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Volumn 1834, Issue 10, 2013, Pages 2170-2175

Insulin receptor-related receptor as an extracellular pH sensor involved in the regulation of acid-base balance

Author keywords

Alkaline pH; Alkalosis; Insulin receptor; Insulin receptor related receptor; Receptor tyrosine kinase

Indexed keywords

ALKALI; INSULIN RECEPTOR; PROTEIN TYROSINE KINASE;

EID: 84884498884     PISSN: 15709639     EISSN: 18781454     Source Type: Journal    
DOI: 10.1016/j.bbapap.2012.11.011     Document Type: Review
Times cited : (37)

References (83)
  • 1
    • 84862616645 scopus 로고    scopus 로고
    • Similar but different: Ligand-induced activation of the insulin and epidermal growth factor receptor families
    • C.W. Ward, and M.C. Lawrence Similar but different: ligand-induced activation of the insulin and epidermal growth factor receptor families Curr. Opin. Struct. Biol. 22 2012 360 366
    • (2012) Curr. Opin. Struct. Biol. , vol.22 , pp. 360-366
    • Ward, C.W.1    Lawrence, M.C.2
  • 2
    • 0024461746 scopus 로고
    • Primary structure of a putative receptor for a ligand of the insulin family
    • P. Shier, and V.M. Watt Primary structure of a putative receptor for a ligand of the insulin family J. Biol. Chem. 264 1989 14605 14608 (Pubitemid 19237270)
    • (1989) Journal of Biological Chemistry , vol.264 , Issue.25 , pp. 14605-14608
    • Shier, P.1    Watt, V.M.2
  • 3
    • 0026693671 scopus 로고
    • The insulin receptor-related receptor. Tissue expression, ligand binding specificity, and signaling capabilities
    • B. Zhang, and R.A. Roth The insulin receptor-related receptor. Tissue expression, ligand binding specificity, and signaling capabilities J. Biol. Chem. 267 1992 18320 18328
    • (1992) J. Biol. Chem. , vol.267 , pp. 18320-18328
    • Zhang, B.1    Roth, R.A.2
  • 4
    • 0027930275 scopus 로고
    • Expression of a cDNA encoding the human insulin receptor-related receptor
    • H.Y. Jui, Y. Suzuki, D. Accili, and S.I. Taylor Expression of a cDNA encoding the human insulin receptor-related receptor J. Biol. Chem. 269 1994 22446 22452 (Pubitemid 24282183)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.35 , pp. 22446-22452
    • Jui, H.-Y.1    Suzuki, Y.2    Accili, D.3    Taylor, S.I.4
  • 5
    • 29344460061 scopus 로고    scopus 로고
    • Expression of the insulin receptor-related receptor is induced by the preovulatory surge of luteinizing hormone in thecal-interstitial cells of the rat ovary
    • DOI 10.1210/en.2005-0386
    • G.A. Dissen, C. Garcia-Rudaz, V. Tapia, L.F. Parada, S.Y. Hsu, and S.R. Ojeda Expression of the insulin receptor-related receptor (IRR) is induced by the preovulatory surge of LH in thecal-interstitial cells of the rat ovary Endocrinology 147 1 2005 155 165 (Pubitemid 43004270)
    • (2006) Endocrinology , vol.147 , Issue.1 , pp. 155-165
    • Dissen, G.A.1    Garcia-Rudaz, C.2    Tapia, V.3    Parada, L.F.4    Hsu, S.-Y.T.5    Ojeda, S.R.6
  • 8
    • 0021985413 scopus 로고
    • Human insulin receptor and its relationship to the tyrosine kinase family of oncogenes
    • DOI 10.1038/313756a0
    • A. Ullrich, J.R. Bell, E.Y. Chen, R. Herrera, L.M. Petruzzelli, T.J. Dull, A. Gray, L. Coussens, Y.C. Liao, and M. Tsubokawa Human insulin receptor and its relationship to the tyrosine kinase family of oncogenes Nature 313 1985 756 761 (Pubitemid 15130823)
    • (1985) Nature , vol.313 , Issue.6005 , pp. 756-761
    • Ullrich, A.1    Bell, J.R.2    Chen, E.Y.3
  • 9
    • 0022800838 scopus 로고
    • Insulin-like growth factor i receptor primary structure: Comparison with insulin receptor suggests structural determinants that define functional specificity
    • A. Ullrich, A. Gray, A.W. Tam, T. Yang-Feng, M. Tsubokawa, C. Collins, W. Henzel, T. Le Bon, S. Kathuria, and E. Chen Insulin-like growth factor I receptor primary structure: comparison with insulin receptor suggests structural determinants that define functional specificity EMBO J. 5 1986 2503 2512
    • (1986) EMBO J. , vol.5 , pp. 2503-2512
    • Ullrich, A.1    Gray, A.2    Tam, A.W.3    Yang-Feng, T.4    Tsubokawa, M.5    Collins, C.6    Henzel, W.7    Le Bon, T.8    Kathuria, S.9    Chen, E.10
