Brx, a link between osmotic stress, inflammation and organ physiology/pathophysiology

References

• Griffith RW. Composition of blood serum of deep-sea fishes. Biol. Bull.160, 250–264 (1981).
   Google Scholar
• Burg MB, Kwon ED, Kultz D. Regulation of gene expression by hypertonicity. Annu. Rev. Physiol.59, 437–455 (1997).
   PubMed Web of Science ®Google Scholar
• Burg MB, Ferraris JD, Dmitrieva NI. Cellular response to hyperosmotic stresses. Physiol. Rev.87(4), 1441–1474 (2007).
   PubMed Web of Science ®Google Scholar
• Ho SN. Intracellular water homeostasis and the mammalian cellular osmotic stress response. J. Cell Physiol.206(1), 9–15 (2006).
   PubMed Web of Science ®Google Scholar
• Jungersted JM, Hellgren LI, Jemec GB, Agner T. Lipids and skin barrier function – a clinical perspective. Contact Dermatitis58(5), 255–262 (2008).
   PubMed Web of Science ®Google Scholar
• Bourque CW, Oliet SH. Osmoreceptors in the central nervous system. Annu. Rev. Physiol.59, 601–619 (1997).
   PubMed Web of Science ®Google Scholar
• Ho SN. The role of NFAT5/TonEBP in establishing an optimal intracellular environment. Arch. Biochem. Biophys.413(2), 151–157 (2003).
   PubMed Web of Science ®Google Scholar
• Kino T, Takatori H, Manoli I et al. Brx mediates the response of lymphocytes to osmotic stress through the activation of NFAT5. Sci. Signal.2(57), RA5 (2009).
   Google Scholar
• Aramburu J, Lopez-Rodriguez C. Brx shines a light on the route from hyperosmolarity to NFAT5. Sci. Signal.2(65), PE20 (2009).
   Google Scholar
• Aramburu J, Drews-Elger K, Estrada-Gelonch A et al. Regulation of the hypertonic stress response and other cellular functions by the Rel-like transcription factor NFAT5. Biochem. Pharmacol.72(11), 1597–1604 (2006).
   PubMedGoogle Scholar
• Haussinger D. The role of cellular hydration in the regulation of cell function. Biochem. J.313, 697–710 (1996).
   PubMed Web of Science ®Google Scholar
• Lopez-Rodriguez C, Aramburu J, Jin L, Rakeman AS, Michino M, Rao A. Bridging the NFAT and NF-κB families: NFAT5 dimerization regulates cytokine gene transcription in response to osmotic stress. Immunity15(1), 47–58 (2001).
   PubMed Web of Science ®Google Scholar
• Go WY, Liu X, Roti MA, Liu F, Ho SN. NFAT5/TonEBP mutant mice define osmotic stress as a critical feature of the lymphoid microenvironment. Proc. Natl Acad. Sci. USA101(29), 10673–10678 (2004).
   PubMed Web of Science ®Google Scholar
• Trama J, Go WY, Ho SN. The osmoprotective function of the NFAT5 transcription factor in T cell development and activation. J. Immunol.169(10), 5477–5488 (2002).
   PubMed Web of Science ®Google Scholar
• Morancho B, Minguillon J, Molkentin JD, Lopez-Rodriguez C, Aramburu J. Analysis of the transcriptional activity of endogenous NFAT5 in primary cells using transgenic NFAT-luciferase reporter mice. BMC Mol. Biol.9, 13 (2008).
   PubMedGoogle Scholar
• Lam AK, Ko BC, Tam S et al. Osmotic response element-binding protein (OREBP) is an essential regulator of the urine concentrating mechanism. J. Biol. Chem.279(46), 48048–48054 (2004).
   PubMedGoogle Scholar
• O’Connor RS, Mills ST, Jones KA, Ho SN, Pavlath GK. A combinatorial role for NFAT5 in both myoblast migration and differentiation during skeletal muscle myogenesis. J. Cell Sci.120(Pt 1), 149–159 (2007).
   PubMed Web of Science ®Google Scholar
• Lopez-Rodriguez C, Antos CL, Shelton JM et al. Loss of NFAT5 results in renal atrophy and lack of tonicity-responsive gene expression. Proc. Natl Acad. Sci. USA101(8), 2392–2397 (2004).
