메뉴 건너뛰기




Volumn 287, Issue 5 56-5, 2004, Pages

FHL5, a novel actin-binding protein, is highly expressed in eel gill pillar cells and responds to wall tension

Author keywords

C2C12 myoblast; Endothelin; Four and a half LIM; Immunohistochemistry; Lamella; Zinc finger

Indexed keywords

ACTIN BINDING PROTEIN; COMPLEMENTARY DNA; DEXTRAN; ENDOTHELIN 1; LIM PROTEIN; MESSENGER RNA; PHALLOIDIN; PROTEIN FHL5; RHODAMINE; SODIUM CHLORIDE; UNCLASSIFIED DRUG;

EID: 6344276759     PISSN: 03636119     EISSN: None     Source Type: Journal    
DOI: 10.1152/ajpregu.00108.2004     Document Type: Article
Times cited : (24)

References (68)
  • 2
    • 0034004352 scopus 로고    scopus 로고
    • The LIM domain: Regulation by association
    • Bach I. The LIM domain: regulation by association. Mech Dev 91: 5-17, 2000.
    • (2000) Mech Dev , vol.91 , pp. 5-17
    • Bach, I.1
  • 3
    • 0015885760 scopus 로고
    • Contractile filamentous material in the pillar cells of fish gills
    • Bettex-Galland M and Hughes GM. Contractile filamentous material in the pillar cells of fish gills. J Cell Sci 13: 359-370, 1973.
    • (1973) J Cell Sci , vol.13 , pp. 359-370
    • Bettex-Galland, M.1    Hughes, G.M.2
  • 6
    • 0033578613 scopus 로고    scopus 로고
    • Characterization of two isoforms of the skeletal muscle LIM protein 1, SLIM1. Localization of SLIM1 at focal adhesions and the isoform slimmer in the nucleus of myoblasts and cytoplasm of myotubes suggests distinct roles in the cytoskeleton and in nuclear-cytoplasmic communication
    • Brown S, McGrath MJ, Ooms LM, Gurung R, Maimone MM, and Mitchell CA. Characterization of two isoforms of the skeletal muscle LIM protein 1, SLIM1. Localization of SLIM1 at focal adhesions and the isoform slimmer in the nucleus of myoblasts and cytoplasm of myotubes suggests distinct roles in the cytoskeleton and in nuclear-cytoplasmic communication. J Biol Chem 274: 27083-27091, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 27083-27091
    • Brown, S.1    McGrath, M.J.2    Ooms, L.M.3    Gurung, R.4    Maimone, M.M.5    Mitchell, C.A.6
  • 7
    • 0018639079 scopus 로고
    • Isolation of biologically active ribonucleic acid from sources enriched in ribonuclease
    • Chirgwin JM, Przybyla AE, MacDonald RJ, and Rutter WJ. Isolation of biologically active ribonucleic acid from sources enriched in ribonuclease. Biochemistry 18: 5294-5299, 1979.
    • (1979) Biochemistry , vol.18 , pp. 5294-5299
    • Chirgwin, J.M.1    Przybyla, A.E.2    MacDonald, R.J.3    Rutter, W.J.4
  • 8
    • 0034234785 scopus 로고    scopus 로고
    • Expression patterns of FHL/SLIM family members suggest important functional roles in skeletal muscle and cardiovascular system
    • Chu PH, Ruiz-Lozano P, Zhou Q, Cai C, and Chen J. Expression patterns of FHL/SLIM family members suggest important functional roles in skeletal muscle and cardiovascular system. Mech Dev 95: 259-265, 2000.