  • 11
    • 0029060529 scopus 로고
    • Insulin and epidermal growth-factor receptors contain the cysteine repeat motif found in the tumor-necrosis-factor receptor
    • C.W. Ward, P.A. Hoyne, and R.H. Flegg Insulin and epidermal growth-factor receptors contain the cysteine repeat motif found in the tumor-necrosis-factor receptor Proteins 22 1995 141 153
    • (1995) Proteins , vol.22 , pp. 141-153
    • Ward, C.W.1    Hoyne, P.A.2    Flegg, R.H.3
  • 12
    • 0032410208 scopus 로고    scopus 로고
    • A third fibronectin-type-III domain in the insulin-family receptors
    • DOI 10.1016/S0968-0004(98)01288-2, PII S0968000498012882
    • T.D. Mulhern, G.W. Booker, and L. Cosgrove A third fibronectin-type-III domain in the insulin-family receptors Trends Biochem. Sci. 23 1998 465 466 (Pubitemid 29002904)
    • (1998) Trends in Biochemical Sciences , vol.23 , Issue.12 , pp. 465-466
    • Mulhern, T.D.1    Booker, G.W.2    Cosgrove, L.3
  • 13
    • 0019433697 scopus 로고
    • A unique proteolytic cleavage site on the β subunit of the insulin receptor
    • J. Massague, P.F. Pilch, and M.P. Czech A unique proteolytic cleavage site on the beta subunit of the insulin receptor J. Biol. Chem. 256 1981 3182 3190 (Pubitemid 11076974)
    • (1981) Journal of Biological Chemistry , vol.256 , Issue.7 , pp. 3182-3190
    • Massague, J.1    Pilch, P.F.2    Czech, M.P.3
  • 14
    • 48149095486 scopus 로고    scopus 로고
    • The insulin receptor: A prototype for dimeric, allosteric membrane receptors?
    • P. De Meyts The insulin receptor: a prototype for dimeric, allosteric membrane receptors? Trends Biochem. Sci. 33 2008 376 384
    • (2008) Trends Biochem. Sci. , vol.33 , pp. 376-384
    • De Meyts, P.1
  • 15
    • 0033601260 scopus 로고    scopus 로고
    • Specificity of insulin and insulin-like growth factor i receptors investigated using chimeric mini-receptors. Role of C-terminal of receptor alpha subunit
    • C. Kristensen, F.C. Wiberg, and A.S. Andersen Specificity of insulin and insulin-like growth factor I receptors investigated using chimeric mini-receptors. Role of C-terminal of receptor alpha subunit J. Biol. Chem. 274 1999 37351 37356
    • (1999) J. Biol. Chem. , vol.274 , pp. 37351-37356
    • Kristensen, C.1    Wiberg, F.C.2    Andersen, A.S.3
  • 16
    • 0034644539 scopus 로고    scopus 로고
    • Cell signaling by receptor tyrosine kinases
    • J. Schlessinger Cell signaling by receptor tyrosine kinases Cell 103 2000 211 225
    • (2000) Cell , vol.103 , pp. 211-225
    • Schlessinger, J.1
  • 17
    • 10844223660 scopus 로고    scopus 로고
    • Insulin and its receptor: Structure, function and evolution
    • DOI 10.1002/bies.20151
    • P. De Meyts Insulin and its receptor: structure, function and evolution Bioessays 26 2004 1351 1362 (Pubitemid 39664629)
    • (2004) BioEssays , vol.26 , Issue.12 , pp. 1351-1362
    • De Meyts, P.1
  • 18
    • 0024386366 scopus 로고
    • Conformational changes in the α- and β-subunits of the insulin receptor identified by anti-peptide antibodies
    • R. Perlman, D.P. Bottaro, M.F. White, and C.R. Kahn Conformational changes in the alpha- and beta-subunits of the insulin receptor identified by anti-peptide antibodies J. Biol. Chem. 264 1989 8946 8950 (Pubitemid 19151622)
    • (1989) Journal of Biological Chemistry , vol.264 , Issue.15 , pp. 8946-8950
    • Perlman, R.1    Bottaro, D.P.2    White, M.F.3    Kahn, C.R.4
  • 22
    • 0028146822 scopus 로고
    • The structural basis of insulin and insulin-like growth factor-I receptor binding and negative co-operativity, and its relevance to mitogenic versus metabolic signalling
    • P. De Meyts The structural basis of insulin and insulin-like growth factor-I receptor binding and negative co-operativity, and its relevance to mitogenic versus metabolic signalling Diabetologia 37 Suppl. 2 1994 S135 S148
    • (1994) Diabetologia , vol.37 , Issue.SUPPL. 2
    • De Meyts, P.1
  • 23
    • 0018102801 scopus 로고
    • Mapping of the residues responsible for the negative cooperativity of the receptor-binding region of insulin