   PubMedGoogle Scholar
• Hohmann S. Osmotic stress signaling and osmoadaptation in yeasts. Microbiol. Mol. Biol. Rev.66(2), 300–372 (2002).
   PubMed Web of Science ®Google Scholar
• Saito H, Tatebayashi K. Regulation of the osmoregulatory HOG MAPK cascade in yeast. J. Biochem.136(3), 267–272 (2004).
   PubMed Web of Science ®Google Scholar
• Raitt DC, Posas F, Saito H. Yeast Cdc42 GTPase and Ste20 PAK-like kinase regulate Sho1-dependent activation of the Hog1 MAPK pathway. EMBO J.19(17), 4623–4631 (2000).
   PubMedGoogle Scholar
• Tatebayashi K, Tanaka K, Yang HY et al. Transmembrane mucins Hkr1 and Msb2 are putative osmosensors in the SHO1 branch of yeast HOG pathway. EMBO J.26(15), 3521–3333 (2007).
   PubMed Web of Science ®Google Scholar
• Tatebayashi K, Yamamoto K, Tanaka K et al. Adaptor functions of Cdc42, Ste50, and Sho1 in the yeast osmoregulatory HOG MAPK pathway. EMBO J.25(13), 3033–3044 (2006).
   PubMed Web of Science ®Google Scholar
• Widmann C, Gibson S, Jarpe MB, Johnson GL. Mitogen-activated protein kinase: conservation of a three-kinase module from yeast to human. Physiol. Rev.79(1), 143–180 (1999).
   PubMed Web of Science ®Google Scholar
• Saito H. Histidine phosphorylation and two-component signaling in eukaryotic cells. Chem. Rev.101(8), 2497–2509 (2001).
   PubMedGoogle Scholar
• Maeda T, Takekawa M, Saito H. Activation of yeast PBS2 MAPKK by MAPKKKs or by binding of an SH3-containing osmosensor. Science269(5223), 554–558 (1995).
   PubMed Web of Science ®Google Scholar
• Lunn JA, Rozengurt E. Hyperosmotic stress induces rapid focal adhesion kinase phosphorylation at tyrosines 397 and 577. Role of Src family kinases and Rho family GTPases. J. Biol. Chem.279(43), 45266–45278 (2004).
   Google Scholar
• Uhlik MT, Abell AN, Johnson NL et al. Rac –MEKK3–MKK3 scaffolding for p38 MAPK activation during hyperosmotic shock. Nat. Cell Biol.5(12), 1104–1110 (2003).
   PubMed Web of Science ®Google Scholar
• Sheikh-Hamad D, Di Mari J, Suki WN, Safirstein R, Watts BA 3rd, Rouse D. p38 kinase activity is essential for osmotic induction of mRNAs for HSP70 and transporter for organic solute betaine in Madin-Darby canine kidney cells. J. Biol. Chem.273(3), 1832–1837 (1998).
   Google Scholar
• Macian F, Lopez-Rodriguez C, Rao A. Partners in transcription: NFAT and AP-1. Oncogene20(19), 2476–2489 (2001).
   PubMed Web of Science ®Google Scholar
• Tsai TT, Guttapalli A, Agrawal A, Albert TJ, Shapiro IM, Risbud MV. MEK/ERK signaling controls osmoregulation of nucleus pulposus cells of the intervertebral disc by transactivation of TonEBP/OREBP. J. Bone Miner. Res.22(7), 965–974 (2007).
   Google Scholar
• Lee JH, Kim M, Im YS, Choi W, Byeon SH, Lee HK. NFAT5 induction and its role in hyperosmolar stressed human limbal epithelial cells. Invest. Ophthalmol. Vis. Sci.49(5), 1827–1835 (2008).
   PubMed Web of Science ®Google Scholar
• Graef IA, Gastier JM, Francke U, Crabtree GR. Evolutionary relationships among Rel domains indicate functional diversification by recombination. Proc. Natl Acad. Sci. USA98(10), 5740–5745 (2001).
   PubMedGoogle Scholar
• Keyser P, Borge-Renberg K, Hultmark D. The Drosophila NFAT homolog is involved in salt stress tolerance. Insect. Biochem. Mol. Biol.37(4), 356–362 (2007).
