메뉴 건너뛰기




Volumn 19, Issue 5, 1998, Pages 767-776

Biochemical regulation of the nonmuscle myosin light chain kinase isoform in bovine endothelium

Author keywords

[No Author keywords available]

Indexed keywords

BOVINAE;

EID: 0032209748     PISSN: 10441549     EISSN: None     Source Type: Journal    
DOI: 10.1165/ajrcmb.19.5.3126     Document Type: Article
Times cited : (93)

References (49)
  • 1
    • 0029119895 scopus 로고
    • Myosin light chain kinase-regulated endothelial cell contraction: The relationship between isometric tension, actin polymerization, and myosin phosphorylation
    • Goeckeler, Z. M., and R. B. Wysolmerski. 1995. Myosin light chain kinase-regulated endothelial cell contraction: the relationship between isometric tension, actin polymerization, and myosin phosphorylation. J. Cell Biol. 130:622-635.
    • (1995) J. Cell Biol. , vol.130 , pp. 622-635
    • Goeckeler, Z.M.1    Wysolmerski, R.B.2
  • 2
    • 0020379140 scopus 로고
    • Role of endothelial cell cytoskeleton in control of endothelial permeability
    • Shasby, D. M., S. S. Shasby, J. M. Sullivan, and M. J. Peach. 1982. Role of endothelial cell cytoskeleton in control of endothelial permeability. Circ. Res. 51:657-661.
    • (1982) Circ. Res. , vol.51 , pp. 657-661
    • Shasby, D.M.1    Shasby, S.S.2    Sullivan, J.M.3    Peach, M.J.4
  • 3
    • 0025642947 scopus 로고
    • Role of actin and myosin in the control of paracellular permeability in pig, rat, and human vascular endothelium
    • Schnittler, H. J., A. Wilke, T. Gress, N. Suttorp, and D. Drenckhahn. 1990. Role of actin and myosin in the control of paracellular permeability in pig, rat, and human vascular endothelium. J. Physiol. 431:379-401.
    • (1990) J. Physiol. , vol.431 , pp. 379-401
    • Schnittler, H.J.1    Wilke, A.2    Gress, T.3    Suttorp, N.4    Drenckhahn, D.5
  • 4
    • 0029012398 scopus 로고
    • Regulation of endothelial cell myosin light chain phosphorylation: Role in thrombin-induced barrier dysfunction
    • Garcia, J. G. N., H. W. Davis, and C. E. Patterson. 1995. Regulation of endothelial cell myosin light chain phosphorylation: role in thrombin-induced barrier dysfunction. J. Cell. Physiol. 163:510-522.
    • (1995) J. Cell. Physiol. , vol.163 , pp. 510-522
    • Garcia, J.G.N.1    Davis, H.W.2    Patterson, C.E.3
  • 5
    • 0019348630 scopus 로고
    • The role of phosphorylation in regulating contractile proteins
    • Adelstein, R. S., M. D. Pato, and M. A. Conti. 1981. The role of phosphorylation in regulating contractile proteins. Adv. Cyclic Nucleo. Res. 14:361-373.
    • (1981) Adv. Cyclic Nucleo. Res. , vol.14 , pp. 361-373
    • Adelstein, R.S.1    Pato, M.D.2    Conti, M.A.3
  • 6
    • 0026709998 scopus 로고
    • Control of non-muscle myosins by phosphorylation
    • Tan, J. L., S. Ravid, and J. A. Spudich. 1992. Control of non-muscle myosins by phosphorylation. Annu. Rev. Biochem. 61:721-759.
    • (1992) Annu. Rev. Biochem. , vol.61 , pp. 721-759
    • Tan, J.L.1    Ravid, S.2    Spudich, J.A.3
  • 7
    • 0025743578 scopus 로고
    • Regulation of permeabilized endothelial cell retraction by myosin phosphorylation
    • Wysolmerski, R. B., and D. Lagunoff. 1991. Regulation of permeabilized endothelial cell retraction by myosin phosphorylation. Am. J. Physiol. 261: C32-C40.
    • (1991) Am. J. Physiol. , vol.261
    • Wysolmerski, R.B.1    Lagunoff, D.2
  • 8
    • 0025186832 scopus 로고
    • Involvement of myosin light chain kinase in endothelial cell retraction
    • Wysolmerski, R. B., and D. Lagunoff. 1990. Involvement of myosin light chain kinase in endothelial cell retraction. Proc. Natl. Acad. Sci. USA 87: 16-20.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 16-20
    • Wysolmerski, R.B.1    Lagunoff, D.2
  • 10
    • 0026343743 scopus 로고
    • The carboxyl terminus of the smooth muscle myosin light chain kinase is expressed as an independent protein, telokin
    • Gallagher, P. J., and B. P. Herring. 1991. The carboxyl terminus of the smooth muscle myosin light chain kinase is expressed as an independent protein, telokin. J. Biol. Chem. 266:23945-23952.