    • (2000) Mech Dev , vol.95 , pp. 259-265
    • Chu, P.H.1    Ruiz-Lozano, P.2    Zhou, Q.3    Cai, C.4    Chen, J.5
  • 9
    • 0038605975 scopus 로고    scopus 로고
    • FHL3 is an actin-binding protein that regulates α-actinin-mediated actin bundling: FHL3 localizes to actin stress fibers and enhances cell spreading and stress fiber disassembly
    • Coghill ID, Brown S, Cottle DL, McGrath MJ, Robinson PA, Nandurkar HH, Dyson JM, and Mitchell CA. FHL3 is an actin-binding protein that regulates α-actinin-mediated actin bundling: FHL3 localizes to actin stress fibers and enhances cell spreading and stress fiber disassembly. J Biol Chem 278: 24139-24152, 2003.
    • (2003) J Biol Chem , vol.278 , pp. 24139-24152
    • Coghill, I.D.1    Brown, S.2    Cottle, D.L.3    McGrath, M.J.4    Robinson, P.A.5    Nandurkar, H.H.6    Dyson, J.M.7    Mitchell, C.A.8
  • 10
    • 0023427610 scopus 로고
    • Effects of cytochalasin and phalloidin on actin
    • Cooper JA. Effects of cytochalasin and phalloidin on actin. J Cell Biol 105: 1473-1478, 1987.
    • (1987) J Cell Biol , vol.105 , pp. 1473-1478
    • Cooper, J.A.1
  • 11
    • 0037389558 scopus 로고    scopus 로고
    • Mitogen-activated protein kinases: New signaling pathways functioning in cellular responses to environmental stress
    • Cowan KJ and Storey KB. Mitogen-activated protein kinases: new signaling pathways functioning in cellular responses to environmental stress. J Exp Biol 206: 1107-1115, 2003.
    • (2003) J Exp Biol , vol.206 , pp. 1107-1115
    • Cowan, K.J.1    Storey, K.B.2
  • 12
    • 0033548233 scopus 로고    scopus 로고
    • Stress-activated protein kinase-2/p38 and a rapamycin-sensitive pathway are required for C2C12 myogenesis
    • Cuenda A and Cohen P. Stress-activated protein kinase-2/p38 and a rapamycin-sensitive pathway are required for C2C12 myogenesis. J Biol Chem 274: 4341-4346, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 4341-4346
    • Cuenda, A.1    Cohen, P.2
  • 13
    • 0033167907 scopus 로고    scopus 로고
    • Signaling routes to CREM and CREB: Plasticity in transcriptional activation
    • De Cesare D, Fimia GM, and Sassone-Corsi P. Signaling routes to CREM and CREB: plasticity in transcriptional activation. Trends Biochem Sci 24: 281-285, 1999.
    • (1999) Trends Biochem Sci , vol.24 , pp. 281-285
    • De Cesare, D.1    Fimia, G.M.2    Sassone-Corsi, P.3
  • 14
    • 0037136244 scopus 로고    scopus 로고
    • The LIM-only coactivator FHL2 modulates WT1 transcriptional activity during gonadal differentiation
    • Du X, Hublitz P, Gunther T, Wilhelm D, Englert C, and Schule R. The LIM-only coactivator FHL2 modulates WT1 transcriptional activity during gonadal differentiation. Biochim Biophys Acta 1577: 93-101, 2002.
    • (2002) Biochim Biophys Acta , vol.1577 , pp. 93-101
    • Du, X.1    Hublitz, P.2    Gunther, T.3    Wilhelm, D.4    Englert, C.5    Schule, R.6
  • 15
    • 0033403114 scopus 로고    scopus 로고
    • B receptor in the gill of the dogfish shark Squalus acanthias
    • B receptor in the gill of the dogfish shark Squalus acanthias. J Exp Biol 202: 3605-3610, 1999.
    • (1999) J Exp Biol , vol.202 , pp. 3605-3610
    • Evans, D.H.1    Gunderson, M.P.2
  • 16
    • 0033545640 scopus 로고    scopus 로고
    • CBP-independent activation of CREM and CREB by the LIM-only protein ACT
    • Fimia GM, De Cesare D, and Sassone-Corsi P. CBP-independent activation of CREM and CREB by the LIM-only protein ACT. Nature 398: 165-169, 1999.
