7092, DOI 10.1038/sj.onc.1205855Fukunaga M, 2001, BIOCHEM BIOPH RES CO, V289, P573JOHN A, 2001, PATHOL ONCOL RES, V7, P14Abbott KL, 2000, J MOL CELL CARDIOL, V32, P391Smith WL, 2000, ANNU REV BIOCHEM, V69, P145Fu SL, 1999, P NATL ACAD SCI USA, V96, P5716Clapham DE, 1997, ANNU REV PHARMACOL, V37, P167KOIVUKANGAS V, 1994, ACTA DERM-VENEREOL, V74, P279MARIKOVSKY M, 1993, P NATL ACAD SCI USA, V90, P3889KRAMER M, 1993, J BIOL CHEM, V268, P6734LEE CH, 1992, J BIOL CHEM, V267, P16044GILMAN AG, 1987, ANNU REV BIOCHEM, V56, P615

Stimulatory heterotrimeric GTP-binding protein augments cisplatin-induced apoptosis by upregulating Bak expression in human lung cancer cells

The present study aimed to investigate the effect of the stimulatory heterotrimeric GTP-binding (Gs) protein signaling system on cisplatin-induced apoptosis of lung cancer cells and its underlying mechanism as an attempt to develop a novel strategy to improve the therapeutic efficacy of cisplatin. Overexpression of the constitutively active alpha subunit of Gs (G alpha sQL) in A549 human lung cancer cells increased cisplatin-induced apoptosis, and knockdown of G alpha s with small hairpin RNA decreased the percentage of apoptotic cells. G alpha sQL increased the expression of the proapoptotic proteins B-cell leukemia/lymphoma-2 genes (Bcl-2) homologous antagonist killer protein (Bak) and Bcl-2 associated X protein (Bax), and decreased the expression of the antiapoptotic proteins Bcl-2 and Bcl-Xlong protein. Knockdown of Bak blocked the augmentative effects of G alpha sQL. G alpha sQL decreased the degradation rate of the Bak protein, and increased Bak mRNA transcript levels. G alpha sQL increased Bak-luciferase activity in a protein kinase A and cyclic AMP response element-dependent manner. G alpha sQL also augmented cisplatin-induced apoptosis of H1299 human lung cancer cells that lack functional p53. From this study, it is concluded that G alpha s augments cisplatin-induced apoptosis of lung cancer cells partially through upregulating Bak expression by increasing transcription and by decreasing the rate of protein degradation. (Cancer Sci 2009; 100: 1069-1074).Aggarwal S, 2008, CANCER RES, V68, P981, DOI 10.1158/0008-5472.CAN-06-0249Kim SY, 2008, J BIOL CHEM, V283, P1350, DOI 10.1074/jbc.M702344200Wang L, 2008, MOL PHARMACOL, V73, P119, DOI 10.1124/mol.107.040873Kim SY, 2007, EXP MOL MED, V39, P583Siu YT, 2007, FEBS J, V274, P3224, DOI 10.1111/j.1742-4658.2007.05884.xRabik CA, 2007, CANCER TREAT REV, V33, P9, DOI 10.1016/j.ctrv.2006.09.006Gebbia V, 2006, ANN ONCOL, V17, P83, DOI 10.1093/annonc/mdj933Zhang XM, 2005, P NATL ACAD SCI USA, V102, P4459, DOI 10.1073/pnas.0501076102McCudden CR, 2005, CELL MOL LIFE SCI, V62, P551, DOI 10.1007/s00018-004-4462-3Schweyer S, 2004, INT J ONCOL, V25, P1671Hastings RH, 2004, AM J PHYSIOL-CELL PH, V287, pC1616, DOI 10.1152/ajpcell.00300.2004Hirsh L, 2004, BIOCHEM PHARMACOL, V68, P981, DOI 10.1016/j.bcp.2004.05.026Cho YS, 2002, CLIN CANCER RES, V8, P607Wei MC, 2001, SCIENCE, V292, P727Cohen SM, 2001, PROG NUCLEIC ACID RE, V67, P93Gu CH, 2000, J BIOL CHEM, V275, P20726Wong E, 1999, CHEM REV, V99, P2451JAMIESON ER, 1999, RECOGNITION PROCESSI, V99, P2467Shafer SH, 1998, BIOCHEM PHARMACOL, V56, P1229Chen TC, 1998, LAB INVEST, V78, P165Ruchaud S, 1997, ONCOGENE, V15, P827Allam M, 1997, CANCER RES, V57, P2615Miyajima A, 1997, BRIT J CANCER, V76, P206ALBERTI W, 1995, BRIT MED J, V311, P899CHITTENDEN T, 1995, NATURE, V374, P733CLAPHAM DE, 1993, NATURE, V365, P403CONKLIN BR, 1993, CELL, V73, P631SIMON MI, 1991, SCIENCE, V252, P802BOURNE HR, 1990, NATURE, V348, P125