    • (1991) J. Biol. Chem. , vol.266 , pp. 23945-23952
    • Gallagher, P.J.1    Herring, B.P.2
  • 11
    • 0024330080 scopus 로고
    • Identification in turkey gizzard of an acidic protein related to the C-terminal portion of smooth muscle myosin light chain kinase
    • Ito, M., R. Guerriero, V. Jie, and D. J. Hartshorne. 1989. Identification in turkey gizzard of an acidic protein related to the C-terminal portion of smooth muscle myosin light chain kinase. J. Biol. Chem. 264:13971-13974.
    • (1989) J. Biol. Chem. , vol.264 , pp. 13971-13974
    • Ito, M.1    Guerriero, R.2    Jie, V.3    Hartshorne, D.J.4
  • 12
    • 0019445517 scopus 로고
    • The relationship between calmodulin binding and phosphorylation of smooth muscle myosin kinase by the catalytic subunit of 3′:5′ cAMP-dependent protein kinase
    • Conti, M. A., and R. S. Adelstein. 1981. The relationship between calmodulin binding and phosphorylation of smooth muscle myosin kinase by the catalytic subunit of 3′:5′ cAMP-dependent protein kinase. J. Biol. Chem. 256:3178-3181.
    • (1981) J. Biol. Chem. , vol.256 , pp. 3178-3181
    • Conti, M.A.1    Adelstein, R.S.2
  • 13
    • 0025123347 scopus 로고
    • Myosin light chain kinase phosphorylation in tracheal smooth muscle
    • Stull, J. T., L. Hsu, M. G. Tansey, and K. E. Kamm. 1990. Myosin light chain kinase phosphorylation in tracheal smooth muscle. J. Biol. Chem. 265: 16683-16690.
    • (1990) J. Biol. Chem. , vol.265 , pp. 16683-16690
    • Stull, J.T.1    Hsu, L.2    Tansey, M.G.3    Kamm, K.E.4
  • 14
    • 0026340753 scopus 로고
    • Molecular characterization of a mammalian smooth muscle myosin light chain kinase
    • Gallagher, P. J., B. P. Herring, S. A. Griffin, and J. T. Stull. 1991. Molecular characterization of a mammalian smooth muscle myosin light chain kinase. J. Biol. Chem. 266:23936-23944.
    • (1991) J. Biol. Chem. , vol.266 , pp. 23936-23944
    • Gallagher, P.J.1    Herring, B.P.2    Griffin, S.A.3    Stull, J.T.4
  • 17
    • 0026613093 scopus 로고
    • Reversible hyperphosphorylation and reorganization of vimentin intermediate filaments by okadaic acid in 9L rat brain tumor cells
    • Lee, W. C., J. S. Yu, S. D. Yang, and Y. K. Lai. 1992. Reversible hyperphosphorylation and reorganization of vimentin intermediate filaments by okadaic acid in 9L rat brain tumor cells. J. Cell Biochem. 49:378-393.
    • (1992) J. Cell Biochem. , vol.49 , pp. 378-393
    • Lee, W.C.1    Yu, J.S.2    Yang, S.D.3    Lai, Y.K.4
  • 18
    • 0029131091 scopus 로고
    • Regulation of endothelial cell gap formation and barrier function by myosin-associated phosphatase activities
    • Verin, A. D., C. E. Patterson, M. E. Day, and J. G. N. Garcia. 1995. Regulation of endothelial cell gap formation and barrier function by myosin-associated phosphatase activities. Am. J. Physiol. 269(Lung Cell Mol. Physiol.):L99-L108.
    • (1995) Am. J. Physiol. 269(Lung Cell Mol. Physiol.) , vol.269
    • Verin, A.D.1    Patterson, C.E.2    Day, M.E.3    Garcia, J.G.N.4
  • 19
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of head of bacteriophage
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of head of bacteriophage. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 20
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrilamide gels to nitrocellulose sheets: Procedure and some applications
    • Toubin, H., T. Stachelin, and J. Gordon. 1979. Electrophoretic transfer of proteins from polyacrilamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA 76:4350-4354.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Toubin, H.1    Stachelin, T.2    Gordon, J.3
  • 21
    • 0027986575 scopus 로고
    • Mechanisms of cholera toxin prevention of thrombin- and PMA-induced endothelial cell barrier dysfunction
    • Patterson, C. E., H. Davis, K. Schaphorst, and J. G. N. Garcia. 1994. Mechanisms of cholera toxin prevention of thrombin- and PMA-induced endothelial cell barrier dysfunction. Microvasc. Res. 48:212-235.