   Google Scholar
• Dahl SC, Handler JS, Kwon HM. Hypertonicity-induced phosphorylation and nuclear localization of the transcription factor TonEBP. Am. J. Physiol. Cell Physiol.280(2), C248–C253 (2001).
   Google Scholar
• Ko BC, Lam AK, Kapus A, Fan L, Chung SK, Chung SS. Fyn and p38 signaling are both required for maximal hypertonic activation of the osmotic response element-binding protein/tonicity-responsive enhancer-binding protein (OREBP/TonEBP). J. Biol. Chem.277(48), 46085–46092 (2002).
   PubMed Web of Science ®Google Scholar
• Schmidt A, Hall A. Guanine nucleotide exchange factors for Rho GTPases: turning on the switch. Genes Dev.16(13), 1587–1609 (2002).
   PubMed Web of Science ®Google Scholar
• Cherfils J, Chardin P. GEFs: structural basis for their activation of small GTP-binding proteins. Trends Biochem. Sci.24(8), 306–311 (1999).
   PubMed Web of Science ®Google Scholar
• Takai Y, Sasaki T, Matozaki T. Small GTP-binding proteins. Physiol. Rev.81(1), 153–208 (2001).
   PubMed Web of Science ®Google Scholar
• Kaibuchi K, Kuroda S, Amano M. Regulation of the cytoskeleton and cell adhesion by the Rho family GTPases in mammalian cells. Annu. Rev. Biochem.68, 459–486 (1999).
   PubMed Web of Science ®Google Scholar
• Olofsson B. Rho guanine dissociation inhibitors: pivotal molecules in cellular signalling. Cell. Signal.11(8), 545–554 (1999).
   PubMed Web of Science ®Google Scholar
• Aznar S, Lacal JC. Rho signals to cell growth and apoptosis. Cancer Lett.165(1), 1–10 (2001).
   PubMed Web of Science ®Google Scholar
• Zheng Y, Olson MF, Hall A, Cerione RA, Toksoz D. Direct involvement of the small GTP-binding protein Rho in lbc oncogene function. J. Biol. Chem.270(16), 9031–9034 (1995).
   PubMed Web of Science ®Google Scholar
• Rubino D, Driggers P, Arbit D et al. Characterization of Brx, a novel Dbl family member that modulates estrogen receptor action. Oncogene16(19), 2513–2526 (1998).
   PubMed Web of Science ®Google Scholar
• Driggers PH, Segars JH, Rubino DM. The proto-oncoprotein Brx activates estrogen receptor b by a p38 mitogen-activated protein kinase pathway. J. Biol. Chem.276(50), 46792–476797 (2001).
   PubMed Web of Science ®Google Scholar
• Kino T, Souvatzoglou E, Charmandari E et al. Rho family Guanine nucleotide exchange factor Brx couples extracellular signals to the glucocorticoid signaling system. J. Biol. Chem.281(14), 9118–9126 (2006).
   PubMed Web of Science ®Google Scholar
• Sterpetti P, Hack AA, Bashar MP et al. Activation of the Lbc Rho exchange factor proto-oncogene by truncation of an extended C terminus that regulates transformation and targeting. Mol. Cell. Biol.19(2), 1334–1345 (1999).
   PubMedGoogle Scholar
• Diviani D, Soderling J, Scott JD. AKAP-Lbc anchors protein kinase A and nucleates Gα12-selective Rho-mediated stress fiber formation. J. Biol. Chem.276(47), 44247–44257 (2001).
   PubMed Web of Science ®Google Scholar
• Diviani D, Abuin L, Cotecchia S, Pansier L. Anchoring of both PKA and 14-13-3 inhibits the Rho-GEF activity of the AKAP-Lbc signaling complex. EMBO J.23(14), 2811–2820 (2004).
   PubMed Web of Science ®Google Scholar
• Mayers CM, Wadell J, McLean K et al. The Rho guanine nucleotide exchange factor AKAP13 (BRX) is essential for cardiac development in mice. J. Biol. Chem.285(16), 12344–12354 (2010).
   Google Scholar
• Rogers R, Norian J, Malik M et al. Mechanical homeostasis is altered in uterine leiomyoma. Am. J. Obstet. Gynecol.198(4), 474, E471–E411 (2008).