    • P. De Meyts, E. Van Obberghen, and J. Roth Mapping of the residues responsible for the negative cooperativity of the receptor-binding region of insulin Nature 273 1978 504 509 (Pubitemid 8346576)
    • (1978) Nature , vol.273 , Issue.5663 , pp. 504-509
    • De Meyts, P.1    Van Obberghen, E.2    Roth, J.3
  • 24
    • 0344517365 scopus 로고    scopus 로고
    • Insulin receptor-related receptor is expressed in pancreatic β-cells and stimulates tyrosine phosphorylation of insulin receptor substrate-1 and- 2
    • DOI 10.2337/diabetes.48.6.1237
    • I. Hirayama, H. Tamemoto, H. Yokota, S.K. Kubo, J. Wang, H. Kuwano, Y. Nagamachi, T. Takeuchi, and T. Izumi Insulin receptor-related receptor is expressed in pancreatic beta-cells and stimulates tyrosine phosphorylation of insulin receptor substrate-1 and -2 Diabetes 48 1999 1237 1244 (Pubitemid 29241020)
    • (1999) Diabetes , vol.48 , Issue.6 , pp. 1237-1244
    • Hirayama, I.1    Tamemoto, H.2    Yokota, H.3    Kubo, S.-K.4    Wang, J.5    Kuwano, H.6    Nagamachi, Y.7    Takeuchi, T.8    Izumi, T.9
  • 25
    • 0033403194 scopus 로고    scopus 로고
    • A TrkB/insulin receptor-related receptor chimeric receptor induces PC12 cell differentiation and exhibits prolonged activation of mitogen-activated protein kinase
    • K.S. Kelly-Spratt, L.J. Klesse, J. Merenmies, and L.F. Parada A TrkB/insulin receptor-related receptor chimeric receptor induces PC12 cell differentiation and exhibits prolonged activation of mitogen-activated protein kinase Cell Growth Differ. 10 1999 805 812 (Pubitemid 30036252)
    • (1999) Cell Growth and Differentiation , vol.10 , Issue.12 , pp. 805-812
    • Kelly-Spratt, K.S.1    Klesse, L.J.2    Merenmies, J.3    Parada, L.F.4
  • 26
    • 0035890470 scopus 로고    scopus 로고
    • Hormone-triggered conformational changes within the insulin-receptor ectodomain: Requirement for transmembrane anchors
    • DOI 10.1042/0264-6021:3600189
    • R.R. Florke, K. Schnaith, W. Passlack, M. Wichert, L. Kuehn, M. Fabry, M. Federwisch, and H. Reinauer Hormone-triggered conformational changes within the insulin-receptor ectodomain: requirement for transmembrane anchors Biochem. J. 360 2001 189 198 (Pubitemid 33081964)
    • (2001) Biochemical Journal , vol.360 , Issue.1 , pp. 189-198
    • Florke, R.-R.1    Schnaith, K.2    Passlack, W.3    Wichert, M.4    Kuehn, L.5    Fabry, M.6    Federwisch, M.7    Reinauer, H.8
  • 27
    • 0031761387 scopus 로고    scopus 로고
    • Comparison of the signaling abilities of the cytoplasmic domains of the insulin receptor and the insulin receptor-related receptor in 3T3-L1 adipocytes
    • DOI 10.1210/en.139.8.3578
    • A.A. Dandekar, B.J. Wallach, A. Barthel, and R.A. Roth Comparison of the signaling abilities of the cytoplasmic domains of the insulin receptor and the insulin receptor-related receptor in 3T3-L1 adipocytes Endocrinology 139 1998 3578 3584 (Pubitemid 28512316)
    • (1998) Endocrinology , vol.139 , Issue.8 , pp. 3578-3584
    • Dandekar, A.A.1    Wallach, B.J.2    Barthel, A.3    Roth, R.A.4
  • 28
    • 0037100207 scopus 로고    scopus 로고
    • BDNF activated TrkB/IRR receptor chimera promotes survival of sympathetic neurons through ras and PI-3 kinase signaling
    • DOI 10.1002/jnr.10172
    • K.S. Kelly-Spratt, L.J. Klesse, and L.F. Parada BDNF activated TrkB/IRR receptor chimera promotes survival of sympathetic neurons through Ras and PI-3 kinase signaling J. Neurosci. Res. 69 2002 151 159 (Pubitemid 34734146)
    • (2002) Journal of Neuroscience Research , vol.69 , Issue.2 , pp. 151-159
    • Kelly-Spratt, K.S.1    Klesse, L.J.2    Parada, L.F.3
  • 29
    • 77954771871 scopus 로고    scopus 로고
    • Activation of Erk1/2 phosphorylation but not of Akt/Pkb through an inducible CSF1R/IRR-receptor construct in INS-1E beta-cells
    • R. Vogel, A. Garten, J. Klammt, A. Barnikol-Oettler, and W. Kiess Activation of Erk1/2 phosphorylation but not of Akt/Pkb through an inducible CSF1R/IRR-receptor construct in INS-1E beta-cells Arch. Physiol. Biochem. 116 2010 128 136
    • (2010) Arch. Physiol. Biochem. , vol.116 , pp. 128-136
    • Vogel, R.1    Garten, A.2    Klammt, J.3    Barnikol-Oettler, A.4    Kiess, W.5
  • 30
    • 0024358352 scopus 로고