    • (1994) Microvasc. Res. , vol.48 , pp. 212-235
    • Patterson, C.E.1    Davis, H.2    Schaphorst, K.3    Garcia, J.G.N.4
  • 22
    • 0026058812 scopus 로고
    • Myosin phosphorylation/dephosphorylation and regulation of airway smooth muscle contractility
    • DeLanerolle, P., and R. J. Paul. 1991. Myosin phosphorylation/dephosphorylation and regulation of airway smooth muscle contractility. Am. J. Physiol. 261:L1-L14.
    • (1991) Am. J. Physiol. , vol.261
    • DeLanerolle, P.1    Paul, R.J.2
  • 24
    • 85033872217 scopus 로고    scopus 로고
    • Thrombin-induced endothelial cell (EC) activation is accompanied by decreases in EC myosin-specific phosphatase (PPase) activity
    • Abstr.
    • Verin, A. D., M. Herenyiova, and J. G. N. Garcia. 1997. Thrombin-induced endothelial cell (EC) activation is accompanied by decreases in EC myosin-specific phosphatase (PPase) activity. Am. J. Respir. Crit. Care Med. 155:635A. (Abstr.)
    • (1997) Am. J. Respir. Crit. Care Med. , vol.155
    • Verin, A.D.1    Herenyiova, M.2    Garcia, J.G.N.3
  • 25
    • 0019941979 scopus 로고
    • Role of phosphorylation in mediating the association of myosin with the cytoskeletal structures of human platelets
    • Fox, J. E. B., and D. R. Phillips. 1982. Role of phosphorylation in mediating the association of myosin with the cytoskeletal structures of human platelets. J. Biol. Chem. 257:4120-4126.
    • (1982) J. Biol. Chem. , vol.257 , pp. 4120-4126
    • Fox, J.E.B.1    Phillips, D.R.2
  • 26
    • 0021321488 scopus 로고
    • Increased phosphorylation of myosin light chain kinase after an increase in cyclic AMP in intact smooth muscle
    • DeLanerolle, P., M. Nishikawa, D. A. Yost, and R. S. Adelstein. 1984. Increased phosphorylation of myosin light chain kinase after an increase in cyclic AMP in intact smooth muscle. Science 223:1415-1417.
    • (1984) Science , vol.223 , pp. 1415-1417
    • Delanerolle, P.1    Nishikawa, M.2    Yost, D.A.3    Adelstein, R.S.4
  • 27
    • 0021268721 scopus 로고
    • Phosphorylation of mammalian myosin light chain kinases by the catalytic subunit of cyclic AMP-dependent kinase and by cyclic GMP-dependent protein kinase
    • Nishikawa, M., P. deLanerolle, T. Lincoln, and R. Adelstein. 1984. Phosphorylation of mammalian myosin light chain kinases by the catalytic subunit of cyclic AMP-dependent kinase and by cyclic GMP-dependent protein kinase. J. Biol. Chem. 259:8429-8436.
    • (1984) J. Biol. Chem. , vol.259 , pp. 8429-8436
    • Nishikawa, M.1    DeLanerolle, P.2    Lincoln, T.3    Adelstein, R.4
  • 29
    • 0026781107 scopus 로고
    • 77 and vimentin and enhances albumin permeability across cultured bovine pulmonary artery endothelial cell monolayers
    • 77 and vimentin and enhances albumin permeability across cultured bovine pulmonary artery endothelial cell monolayers. J. Cell. Physiol. 153:62-75.
    • (1992) J. Cell. Physiol. , vol.153 , pp. 62-75
    • Stasek, J.E.1    Patterson, C.E.2    Garcia, J.G.N.3
  • 32
    • 0024468408 scopus 로고
    • Phallacidin prevents thrombin-induced increases in endothelial permeability to albumin
    • Phillips, P. G., H. Lum, A. B. Malik, and M. F. Tsan. 1989. Phallacidin prevents thrombin-induced increases in endothelial permeability to albumin. Am. J. Physiol. 257:C562-C567.