    • (1999) Nature , vol.398 , pp. 165-169
    • Fimia, G.M.1    De Cesare, D.2    Sassone-Corsi, P.3
  • 17
    • 0033766856 scopus 로고    scopus 로고
    • A family of LIM-only transcriptional coactivators: Tissue-specific expression and selective activation of CREB and CREM
    • Fimia GM, De Cesare D, and Sassone-Corsi P. A family of LIM-only transcriptional coactivators: tissue-specific expression and selective activation of CREB and CREM. Mol Cell Biol 20: 8613-8622, 2000.
    • (2000) Mol Cell Biol , vol.20 , pp. 8613-8622
    • Fimia, G.M.1    De Cesare, D.2    Sassone-Corsi, P.3
  • 18
    • 0014676477 scopus 로고
    • Note on innervation of the gills in Anguilla anguilla L
    • Gilloteaux J. Note on innervation of the gills in Anguilla anguilla L. Experientia 25: 270-271, 1969.
    • (1969) Experientia , vol.25 , pp. 270-271
    • Gilloteaux, J.1
  • 19
    • 0033620624 scopus 로고    scopus 로고
    • Genomic structure, tissue expression and chromosomal location of the LIM-only gene, SLIM1
    • Greene WK, Baker E, Rabbitts TH, and Kees UR. Genomic structure, tissue expression and chromosomal location of the LIM-only gene, SLIM1. Gene 232: 203-207, 1999.
    • (1999) Gene , vol.232 , pp. 203-207
    • Greene, W.K.1    Baker, E.2    Rabbitts, T.H.3    Kees, U.R.4
  • 20
    • 0034016121 scopus 로고    scopus 로고
    • Effects of endothelin-1 and homologous trout endothelin on cardiovascular function in rainbow trout
    • Hoagland TM, Weaver L Jr, Conlon JM, Wang Y, and Olson KR. Effects of endothelin-1 and homologous trout endothelin on cardiovascular function in rainbow trout. Am J Physiol Regul Integr Comp Physiol 278: R460-R468, 2000.
    • (2000) Am J Physiol Regul Integr Comp Physiol , vol.278
  • 21
    • 0342370655 scopus 로고
    • Gills, edited by Houlihan DF, Rankin JC, and Shuttleworth TJ. London, UK: Cambridge Univ Press
    • Hughes GM. An introduction to the study of gills. In: Gills, edited by Houlihan DF, Rankin JC, and Shuttleworth TJ. London, UK: Cambridge Univ Press, 1982, p. 1-24.
    • (1982) An Introduction to the Study of Gills , pp. 1-24
    • Hughes, G.M.1
  • 22
    • 6344247893 scopus 로고
    • The fine structure of the secondary lamellae of the gills of Gadus pollachius
    • Hughes GM and Grimstone AV. The fine structure of the secondary lamellae of the gills of Gadus pollachius. Q J Microsc Sci 106: 343-353, 1965.
    • (1965) Q J Microsc Sci , vol.106 , pp. 343-353
    • Hughes, G.M.1    Grimstone, A.V.2
  • 23
    • 0034957412 scopus 로고    scopus 로고
    • Mitogen-activated protein kinases are in vivo transducers of osmosensory signals in fish gill cells
    • Kultz D and Avila K. Mitogen-activated protein kinases are in vivo transducers of osmosensory signals in fish gill cells. Comp Biochem Physiol B Biochem Mol Biol 129: 821-829, 2001.
    • (2001) Comp Biochem Physiol B Biochem Mol Biol , vol.129 , pp. 821-829
    • Kultz, D.1    Avila, K.2
  • 24
    • 0032214489 scopus 로고    scopus 로고
    • Evolution of osmotic stress signaling via MAP kinase cascades
    • Kultz D and Burg M. Evolution of osmotic stress signaling via MAP kinase cascades. J Exp Biol 201: 3015-3021, 1998.