    • Insulin-like growth factor I receptor β-subunit heterogeneity. Evidence for hybrid tetramers composed of insulin-like growth factor I and insulin receptor heterodimers
    • C.P. Moxham, V. Duronio, and S. Jacobs Insulin-like growth factor-I receptor beta-subunit heterogeneity - evidence for hybrid tetramers composed of insulin-like growth factor-I and insulin-receptor heterodimers J. Biol. Chem. 264 1989 13238 13244 (Pubitemid 19194902)
    • (1989) Journal of Biological Chemistry , vol.264 , Issue.22 , pp. 13238-13244
    • Moxham, C.P.1    Duronio, V.2    Jacobs, S.3
  • 31
    • 0025131648 scopus 로고
    • Receptors for insulin and insulin-like growth factor-I can form hybrid dimers. Characterisation of hybrid receptors in transfected cells
    • M.A. Soos, J. Whittaker, R. Lammers, A. Ullrich, and K. Siddle Receptors for insulin and insulin-like growth factor-I can form hybrid dimers - characterization of hybrid receptors in transfected cells Biochem. J. 270 1990 383 390 (Pubitemid 20273478)
    • (1990) Biochemical Journal , vol.270 , Issue.2 , pp. 383-390
    • Soos, M.A.1    Whittaker, J.2    Lammers, R.3    Ullrich, A.4    Siddle, K.5
  • 32
    • 0037131385 scopus 로고    scopus 로고
    • Insulin/insulin-like growth factor I hybrid receptors have different biological characteristics depending on the insulin receptor isoform involved
    • DOI 10.1074/jbc.M202766200
    • G. Pandini, F. Frasca, R. Mineo, L. Sciacca, R. Vigneri, and A. Belfiore Insulin/insulin-like growth factor I hybrid receptors have different biological characteristics depending on the insulin receptor isoform involved J. Biol. Chem. 277 2002 39684 39695 (Pubitemid 35190951)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.42 , pp. 39684-39695
    • Pandini, G.1    Frasca, F.2    Mineo, R.3    Sciacca, L.4    Vigneri, R.5    Belfiore, A.6
  • 33
    • 0029828766 scopus 로고    scopus 로고
    • Characterization of a hybrid receptor formed by dimerization of the insulin receptor-related receptor (IRR) with the insulin receptor (IR): Coexpression of cDNAs encoding human IRR and human IR in NIH-3T3 cells
    • DOI 10.1021/bi9613032
    • H.Y. Jui, D. Accili, and S.I. Taylor Characterization of a hybrid receptor formed by dimerization of the insulin receptor-related receptor (IRR) with the insulin receptor (IR): coexpression of cDNAs encoding human IRR and human IR in NIH-3T3 cells Biochemistry 35 1996 14326 14330 (Pubitemid 26384429)
    • (1996) Biochemistry , vol.35 , Issue.45 , pp. 14326-14330
    • Jui, H.-Y.1    Accili, D.2    Taylor, S.I.3
  • 35
    • 80054787148 scopus 로고    scopus 로고
    • New insights into the characteristics of sweet and bitter taste receptors
    • P.A. Temussi New insights into the characteristics of sweet and bitter taste receptors Int. Rev. Cell Mol. Biol. 291 2011 191 226
    • (2011) Int. Rev. Cell Mol. Biol. , vol.291 , pp. 191-226
    • Temussi, P.A.1
  • 36
    • 0019975497 scopus 로고
    • + exchanger in renal microvillus membrane vesicles
    • DOI 10.1038/299161a0
    • + exchanger in renal microvillus membrane vesicles Nature 299 1982 161 163 (Pubitemid 12056792)
    • (1982) Nature , vol.299 , Issue.5879 , pp. 161-163
    • Aronson, P.S.1    Nee, J.2    Suhm, M.A.3
  • 37
    • 0000004237 scopus 로고    scopus 로고
    • Renal acidification mechanisms
    • R.J. Alpern Renal acidification mechanisms Kidney 2000 455 519
    • (2000) Kidney , pp. 455-519
    • Alpern, R.J.1
  • 38
    • 0025055465 scopus 로고
    • Cell mechanisms of proximal tubule acidification
    • R.J. Alpern Cell mechanisms of proximal tubule acidification Physiol. Rev. 70 1990 79 114 (Pubitemid 20037282)
    • (1990) Physiological Reviews , vol.70 , Issue.1 , pp. 79-114
    • Alpern, R.J.1
  • 39
    • 0017699888 scopus 로고
    • Bicarbonate transport by rabbit cortical collecting tubules. Effect of acid and alkali loads in vivo on transport in vitro
    • T.D. McKinney, and M.B. Burg Bicarbonate transport by rabbit cortical collecting tubules. Effect of acid and alkali loads in vivo on transport in vitro J. Clin. Investig. 60 1977 766 768 (Pubitemid 8180882)
    • (1977) Journal of Clinical Investigation , vol.60 , Issue.3 , pp. 766-768