    • (1989) Am. J. Physiol. , vol.257
    • Phillips, P.G.1    Lum, H.2    Malik, A.B.3    Tsan, M.F.4
  • 33
    • 0028800221 scopus 로고
    • Contraction due to microtubule disruption is associated with increased phosphorylation of myosin regulatory light chain kinase
    • Kolodney, M. S., and E. L. Elson. 1995. Contraction due to microtubule disruption is associated with increased phosphorylation of myosin regulatory light chain kinase. Proc. Natl. Acad. Sci. USA 92:10252-10256.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 10252-10256
    • Kolodney, M.S.1    Elson, E.L.2
  • 34
    • 0025925359 scopus 로고
    • c-src, phospholipase C, inositol lipid, and diacylglycerol kinases with the cytoskeleton of thrombin-stimulated platelets
    • c-src, phospholipase C, inositol lipid, and diacylglycerol kinases with the cytoskeleton of thrombin-stimulated platelets. J. Biol. Chem. 266:15705-15709.
    • (1991) J. Biol. Chem. , vol.266 , pp. 15705-15709
    • Grondin, P.1    Plantavid, M.2    Sultan, C.3    Breton, M.4    Mauco, G.5    Chap, H.6
  • 35
    • 0026597050 scopus 로고
    • c-src to the cytoskeleton during platelet aggregation
    • c-src to the cytoskeleton during platelet aggregation. EMBO. J. 11:855-861.
    • (1992) EMBO. J. , vol.11 , pp. 855-861
    • Horvath, A.R.1    Muzbek, L.2    Kellie, S.3
  • 36
    • 0027340192 scopus 로고
    • c-src to integrin-dependent cytoskeletal complexes in thrombin-stimulated platelets
    • c-src to integrin-dependent cytoskeletal complexes in thrombin-stimulated platelets. Mol. Cell. Biol. 13:1863-1871.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 1863-1871
    • Clark, E.A.1    Brugge, J.C.2
  • 37
    • 0026739248 scopus 로고
    • c-src with Triton X-100 insoluble residue in human blood platelets requires platelet aggregation and actin polymerization
    • c-src with Triton X-100 insoluble residue in human blood platelets requires platelet aggregation and actin polymerization. J. Biol. Chem. 267: 20075-20081.
    • (1992) J. Biol. Chem. , vol.267 , pp. 20075-20081
    • Oda, A.1    Druker, B.J.2    Smith, M.3    Salzman, E.W.4
  • 38
    • 0029884155 scopus 로고    scopus 로고
    • Differential translocation of phospholipase C isozymes to integrin-mediated cytoskeletal complexes in thrombin-stimulated human platelets
    • Banno, Y., S. Nakashima, M. Ohzawa, and Y. Nazawa. 1996. Differential translocation of phospholipase C isozymes to integrin-mediated cytoskeletal complexes in thrombin-stimulated human platelets. J. Biol. Chem. 271: 14989-14994.
    • (1996) J. Biol. Chem. , vol.271 , pp. 14989-14994
    • Banno, Y.1    Nakashima, S.2    Ohzawa, M.3    Nazawa, Y.4
  • 39
    • 0028476962 scopus 로고
    • Thrombin-induced redistribution of protein tyrosine-phosphatases to the cytoskeletal complexes in human platelets
    • Li, R. Y., A. Ragal, F. Gaits, J. M. F. Ragal-Thomas, and H. Chap. 1994. Thrombin-induced redistribution of protein tyrosine-phosphatases to the cytoskeletal complexes in human platelets. Cell. Mol. Biol. 40:665-675.
    • (1994) Cell. Mol. Biol. , vol.40 , pp. 665-675
    • Li, R.Y.1    Ragal, A.2    Gaits, F.3    Ragal-Thomas, J.M.F.4    Chap, H.5
  • 40
    • 85033873109 scopus 로고    scopus 로고
    • Mapping the cytoskeletal protein binding domains within the CD18 integrin-cytoplasmic tail
    • Abstr.
    • Sampath, R., P. J. Gallagher, and F. M. Pavalko. 1996. Mapping the cytoskeletal protein binding domains within the CD18 integrin-cytoplasmic tail. Mol. Biol. Cell 7:385A. (Abstr.)
    • (1996) Mol. Biol. Cell , vol.7
    • Sampath, R.1    Gallagher, P.J.2    Pavalko, F.M.3
  • 41
    • 85033897949 scopus 로고    scopus 로고
    • Purification and characterization of the 208 kDa integrin-binding protein
    • Abstr.
    • Walker, D. M., P. J. Gallagher, and F. M. Pavalko. 1996. Purification and characterization of the 208 kDa integrin-binding protein. Mol. Biol. Cell 7:385A. (Abstr.)