    • (1998) J Exp Biol , vol.201 , pp. 3015-3021
    • Kultz, D.1    Burg, M.2
  • 25
    • 0032580152 scopus 로고    scopus 로고
    • A molecular timescale for vertebrate evolution
    • Kumar S and Hedges SB. A molecular timescale for vertebrate evolution. Nature 392: 917-920, 1998.
    • (1998) Nature , vol.392 , pp. 917-920
    • Kumar, S.1    Hedges, S.B.2
  • 26
    • 0036139211 scopus 로고    scopus 로고
    • EGA2: Molecular evolutionary genetics analysis software
    • Kumar S, Tamura K, Jakobsen IB, and Nei M. MEGA2: molecular evolutionary genetics analysis software. Bioinformatics 17: 1244-1245, 2001.
    • (2001) Bioinformatics , vol.17 , pp. 1244-1245
    • Kumar, S.1    Tamura, K.2    Jakobsen, I.B.3    Nei, M.M.4
  • 28
    • 0032906624 scopus 로고    scopus 로고
    • Central and peripheral administration of endothelin-1 induces an increase in blood pressure in conscious trout
    • le Mevel JC, Delarue C, Mabin D, and Vaudry H. Central and peripheral administration of endothelin-1 induces an increase in blood pressure in conscious trout. Am J Physiol Regul Integr Comp Physiol 276: R1010-R1017, 1999.
    • (1999) Am J Physiol Regul Integr Comp Physiol , vol.276
    • Le Mevel, J.C.1    Delarue, C.2    Mabin, D.3    Vaudry, H.4
  • 29
    • 0035173456 scopus 로고    scopus 로고
    • Translocation of a human focal adhesion LIM-only protein, FHL2, during myofibrillogenesis and identification of LIM2 as the principal determinants of FHL2 focal adhesion localization
    • Li HY, Kotaka M, Kostin S, Lee SM, Kok LD, Chan KK, Tsui SK, Schaper J, Zimmermann R, Lee CY, Fung KP, and Waye MM. Translocation of a human focal adhesion LIM-only protein, FHL2, during myofibrillogenesis and identification of LIM2 as the principal determinants of FHL2 focal adhesion localization. Cell Motil Cytoskeleton 48: 11-23, 2001.
    • (2001) Cell Motil Cytoskeleton , vol.48 , pp. 11-23
    • Li, H.Y.1    Kotaka, M.2    Kostin, S.3    Lee, S.M.4    Kok, L.D.5    Chan, K.K.6    Tsui, S.K.7    Schaper, J.8    Zimmermann, R.9    Lee, C.Y.10    Kp, F.11    Waye, M.M.12
  • 30
    • 0034801287 scopus 로고    scopus 로고
    • Expression profiling of cardiac genes in human hypertrophic cardiomyopathy: Insight into the pathogenesis of phenotypes
    • Lim DS, Roberts R, and Marian AJ. Expression profiling of cardiac genes in human hypertrophic cardiomyopathy: insight into the pathogenesis of phenotypes. J Am Coll Cardiol 38: 1175-1180, 2001.
    • (2001) J Am Coll Cardiol , vol.38 , pp. 1175-1180
    • Lim, D.S.1    Roberts, R.2    Marian, A.J.3
  • 31
    • 0029134919 scopus 로고
    • Localization and characterization of a novel receptor for endothelin in the gills of the rainbow trout
    • Lodhi KM, Sakaguchi H, Hirose S, and Hagiwara H. Localization and characterization of a novel receptor for endothelin in the gills of the rainbow trout. J Biochem (Tokyo) 118: 376-379, 1995.