    • McKinney, T.D.1    Burg, M.B.2
  • 40
    • 0022137179 scopus 로고
    • Bicarbonate transport by isolated perfused rat collecting ducts
    • J.L. Atkins, and M.B. Burg Bicarbonate transport by isolated perfused rat collecting ducts Am. J. Physiol. 249 1985 F485 F489
    • (1985) Am. J. Physiol. , vol.249
    • Atkins, J.L.1    Burg, M.B.2
  • 41
    • 0020680992 scopus 로고
    • Effects of extracellular fluid volume and plasma bicarbonate concentration on proximal acidification in the rat
    • R.J. Alpern, M.G. Cogan, and F.C. Rector Jr. Effects of extracellular fluid volume and plasma bicarbonate concentration on proximal acidification in the rat J. Clin. Invest. 71 1983 736 746 (Pubitemid 13160822)
    • (1983) Journal of Clinical Investigation , vol.71 , Issue.3 , pp. 736-746
    • Alpern, R.J.1    Cogan, M.G.2    Rector Jr., F.C.3
  • 42
    • 0036083586 scopus 로고    scopus 로고
    • Rat proximal NHE3 adapts to chronic acid-base disorders but not to chronic changes in dietary NaCl intake
    • D. Eladari, F. Leviel, F. Pezy, M. Paillard, and R. Chambrey Rat proximal NHE3 adapts to chronic acid-base disorders but not to chronic changes in dietary NaCl intake Am. J. Physiol. Renal Physiol. 282 2002 F835 F843
    • (2002) Am. J. Physiol. Renal Physiol. , vol.282
    • Eladari, D.1    Leviel, F.2    Pezy, F.3    Paillard, M.4    Chambrey, R.5
  • 44
    • 84860629012 scopus 로고    scopus 로고
    • Molecular mechanisms of acid-base sensing by the kidney
    • D. Brown, and C.A. Wagner Molecular mechanisms of acid-base sensing by the kidney J. Am. Soc. Nephrol. 23 2012 774 780
    • (2012) J. Am. Soc. Nephrol. , vol.23 , pp. 774-780
    • Brown, D.1    Wagner, C.A.2
  • 45
    • 78549266789 scopus 로고    scopus 로고
    • Physiological carbon dioxide, bicarbonate, and pH sensing
    • M. Tresguerres, J. Buck, and L.R. Levin Physiological carbon dioxide, bicarbonate, and pH sensing Pflugers Arch. 460 2010 953 964
    • (2010) Pflugers Arch. , vol.460 , pp. 953-964
    • Tresguerres, M.1    Buck, J.2    Levin, L.R.3
  • 46
    • 70349916098 scopus 로고    scopus 로고
    • Acid-sensitive ion channels and receptors
    • P. Holzer Acid-sensitive ion channels and receptors Handb. Exp. Pharmacol. 2009 283 332
    • (2009) Handb. Exp. Pharmacol. , pp. 283-332
    • Holzer, P.1
  • 47
    • 84861792317 scopus 로고    scopus 로고
    • Acidosis, acid-sensing ion channels, and neuronal cell death
    • Y.Z. Wang, and T.L. Xu Acidosis, acid-sensing ion channels, and neuronal cell death Mol. Neurobiol. 44 2011 350 358
    • (2011) Mol. Neurobiol. , vol.44 , pp. 350-358
    • Wang, Y.Z.1    Xu, T.L.2
  • 49
    • 84864656610 scopus 로고    scopus 로고
    • Human ASIC3 channel dynamically adapts its activity to sense the extracellular pH in both acidic and alkaline directions
    • A. Delaunay, X. Gasull, M. Salinas, J. Noel, V. Friend, E. Lingueglia, and E. Deval Human ASIC3 channel dynamically adapts its activity to sense the extracellular pH in both acidic and alkaline directions Proc. Natl. Acad. Sci. U. S. A. 109 2012 13124 13129
    • (2012) Proc. Natl. Acad. Sci. U. S. A. , vol.109 , pp. 13124-13129
    • Delaunay, A.1    Gasull, X.2    Salinas, M.3    Noel, J.4    Friend, V.5    Lingueglia, E.6    Deval, E.7
  • 50
    • 0030946297 scopus 로고    scopus 로고
    • A proton-gated cation channel involved in acid-sensing
    • DOI 10.1038/386173a0
    • R. Waldmann, G. Champigny, F. Bassilana, C. Heurteaux, and M. Lazdunski A proton-gated cation channel involved in acid-sensing Nature 386 1997 173 177 (Pubitemid 27131444)
    • (1997) Nature , vol.386 , Issue.6621 , pp. 173-177
    • Waldmann, R.1    Champigny, G.2    Bassilana, F.3    Heurteaux, C.4    Lazdunski, M.5
  • 51
    • 0019185036 scopus 로고
    • A receptor for protons in the nerve cell membrane
    • DOI 10.1016/0306-4522(80)90149-9
    • O.A. Krishtal, and V.I. Pidoplichko A receptor for protons in the nerve cell membrane Neuroscience 5 1980 2325 2327 (Pubitemid 11200029)
    • (1980) Neuroscience , vol.5 , Issue.12 , pp. 2325-2327
    • Krishtal, O.A.1    Pidoplichko, V.I.2
  • 52
    • 0042926849 scopus 로고    scopus 로고
    • The ASICs: Signaling molecules? Modulators?