    • (1996) Mol. Biol. Cell , vol.7
    • Walker, D.M.1    Gallagher, P.J.2    Pavalko, F.M.3
  • 42
    • 0027203489 scopus 로고
    • Actin-binding peptide from smooth muscle myosin light chain kinase
    • Kanoh, S., M. Ito, E. Niwa, Y. Kawano, and D. J. Hartshorne. 1993. Actin-binding peptide from smooth muscle myosin light chain kinase. Biochemistry 32:8902-8907.
    • (1993) Biochemistry , vol.32 , pp. 8902-8907
    • Kanoh, S.1    Ito, M.2    Niwa, E.3    Kawano, Y.4    Hartshorne, D.J.5
  • 43
    • 0026778183 scopus 로고
    • A novel regulatory effect of myosin light chain kinase from smooth muscle on the ATP-dependent interaction between actin and myosin
    • Kohama, K., T. Okagaki, K. Hayakawa, Y. Lin, R. Ishikawa, T. Shimmen, and A. Inoue. 1992. A novel regulatory effect of myosin light chain kinase from smooth muscle on the ATP-dependent interaction between actin and myosin. Biochem. Biophys. Res. Commun. 184:1204-1211.
    • (1992) Biochem. Biophys. Res. Commun. , vol.184 , pp. 1204-1211
    • Kohama, K.1    Okagaki, T.2    Hayakawa, K.3    Lin, Y.4    Ishikawa, R.5    Shimmen, T.6    Inoue, A.7
  • 45
    • 0022259923 scopus 로고
    • Phosphorylation of smooth muscle myosin light chain kinase by protein kinase C. Comparative study of the phosphorylated sites
    • Nishikawa, M., S. Shirakawa, and R. S. Adelstein. 1985. Phosphorylation of smooth muscle myosin light chain kinase by protein kinase C. Comparative study of the phosphorylated sites. J. Biol. Chem. 260:8978-8983.
    • (1985) J. Biol. Chem. , vol.260 , pp. 8978-8983
    • Nishikawa, M.1    Shirakawa, S.2    Adelstein, R.S.3
  • 46
    • 0030340292 scopus 로고    scopus 로고
    • Phosphorylation and activation of smooth muscle myosin light chain kinase by MAP kinase and cyclin-dependent kinase-1
    • Morrison, D. L., J. S. Sanghera, J. Stewart, C. Sutherland, M. P. Walsh, and S. L. Pelech. 1996. Phosphorylation and activation of smooth muscle myosin light chain kinase by MAP kinase and cyclin-dependent kinase-1. Biochem. Cell Biol. 74:549-557.
    • (1996) Biochem. Cell Biol. , vol.74 , pp. 549-557
    • Morrison, D.L.1    Sanghera, J.S.2    Stewart, J.3    Sutherland, C.4    Walsh, M.P.5    Pelech, S.L.6
  • 47
    • 0025270587 scopus 로고
    • 2+/calmodulin-dependcnt protein kinase-II: Comparative study of the phosphorylation sites
    • 2+/calmodulin-dependcnt protein kinase-II: comparative study of the phosphorylation sites. Arch. Biochem. Biophys. 278:41-45.
    • (1990) Arch. Biochem. Biophys. , vol.278 , pp. 41-45
    • Hashimoto, Y.1    Soderling, T.R.2
  • 48
    • 0025311283 scopus 로고
    • 2+/calmodulin-dependent multi-functional protein kinase
    • 2+/calmodulin-dependent multi-functional protein kinase. J. Biol. Chem. 265:8975-8978.
    • (1990) J. Biol. Chem. , vol.265 , pp. 8975-8978
    • Ikebe, M.1    Reardon, S.2
  • 49
    • 0026720867 scopus 로고
    • Phosphorylation of myosin light chain kinase by the multi-functional calmodulin-dependent protein kinase II in smooth muscle cells
    • Tansey, M. G., R. A. Word, H. Hidaka, H. A. Singer, C. M. Schwoker, K. E. Kamm, and J. T. Stull. 1992. Phosphorylation of myosin light chain kinase by the multi-functional calmodulin-dependent protein kinase II in smooth muscle cells. J. Biol. Chem. 267:12511-12516.
    • (1992) J. Biol. Chem. , vol.267 , pp. 12511-12516
    • Tansey, M.G.1    Word, R.A.2    Hidaka, H.3    Singer, H.A.4    Schwoker, C.M.5    Kamm, K.E.6    Stull, J.T.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.