   Google Scholar
• Morrison DK, Davis RJ. Regulation of MAP kinase signaling modules by scaffold proteins in mammals. Annu. Rev. Cell Dev. Biol.19, 91–118 (2003).
   PubMed Web of Science ®Google Scholar
• Whitmarsh AJ. The JIP family of MAPK scaffold proteins. Biochem. Soc. Trans.34(Pt 5), 828–832 (2006).
   PubMed Web of Science ®Google Scholar
• Kelkar N, Standen CL, Davis RJ. Role of the JIP4 scaffold protein in the regulation of mitogen-activated protein kinase signaling pathways. Mol. Cell. Biol.25(7), 2733–2743 (2005).
   PubMedGoogle Scholar
• Standen CL, Kennedy NJ, Flavell RA, Davis RJ. Signal transduction cross-talk mediated by JIP and IRS scaffold protein complexes. Mol. Cell. Biol.29(17), 4831–4840 (2009).
   PubMedGoogle Scholar
• Ge W, Wu J, Zhai J et al. Binding of p190RhoGEF to a destabilizing element on the light neurofilament mRNA is competed by BC1 RNA. J. Biol. Chem.277(45), 42701–42705 (2002).
   Google Scholar
• Buchsbaum RJ, Connolly BA, Feig LA. Interaction of Rac exchange factors Tiam1 and Ras–GRF1 with a scaffold for the p38 mitogen-activated protein kinase cascade. Mol. Cell. Biol.22(12), 4073–4085 (2002).
   PubMedGoogle Scholar
• Shi Y, Gaestel M. In the cellular garden of forking paths: how p38 MAPKs signal for downstream assistance. Biol. Chem.383(10), 1519–1536 (2002).
   PubMedGoogle Scholar
• Pedersen SF, Hoffmann EK, Mills JW. The cytoskeleton and cell volume regulation. Comp. Biochem. Physiol. Part A Mol. Integr. Physiol.130(3), 385–399 (2001).
   Google Scholar
• Henson JH. Relationships between the actin cytoskeleton and cell volume regulation. Microsc. Res. Tech.47(2), 155–162 (1999).
   Google Scholar
• Hoffmann EK, Dunham PB. Membrane mechanisms and intracellular signalling in cell volume regulation. Int. Rev. Cytol.161, 173–262 (1995).
   PubMedGoogle Scholar
• Di Ciano-Oliveira C, Thirone AC, Szaszi K, Kapus A. Osmotic stress and the cytoskeleton: the R(h)ole of Rho GTPases. Acta Physiol. (Oxf.)187(1–2), 257–272 (2006).
   PubMedGoogle Scholar
• Li C, Xu Q. Mechanical stress-initiated signal transduction in vascular smooth muscle cells in vitro and in vivo . Cell. Signal.19(5), 881–891 (2007).
   PubMed Web of Science ®Google Scholar
• Wang JH, Thampatty BP, Lin JS, Im HJ. Mechanoregulation of gene expression in fibroblasts. Gene391(1–2), 1–15 (2007).
   PubMed Web of Science ®Google Scholar
• Drews-Elger K, Ortells MC, Rao A, Lopez-Rodriguez C, Aramburu J. The transcription factor NFAT5 is required for cyclin expression and cell cycle progression in cells exposed to hypertonic stress. PLoS ONE4(4), E5245 (2009).
   Google Scholar
• Mahnke K, Ring S, Bedke T, Karakhanova S, Enk AH. Interaction of regulatory T cells with antigen-presenting cells in health and disease. Chem. Immunol. Allergy94, 29–39 (2008).
   PubMedGoogle Scholar
• Li Y, Sassano A, Majchrzak B et al. Role of p38a MAP kinase in Type I interferon signaling. J. Biol. Chem.279(2), 970–979 (2004).
   PubMed Web of Science ®Google Scholar
• Schwartz L, Guais A, Pooya M, Abolhassan M. Is inflammation a consequence of extracellular hyperosmolarity? J. Inflamm. (Lond.)6, 21 (2009).
   Google Scholar
• Hoffman WH, Helman SW, Passmore G. Acute activation of peripheral lymphocytes during treatment of diabetic ketoacidosis. J. Diabetes Complicat.15(3), 144–149 (2001).