    • (1995) J Biochem (Tokyo) , vol.118 , pp. 376-379
    • Lodhi, K.M.1    Sakaguchi, H.2    Hirose, S.3    Hagiwara, H.4
  • 32
    • 0033920601 scopus 로고    scopus 로고
    • The LIM-domain protein FHL1 (SLIM 1) exhibits functional regulation in skeletal muscle
    • Loughna PT, Mason P, Bayol S, and Brownson C. The LIM-domain protein FHL1 (SLIM 1) exhibits functional regulation in skeletal muscle. Mol Cell Biol Res Commun 3: 136-140, 2000.
    • (2000) Mol Cell Biol Res Commun , vol.3 , pp. 136-140
    • Loughna, P.T.1    Mason, P.2    Bayol, S.3    Brownson, C.4
  • 33
    • 0028987867 scopus 로고
    • Possible role of endothelin in endothelial regulation of vascular tone
    • Masaki T. Possible role of endothelin in endothelial regulation of vascular tone. Annu Rev Pharmacol Toxicol 35: 235-255, 1995.
    • (1995) Annu Rev Pharmacol Toxicol , vol.35 , pp. 235-255
    • Masaki, T.1
  • 34
    • 0347093483 scopus 로고    scopus 로고
    • LIM-domain-binding protein 1: A multifunctional cofactor that interacts with diverse proteins
    • Matthews JM and Visvader JE. LIM-domain-binding protein 1: a multifunctional cofactor that interacts with diverse proteins. EMBO Rep 4: 1132-1137, 2003.
    • (2003) EMBO Rep , vol.4 , pp. 1132-1137
    • Matthews, J.M.1    Visvader, J.E.2
  • 35
    • 0037020151 scopus 로고    scopus 로고
    • The LIM-only protein DRAL/FHL2 interacts with and is a corepressor for the promyelocytic leukemia zinc finger protein
    • McLoughlin P, Ehler E, Carlile G, Licht JD, and Schafer BW. The LIM-only protein DRAL/FHL2 interacts with and is a corepressor for the promyelocytic leukemia zinc finger protein. J Biol Chem 277: 37045-37053, 2002.
    • (2002) J Biol Chem , vol.277 , pp. 37045-37053
    • McLoughlin, P.1    Ehler, E.2    Carlile, G.3    Licht, J.D.4    Schafer, B.W.5
  • 37
    • 0035890468 scopus 로고    scopus 로고
    • Structure, properties and enhanced expression of galactose-binding C-type lectins in mucous cells of gills from freshwater Japanese eels (Anguilla japonica)
    • Mistry AC, Honda S, and Hirose S. Structure, properties and enhanced expression of galactose-binding C-type lectins in mucous cells of gills from freshwater Japanese eels (Anguilla japonica). Biochem J 360: 107-115, 2001.
    • (2001) Biochem J , vol.360 , pp. 107-115
    • Mistry, A.C.1    Honda, S.2    Hirose, S.3
  • 38
    • 0036453682 scopus 로고    scopus 로고
    • RING finger, B-box, and coiled-coil (RBCC) protein expression in branchial epithelial cells of Japanese eel, Anguilla japonica
    • Miyamoto K, Nakamura N, Kashiwagi M, Honda S, Kato A, Hasegawa S, Takei Y, and Hirose S. RING finger, B-box, and coiled-coil (RBCC) protein expression in branchial epithelial cells of Japanese eel, Anguilla japonica. Eur J Biochem 269: 6152-6161, 2002.
    • (2002) Eur J Biochem , vol.269 , pp. 6152-6161
    • Miyamoto, K.1    Nakamura, N.2    Kashiwagi, M.3    Honda, S.4    Kato, A.5    Hasegawa, S.6    Takei, Y.7    Hirose, S.8
  • 39
    • 0033068028 scopus 로고    scopus 로고
    • Pathophysiology of endothelin in the cardiovascular system
    • Miyauchi T and Masaki T. Pathophysiology of endothelin in the cardiovascular system. Annu Rev Physiol 61: 391-415, 1999.