    • DOI 10.1016/S0166-2236(03)00210-8
    • O. Krishtal The ASICs: signaling molecules? Modulators? Trends Neurosci. 26 2003 477 483 (Pubitemid 37025785)
    • (2003) Trends in Neurosciences , vol.26 , Issue.9 , pp. 477-483
    • Krishtal, O.1
  • 53
    • 15044354555 scopus 로고    scopus 로고
    • Pyk2 activation is integral to acid stimulation of sodium/hydrogen exchanger 3
    • DOI 10.1172/JCI200418046
    • S.Y. Li, S. Sato, X.J. Yang, P.A. Preisig, and R.J. Alpern Pyk2 activation is integral to acid stimulation of sodium/hydrogen exchanger 3 J. Clin. Invest. 114 2004 1782 1789 (Pubitemid 40385534)
    • (2004) Journal of Clinical Investigation , vol.114 , Issue.12 , pp. 1782-1789
    • Li, S.1    Sato, S.2    Yang, X.3    Preisig, P.A.4    Alpern, R.J.5
  • 54
    • 15244351172 scopus 로고    scopus 로고
    • Acid sensing in renal epithelial cells
    • DOI 10.1172/JCI200423864
    • S.L. Gluck Acid sensing in renal epithelial cells J. Clin. Invest. 114 2004 1696 1699 (Pubitemid 40385524)
    • (2004) Journal of Clinical Investigation , vol.114 , Issue.12 , pp. 1696-1699
    • Gluck, S.L.1
  • 55
    • 44649147805 scopus 로고    scopus 로고
    • Evolution of the insulin receptor family and receptor isoform expression in vertebrates
    • C. Hernandez-Sanchez, A. Mansilla, F. de Pablo, and R. Zardoya Evolution of the insulin receptor family and receptor isoform expression in vertebrates Mol. Biol. Evol. 25 2008 1043 1053
    • (2008) Mol. Biol. Evol. , vol.25 , pp. 1043-1053
    • Hernandez-Sanchez, C.1    Mansilla, A.2    De Pablo, F.3    Zardoya, R.4
  • 56
    • 56349123217 scopus 로고    scopus 로고
    • A comparative structural bioinformatics analysis of the insulin receptor family ectodomain based on phylogenetic information
    • M.E. Renteria, N.S. Gandhi, P. Vinuesa, E. Helmerhorst, and R.L. Mancera A comparative structural bioinformatics analysis of the insulin receptor family ectodomain based on phylogenetic information PLoS One 3 2008 e3667
    • (2008) PLoS One , vol.3 , pp. 3667
    • Renteria, M.E.1    Gandhi, N.S.2    Vinuesa, P.3    Helmerhorst, E.4    Mancera, R.L.5
  • 57
    • 0034941125 scopus 로고    scopus 로고
    • Preserved pancreatic β-cell development and function in mice lacking the insulin receptor-related receptor
    • DOI 10.1128/MCB.21.16.5624-5630.2001
    • T. Kitamura, Y. Kido, S. Nef, J. Merenmies, L.F. Parada, and D. Accili Preserved pancreatic beta-cell development and function in mice lacking the insulin receptor-related receptor Mol. Cell. Biol. 21 2001 5624 5630 (Pubitemid 32702465)
    • (2001) Molecular and Cellular Biology , vol.21 , Issue.16 , pp. 5624-5630
    • Kitamura, T.1    Kido, Y.2    Nef, S.3    Merenmies, J.4    Parada, L.F.5    Accili, D.6
  • 59
    • 0029097571 scopus 로고
    • Insulin receptor-related receptor messenger ribonucleic acid: Quantitative distribution and localization to subpopulations of epithelial cells in stomach and kidney
    • S.K. Mathi, J. Chan, and V.M. Watt Insulin receptor-related receptor messenger ribonucleic acid: quantitative distribution and localization to subpopulations of epithelial cells in stomach and kidney Endocrinology 136 1995 4125 4132
    • (1995) Endocrinology , vol.136 , pp. 4125-4132
    • Mathi, S.K.1    Chan, J.2    Watt, V.M.3
  • 60
    • 0030847375 scopus 로고    scopus 로고
    • Insulin receptor-related receptor expression in non-A intercalated cells in the kidney
    • C.M. Bates, J.M. Merenmies, K.S. Kelly-Spratt, and L.F. Parada Insulin receptor-related receptor expression in non-A intercalated cells in the kidney Kidney Int. 52 1997 674 681 (Pubitemid 27402365)