   Google Scholar
• Wu SG, Jeng FR, Wei SY et al. Red blood cell osmotic fragility in chronically hemodialyzed patients. Nephron78(1), 28–32 (1998).
   PubMedGoogle Scholar
• Mitono H, Endoh H, Okazaki K et al. Acute hypoosmolality attenuates the suppression of cutaneous vasodilation with increased exercise intensity. J. Appl. Physiol.99(3), 902–908 (2005).
   PubMed Web of Science ®Google Scholar
• Ito T, Itoh T, Hayano T, Yamauchi K, Takamata A. Plasma hyperosmolality augments peripheral vascular response to baroreceptor unloading during heat stress. Am. J. Physiol. Regul. Integr. Comp. Physiol.289(2), R432–R440 (2005).
   PubMed Web of Science ®Google Scholar
• Holtfreter B, Bandt C, Kuhn SO et al. Serum osmolality and outcome in intensive care unit patients. Acta Anaesthesiol. Scand.50(8), 970–977 (2006).
   PubMed Web of Science ®Google Scholar
• Wong CK, Szeto CC, Chan MH, Leung CB, Li PK, Lam CW. Elevation of pro-inflammatory cytokines, C-reactive protein and cardiac troponin T in chronic renal failure patients on dialysis. Immunol. Invest.36(1), 47–57 (2007).
   PubMed Web of Science ®Google Scholar
• Yano A, Nakao K, Sarai A et al. Elevated serum interleukin-18 levels might reflect the high risk of hospitalization in patients on peritoneal dialysis. Nephrology (Carlton)10(6), 576–582 (2005).
   Google Scholar
• Nakanishi I, Moutabarrik A, Okada N et al. Interleukin-8 in chronic renal failure and dialysis patients. Nephrol. Dial. Transplant.9(10), 1435–1442 (1994).
   PubMed Web of Science ®Google Scholar
• Descamps-Latscha B, Herbelin A, Nguyen AT et al. Balance between IL-1β, TNF-α, and their specific inhibitors in chronic renal failure and maintenance dialysis. Relationships with activation markers of T cells, B cells, and monocytes. J. Immunol.154(2), 882–892 (1995).
   PubMed Web of Science ®Google Scholar
• Ostrowski K, Schjerling P, Pedersen BK. Physical activity and plasma interleukin-6 in humans – effect of intensity of exercise. Eur. J. Appl. Physiol.83(6), 512–515 (2000).
   PubMed Web of Science ®Google Scholar
• Bird MD, Kovacs EJ. Organ-specific inflammation following acute ethanol and burn injury. J. Leukoc. Biol.84(3), 607–613 (2008).
   Google Scholar
• Machnik A, Neuhofer W, Jantsch J et al. Macrophages regulate salt-dependent volume and blood pressure by a vascular endothelial growth factor-C-dependent buffering mechanism. Nat. Med.15(5), 545–552 (2009).
   PubMed Web of Science ®Google Scholar
• Shanfield S, Campbell P, Baumgarten M, Bloebaum R, Sarmiento A. Synovial fluid osmolality in osteoarthritis and rheumatoid arthritis. Clin. Orthop. Relat. Res. (235), 289–295 (1988).
   Google Scholar
• Nemeth ZH, Deitch EA, Szabo C, Hasko G. Hyperosmotic stress induces nuclear factor-κB activation and interleukin-8 production in human intestinal epithelial cells. Am. J. Pathol.161(3), 987–996 (2002).
   PubMed Web of Science ®Google Scholar
• Vernia P, Gnaedinger A, Hauck W, Breuer RI. Organic anions and the diarrhea of inflammatory bowel disease. Dig. Dis. Sci.33(11), 1353–1358 (1988).
   PubMed Web of Science ®Google Scholar
• Foulks GN. The correlation between the tear film lipid layer and dry eye disease. Surv. Ophthalmol.52(4), 369–374 (2007).
   PubMed Web of Science ®Google Scholar
• Elenkov IJ, Iezzoni DG, Daly A, Harris AG, Chrousos GP. Cytokine dysregulation, inflammation and well-being. Neuroimmunomodulation12(5), 255–269 (2005).