    • (1999) Annu Rev Physiol , vol.61 , pp. 391-415
    • Miyauchi, T.1    Masaki, T.2
  • 40
    • 0033573880 scopus 로고    scopus 로고
    • The fourth member of the FHL family of LIM proteins is expressed exclusively in the testis
    • Morgan MJ and Madgwick AJ. The fourth member of the FHL family of LIM proteins is expressed exclusively in the testis. Biochem Biophys Res Commun 255: 251-255, 1999.
    • (1999) Biochem Biophys Res Commun , vol.255 , pp. 251-255
    • Morgan, M.J.1    Madgwick, A.J.2
  • 41
    • 0033574044 scopus 로고    scopus 로고
    • The LIM proteins FHL1 and FHL3 are expressed differently in skeletal muscle
    • Morgan MJ and Madgwick AJ. The LIM proteins FHL1 and FHL3 are expressed differently in skeletal muscle. Biochem Biophys Res Commun 255: 245-250, 1999.
    • (1999) Biochem Biophys Res Commun , vol.255 , pp. 245-250
    • Morgan, M.J.1    Madgwick, A.J.2
  • 42
    • 0037386704 scopus 로고    scopus 로고
    • The LIM-only protein FHL2 is a serum-inducible transcriptional coactivator of AP-1
    • Morlon A and Sassone-Corsi P. The LIM-only protein FHL2 is a serum-inducible transcriptional coactivator of AP-1. Proc Natl Acad Sci USA 100: 3977-3982, 2003.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 3977-3982
    • Morlon, A.1    Sassone-Corsi, P.2
  • 44
    • 0037083981 scopus 로고    scopus 로고
    • The transcriptional coactivator FHL2 transmits Rho signals from the cell membrane into the nucleus
    • Muller JM, Metzger E, Greschik H, Bosserhoff AK, Mercep L, Buettner R, and Schule R. The transcriptional coactivator FHL2 transmits Rho signals from the cell membrane into the nucleus. EMBO J 21: 736-748, 2002.
    • (2002) EMBO J , vol.21 , pp. 736-748
    • Muller, J.M.1    Metzger, E.2    Greschik, H.3    Bosserhoff, A.K.4    Mercep, L.5    Buettner, R.6    Schule, R.7
  • 45
    • 0030791307 scopus 로고    scopus 로고
    • Evolution by the birth-and-death process in multigene families of the vertebrate immune system
    • Nei M, Gu X, and Sitnikova T. Evolution by the birth-and-death process in multigene families of the vertebrate immune system. Proc Natl Acad Sci USA 94: 7799-7806, 1997.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 7799-7806
    • Nei, M.1    Gu, X.2    Sitnikova, T.3
  • 47
    • 0014179384 scopus 로고
    • Fine structure of the respiratory lamellae of teleostean gills
    • Newstead JD. Fine structure of the respiratory lamellae of teleostean gills. Z Zellforsch Mikrosk Anat 79: 396-428, 1967.
    • (1967) Z Zellforsch Mikrosk Anat , vol.79 , pp. 396-428
    • Newstead, J.D.1
  • 48
    • 0031966444 scopus 로고    scopus 로고
    • Hormone metabolism by the fish gill
    • Olson KR. Hormone metabolism by the fish gill. Comp Biochem Physiol A 119: 55-65, 1998.
    • (1998) Comp Biochem Physiol a , vol.119 , pp. 55-65
    • Olson, K.R.1
  • 49
    • 0036667259 scopus 로고    scopus 로고
    • Gill circulation: Regulation of perfusion distribution and metabolism of regulatory molecules
    • Olson KR. Gill circulation: regulation of perfusion distribution and metabolism of regulatory molecules. J Exp Zool 293: 320-335, 2002.