    • (1997) Kidney International , vol.52 , Issue.3 , pp. 674-681
    • Bates, C.M.1    Merenmies, J.M.2    Kelly-Spratt, K.S.3    Parada, L.F.4
  • 62
    • 79951802711 scopus 로고    scopus 로고
    • Terminal differentiation in epithelia: The role of integrins in hensin polymerization
    • Q. Al-Awqati Terminal differentiation in epithelia: the role of integrins in hensin polymerization Annu. Rev. Physiol. 73 2011 401 412
    • (2011) Annu. Rev. Physiol. , vol.73 , pp. 401-412
    • Al-Awqati, Q.1
  • 63
    • 0025738533 scopus 로고
    • Expression and distribution of renal vacuolar proton-translocating adenosine triphosphatase in response to chronic acid and alkali loads in the rat
    • B. Bastani, H. Purcell, P. Hemken, D. Trigg, and S. Gluck Expression and distribution of renal vacuolar proton-translocating adenosine triphosphatase in response to chronic acid and alkali loads in the rat J. Clin. Invest. 88 1991 126 136
    • (1991) J. Clin. Invest. , vol.88 , pp. 126-136
    • Bastani, B.1    Purcell, H.2    Hemken, P.3    Trigg, D.4    Gluck, S.5
  • 64
    • 0031047916 scopus 로고    scopus 로고
    • +-ATPase in rat cortex by acute metabolic acidosis and alkalosis
    • I. Sabolic, D. Brown, S.L. Gluck, and S.L. Alper Regulation of AE1 anion exchanger and H(+)-ATPase in rat cortex by acute metabolic acidosis and alkalosis Kidney Int. 51 1997 125 137 (Pubitemid 27064530)
    • (1997) Kidney International , vol.51 , Issue.1 , pp. 125-137
    • Sabolic, I.1    Brown, D.2    Gluck, S.L.3    Alper, S.L.4
  • 68
    • 0031000787 scopus 로고    scopus 로고
    • The chloride cell: Structure and function in the gills of freshwater fishes
    • DOI 10.1146/annurev.physiol.59.1.325
    • S.F. Perry The chloride cell: structure and function in the gills of freshwater fishes Annu. Rev. Physiol. 59 1997 325 347 (Pubitemid 27142445)
    • (1997) Annual Review of Physiology , vol.59 , pp. 325-347
    • Perry, S.F.1
  • 72
    • 84857254245 scopus 로고    scopus 로고
    • A new look at electrolyte transport in the distal tubule
    • D. Eladari, R. Chambrey, and J. Peti-Peterdi A new look at electrolyte transport in the distal tubule Annu. Rev. Physiol. 74 2012 325 349
    • (2012) Annu. Rev. Physiol. , vol.74 , pp. 325-349
    • Eladari, D.1    Chambrey, R.2    Peti-Peterdi, J.3
  • 74
    • 0042333487 scopus 로고    scopus 로고
    • Deoxycorticosterone upregulates PDS (Slc26a4) in mouse kidney: Role of pendrin in mineralocorticoid-induced hypertension
    • DOI 10.1161/01.HYP.0000088321.67254.B7
    • J.W. Verlander, K.A. Hassell, I.E. Royaux, D.M. Glapion, M.E. Wang, L.A. Everett, E.D. Green, and S.M. Wall Deoxycorticosterone upregulates PDS (Slc26a4) in mouse kidney: role of pendrin in mineralocorticoid-induced hypertension Hypertension 42 2003 356 362 (Pubitemid 37093485)
    • (2003) Hypertension , vol.42 , Issue.3 , pp. 356-362
    • Verlander, J.W.1    Hassell, K.A.2    Royaux, I.E.3    Glapion, D.M.4    Wang, M.-E.5    Everett, L.A.6    Green, E.D.7    Wall, S.M.8
  • 75
    • 0028931897 scopus 로고
    • Insulin receptor-related receptor messenger ribonucleic acid in the stomach is focally expressed in the enterochromaffin-like cells
    • K. Tsujimoto, N. Tsuji, K. Ozaki, M. Ohta, and N. Itoh Insulin receptor-related receptor messenger ribonucleic acid in the stomach is focally expressed in the enterochromaffin-like cells Endocrinology 136 1995 558 561
    • (1995) Endocrinology , vol.136 , pp. 558-561
    • Tsujimoto, K.1    Tsuji, N.2    Ozaki, K.3    Ohta, M.4    Itoh, N.5
  • 76