   PubMed Web of Science ®Google Scholar
• Goldstein BI, Kemp DE, Soczynska JK, McIntyre RS. Inflammation and the phenomenology, pathophysiology, comorbidity, and treatment of bipolar disorder: a systematic review of the literature. J. Clin. Psychiatry70(8), 1078–1090 (2009).
   PubMed Web of Science ®Google Scholar
• Papa S, Bubici C, Zazzeroni F, Franzoso G. Mechanisms of liver disease: the crosstalk between the NF-κB and JNK pathways. Biol. Chem.390(10), 965–976 (2009).
   PubMed Web of Science ®Google Scholar
• Yu R, Kim CS, Kang JH. Inflammatory components of adipose tissue as target for treatment of metabolic syndrome. Forum Nutr.61, 95–103 (2009).
   Google Scholar
• Fildes JE, Shaw SM, Yonan N, Williams SG. The immune system and chronic heart failure: is the heart in control? J. Am. Coll. Cardiol.53(12), 1013–1020 (2009).
   Google Scholar
• Kim JH, Bachmann RA, Chen J. Interleukin-6 and insulin resistance. Vitam. Horm.80, 613–633 (2009).
   PubMed Web of Science ®Google Scholar
• Gorski J, Hou Q. Embryonic estrogen receptors: do they have a physiological function? Environ. Health Perspect.103(Suppl. 7), 69–72 (1995).
   PubMed Web of Science ®Google Scholar
• Li R, Whitworth K, Lai L et al. Concentration and composition of free amino acids and osmolalities of porcine oviductal and uterine fluid and their effects on development of porcine IVF embryos. Mol. Reprod. Dev.74(9), 1228–1235 (2007).
   Google Scholar
• Kino T, De Martino MU, Charmandari E, Mirani M, Chrousos GP. Tissue glucocorticoid resistance/hypersensitivity syndromes. J. Steroid Biochem. Mol. Biol.85(2–5), 457–467 (2003).
   PubMed Web of Science ®Google Scholar
• Chrousos GP, Kino T. Intracellular glucocorticoid signaling: a formerly simple system turns stochastic. Sci. STKE2005(304), PE48 (2005).
   PubMedGoogle Scholar
• Chrousos GP. The hypothalamic–pituitary–adrenal axis and immune-mediated inflammation. N. Engl J. Med.332(20), 1351–1362 (1995).
   PubMed Web of Science ®Google Scholar
• Antoni FA. Vasopressinergic control of pituitary adrenocorticotropin secretion comes of age. Front. Neuroendocrinol.14(2), 76–122 (1993).
   PubMed Web of Science ®Google Scholar
• Weitzman RE, Kleeman CR. The clinical physiology of water metabolism. Part I: the physiologic regulation of arginine vasopressin secretion and thirst. West J. Med.131(5), 373–400 (1979).
   PubMedGoogle Scholar
• Eddington DO, Baldwin EL, Segars JH, Wu TJ. Estrogen effects on the expression of Brx in the brain and pituitary of the mouse. Brain Res. Bull.69(4), 447–451 (2006).
   Google Scholar
• Zhan Y, Gerondakis S, Coghill E et al. Glucocorticoid-induced TNF receptor expression by T cells is reciprocally regulated by NF-κB and NFAT. J. Immunol.181(8), 5405–5413 (2008).
   PubMed Web of Science ®Google Scholar
• Yildiz EH, Fan VC, Banday H et al. Evaluation of a new tear osmometer for repeatability and accuracy, using 0.5-microL (500-Nanoliter) samples. Cornea28(6), 677–680 (2009).
   PubMed Web of Science ®Google Scholar
• Gilbard JP, Farris RL, Santamaria J 2nd. Osmolarity of tear microvolumes in keratoconjunctivitis sicca. Arch. Ophthalmol.96(4), 677–681 (1978).
   PubMed Web of Science ®Google Scholar
• Bohr J, Jarnerot G, Tysk C, Jones I, Eriksson S. Effect of fasting on diarrhoea in collagenous colitis. Digestion65(1), 30–34 (2002).
   PubMed Web of Science ®Google Scholar
• Collins JL, Baltz JM. Estimates of mouse oviductal fluid tonicity based on osmotic responses of embryos. Biol. Reprod.60(5), 1188–1193 (1999).
   Google Scholar