    • (2002) J Exp Zool , vol.293 , pp. 320-335
    • Olson, K.R.1
  • 50
    • 0036667256 scopus 로고    scopus 로고
    • Vascular anatomy of the fish gill
    • Olson KR. Vascular anatomy of the fish gill. J Exp Zool 293: 214-231, 2002.
    • (2002) J Exp Zool , vol.293 , pp. 214-231
    • Olson, K.R.1
  • 51
    • 0342510279 scopus 로고
    • Blood flow through gills
    • edited by Houlihan DF, Rankin JC, and Shuttleworth TJ. New York, NY: Cambridge Univ Press
    • Randall D. Blood flow through gills. In: Gills, edited by Houlihan DF, Rankin JC, and Shuttleworth TJ. New York, NY: Cambridge Univ Press, 1982, p. 173-191.
    • (1982) Gills , pp. 173-191
    • Randall, D.1
  • 53
    • 0027984808 scopus 로고
    • Endothelins: Molecular biology, biochemistry, pharmacology, physiology, and pathophysiology
    • Rubanyi GM and Polokoff MA. Endothelins: molecular biology, biochemistry, pharmacology, physiology, and pathophysiology. Pharmacol Rev 46: 325-415, 1994.
    • (1994) Pharmacol Rev , vol.46 , pp. 325-415
    • Rubanyi, G.M.1    Polokoff, M.A.2
  • 55
    • 0019440163 scopus 로고
    • Localization of smooth-muscle myosin in branchial pillar cells of snapper (Chrysophys auratus) by immunofluorescence histochemistry
    • Smith DG and Chamley-Campbell J. Localization of smooth-muscle myosin in branchial pillar cells of snapper (Chrysophys auratus) by immunofluorescence histochemistry. J Exp Zool 215: 121-124, 1981.
    • (1981) J Exp Zool , vol.215 , pp. 121-124
    • Smith, D.G.1    Chamley-Campbell, J.2
  • 56
    • 0032978843 scopus 로고    scopus 로고
    • Cardiovascular and gill microcirculatory effects of endothelin-1 in atlantic cod: Evidence for pillar cell contraction
    • Stenslokken KO, Sundin L, and Nilsson GE. Cardiovascular and gill microcirculatory effects of endothelin-1 in atlantic cod: evidence for pillar cell contraction. J Exp Biol 202: 1151-1157, 1999.
    • (1999) J Exp Biol , vol.202 , pp. 1151-1157
    • Stenslokken, K.O.1    Sundin, L.2    Nilsson, G.E.3
  • 57
    • 0032442451 scopus 로고    scopus 로고
    • Endothelin redistributes blood flow through the lamellae of rainbow trout gills
    • Sundin L and Nilsson GE. Endothelin redistributes blood flow through the lamellae of rainbow trout gills. J Comp Physiol [B] 168: 619-623, 1998.
    • (1998) J Comp Physiol [B] , vol.168 , pp. 619-623
    • Sundin, L.1    Nilsson, G.E.2
  • 58
    • 0033574419 scopus 로고    scopus 로고
    • Identification by differential display of a hypertonicity-inducible inward rectifier potassium channel highly expressed in chloride cells
    • Suzuki Y, Itakura M, Kashiwagi M, Nakamura N, Matsuki T, Sakuta H, Naito N, Takano K, Fujita T, and Hirose S. Identification by differential display of a hypertonicity-inducible inward rectifier potassium channel highly expressed in chloride cells. J Biol Chem 274: 11376-11382, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 11376-11382
    • Suzuki, Y.1    Itakura, M.2    Kashiwagi, M.3    Nakamura, N.4    Matsuki, T.5    Sakuta, H.6    Naito, N.7    Takano, K.8    Fujita, T.9    Hirose, S.10
  • 59
    • 0034703284 scopus 로고    scopus 로고
    • Alzheimer's disease-associated presenilin 2 interacts with DRAL, an LIM-domain protein
    • Tanahashi H and Tabira T. Alzheimer's disease-associated presenilin 2 interacts with DRAL, an LIM-domain protein. Hum Mol Genet 9: 2281-2289, 2000.