TNF-α-Induced YAP/TAZ Activity Mediates Leukocyte-Endothelial Adhesion by Regulating VCAM1 Expression in Endothelial Cells

YAP/TAZ, a transcriptional co-activator of Hippo pathway, has emerged as a central player in vessel homeostasis such as sprouting angiogenesis and vascular barrier stabilization, during development. However, the role of YAP/TAZ in pathological angiogenesis remains unclear. Here, we demonstrated that YAP/TAZ is a critical mediator in leukocyte-endothelial adhesion induced by the vascular inflammatory cytokine TNF-α. YAP/TAZ was dephosphorylated, translocated from the cytosol to the nucleus, and activated by TNF-α in endothelial cells. A specific inhibitor of Rho GTPases suppressed the TNF-α-induced dephosphorylation of YAP. Knockdown of YAP/TAZ using siRNA significantly reduced the expression of the leukocyte adhesion molecule VCAM1 induced by TNF-α. The adhesion of monocytes to endothelial cells was also markedly reduced by YAP/TAZ silencing. However, knockdown of YAP/TAZ did not affect TNF-α-induced NF-κB signaling. Overall, these results suggest that YAP/TAZ plays critical roles in regulating TNF-α-induced endothelial cell adhesive properties without affecting the NF-κB pathway, and implicate YAP/TAZ as a potential therapeutic target for treating inflammatory vascular diseases

Dibutyryl cAMP stimulates the proliferation of SH-SY5Y human neuroblastoma cells by up-regulating Skp2 protein

PURPOSE: We previously found that the proliferation of SH-SY5Y neuroblastoma cells is stimulated when cAMP is up-regulated by stable expression of stimulatory G protein. Therefore, this study was performed to investigate the mechanism whereby cAMP stimulates the proliferation of SH-SY5Y cells. METHODS: To investigate the effect of cAMP on cellular proliferation, SH-SY5Y neuroblastoma cells were treated with dibutyryl cAMP (dbcAMP), and then cell growth, thymidine incorporation and cell cycle phase distribution were analyzed. The expression and the activity of the molecules that regulate cell cycle progression were monitored by Western blot, RT-PCR, and kinase activity assay. RESULTS: Treatment with dbcAMP produced a biphasic effect on cellular proliferation; especially treatment with low concentration of dbcAMP (0.5 mM) showed a higher cellular proliferation rate and promoted G1/S transition in cell cycle. The dbcAMP (0.5 mM) treatment increased CDK2 activity, and it significantly decreased p27Kip1 expression with a decreased half-life of p27Kip1 protein. Moreover, dbcAMP (0.5 mM) increased the protein level and the stability of Skp2 with a concomitant decrease in its ubiquitination. CONCLUSIONS: cAMP up-regulates Skp2 protein by reducing its degradation probably through decreasing the ubiquitination of Skp2, which might result in accelerated degradation of p27Kip1, increase in CDK2 activity, and stimulation of SH-SY5Y cell proliferation in sequence