    • 0027284049 scopus 로고
    • Insulin receptor-related receptor messenger ribonucleic acid is focally expressed in sympathetic and sensory neurons and renal distal tubule cells
    • DOI 10.1210/en.133.1.3
    • R.R. Reinhardt, E. Chin, B. Zhang, R.A. Roth, and C.A. Bondy Insulin receptor-related receptor messenger ribonucleic acid is focally expressed in sympathetic and sensory neurons and renal distal tubule cells Endocrinology 133 1993 3 10 (Pubitemid 23206367)
    • (1993) Endocrinology , vol.133 , Issue.1 , pp. 3-10
    • Reinhardt, R.R.1    Chin, E.2    Zhang, B.3    Roth, R.A.4    Bondy, C.A.5
  • 77
    • 0031867093 scopus 로고    scopus 로고
    • Insulin receptor-related receptor in rat islets of Langerhans
    • K. Ozaki Insulin receptor-related receptor in rat islets of Langerhans Eur. J. Endocrinol. 139 1998 244 247 (Pubitemid 28389686)
    • (1998) European Journal of Endocrinology , vol.139 , Issue.2 , pp. 244-247
    • Ozaki, K.1
  • 78
    • 24344482429 scopus 로고    scopus 로고
    • Association between endocrine pancreas and ductal system. More than an epiphenomenon of endocrine differentiation and development?
    • DOI 10.1369/jhc.5R6640.2005
    • E. Bertelli, and M. Bendayan Association between endocrine pancreas and ductal system. More than an epiphenomenon of endocrine differentiation and development? J. Histochem. Cytochem. 53 2005 1071 1086 (Pubitemid 41262976)
    • (2005) Journal of Histochemistry and Cytochemistry , vol.53 , Issue.9 , pp. 1071-1086
    • Bertelli, E.1    Bendayan, M.2
  • 79
    • 0028087895 scopus 로고
    • Selective coexpression of insulin receptor-related receptor (IRR) and TRK in NGF-sensitive neurons
    • R.R. Reinhardt, E. Chin, B. Zhang, R.A. Roth, and C.A. Bondy Selective coexpression of insulin receptor-related receptor (IRR) and TRK in NGF-sensitive neurons J. Neurosci. 14 1994 4674 4683 (Pubitemid 24237890)
    • (1994) Journal of Neuroscience , vol.14 , Issue.8 , pp. 4674-4683
    • Reinhardt, R.R.1    Chin, E.2    Zhang, B.3    Roth, R.A.4    Bondy, C.A.5
  • 80
    • 0033828503 scopus 로고    scopus 로고
    • Molecular characterization of the TrkA/NGF receptor minimal enhancer reveals regulation by multiple cis elements to drive embryonic neuron expression
    • L. Ma, J. Merenmies, and L.F. Parada Molecular characterization of the TrkA/NGF receptor minimal enhancer reveals regulation by multiple cis elements to drive embryonic neuron expression Development 127 2000 3777 3788
    • (2000) Development , vol.127 , pp. 3777-3788
    • Ma, L.1    Merenmies, J.2    Parada, L.F.3
  • 81
    • 0141863313 scopus 로고    scopus 로고
    • Regulation and modulation of pH in the brain
    • M. Chesler Regulation and modulation of pH in the brain Physiol. Rev. 83 2003 1183 1221 (Pubitemid 37222271)
    • (2003) Physiological Reviews , vol.83 , Issue.4 , pp. 1183-1221
    • Chesler, M.1
  • 82
    • 0026440558 scopus 로고
    • Extracellular alkalinity exacerbates injury of cultured cortical neurons
    • R.G. Giffard, J.H. Weiss, and D.W. Choi Extracellular alkalinity exacerbates injury of cultured cortical neurons Stroke 23 1992 1817 1821
    • (1992) Stroke , vol.23 , pp. 1817-1821
    • Giffard, R.G.1    Weiss, J.H.2    Choi, D.W.3
  • 83
    • 5444244399 scopus 로고    scopus 로고
    • Hypoglycemic brain damage
    • DOI 10.1023/B:MEBR.0000043967.78763.5b
    • R.N. Auer Hypoglycemic brain damage Metab. Brain Dis. 19 2004 169 175 (Pubitemid 39361179)
    • (2004) Metabolic Brain Disease , vol.19 , Issue.3-4 , pp. 169-175
    • Auer, R.N.1


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