    • (2000) Hum Mol Genet , vol.9 , pp. 2281-2289
    • Tanahashi, H.1    Tabira, T.2
  • 60
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson JD, Higgins DG, and Gibson TJ. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 22: 4673-4680, 1994.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 61
    • 0037459070 scopus 로고    scopus 로고
    • Induction of SM-α-actin expression by mechanical strain in adult vascular smooth muscle cells is mediated through activation of JNK and p38 MAP kinase
    • Tock J, Van P, V, Stenmark KR, and Nemenoff RA. Induction of SM-α-actin expression by mechanical strain in adult vascular smooth muscle cells is mediated through activation of JNK and p38 MAP kinase. Biochem Biophys Res Commun 301: 1116-1121, 2003.
    • (2003) Biochem Biophys Res Commun , vol.301 , pp. 1116-1121
    • Tock, J.1    Van, P.V.2    Stenmark, K.R.3    Nemenoff, R.A.4
  • 62
    • 0038645813 scopus 로고    scopus 로고
    • The LIM protein FHL3 binds basic Krüppel-like factor/Krüppel- like factor 3 and its co-repressor C-terminal-binding protein 2
    • Turner J, Nicholas II, Bishop D, Matthews JM, and Crossley M. The LIM protein FHL3 binds basic Krüppel-like factor/Krüppel-like factor 3 and its co-repressor C-terminal-binding protein 2. J Biol Chem 278: 12786-12795, 2003.
    • (2003) J Biol Chem , vol.278 , pp. 12786-12795
    • Turner, J.1    Nicholas, I.I.2    Bishop, D.3    Matthews, J.M.4    Crossley, M.5
  • 63
    • 0030596507 scopus 로고    scopus 로고
    • Isolation, characterization and evolution of nine pufferfish (Fugu rubripes) actin genes
    • Venkatesh B, Tay BH, Elgar G, and Brenner S. Isolation, characterization and evolution of nine pufferfish (Fugu rubripes) actin genes. J Mol Biol 259: 655-665, 1996.
    • (1996) J Mol Biol , vol.259 , pp. 655-665
    • Venkatesh, B.1    Tay, B.H.2    Elgar, G.3    Brenner, S.4
  • 64
    • 0036667254 scopus 로고    scopus 로고
    • Fish gill morphology: Inside out
    • Wilson JM and Laurent P. Fish gill morphology: inside out. J Exp Zool 293: 192-213, 2002.
    • (2002) J Exp Zool , vol.293 , pp. 192-213
    • Wilson, J.M.1    Laurent, P.2
  • 65
    • 0034721855 scopus 로고    scopus 로고
    • The LIM-only protein DRAL/FHL2 binds to the cytoplasmic domain of several α and β integrin chains and is recruited to adhesion complexes
    • Wixler V, Geerts D, Laplantine E, Westhoff D, Smyth N, Aumailley M, Sonnenberg A, and Paulsson M. The LIM-only protein DRAL/FHL2 binds to the cytoplasmic domain of several α and β integrin chains and is recruited to adhesion complexes. J Biol Chem 275: 33669-33678, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 33669-33678
    • Wixler, V.1    Geerts, D.2    Laplantine, E.3    Westhoff, D.4    Smyth, N.5    Aumailley, M.6    Sonnenberg, A.7    Paulsson, M.8
  • 67
    • 0017759258 scopus 로고
    • Serial passaging and differentiation of myogenic cells isolated from dystrophic mouse muscle
    • Yaffe D and Saxel O. Serial passaging and differentiation of myogenic cells isolated from dystrophic mouse muscle. Nature 270: 725-727, 1977.
    • (1977) Nature , vol.270 , pp. 725-727
    • Yaffe, D.1    Saxel, O.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.