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Typus
KomplettPlagiat
Bearbeiter
Hindemith
Gesichtet
Yes.png
Untersuchte Arbeit:
Seite: 17, Zeilen: 10-16
Quelle: Ebong et al 2006
Seite(n): H2015, Zeilen: r. Spalte: 6 ff.
Connexins 37, 40, and 43 (Cx37, Cx40, Cx43, respectively) are the major gap junction proteins expressed in vascular endothelial cells[85-89]. These proteins are very dynamic, exhibiting rapid turnover times and variable expression patterns. Because of the unique gating and permselective characteristics of Cx37, Cx40, and Cx43, different combinations of these connexin isoforms contribute to homo- or heteromeric connexons and homo- or heterotypic gap junctions leading to a variety of channel types with different functional properties[83, 90-96].

83. Kumar, N.M. and N.B. Gilula, The gap junction communication channel. Cell, 1996. 84(3): p. 381-8.

85. Bruzzone, R., et al., Connexin40, a component of gap junctions in vascular endothelium, is restricted in its ability to interact with other connexins. Mol Biol Cell, 1993. 4(1): p. 7-20.

86. Larson, D.M., C.C. Haudenschild, and E.C. Beyer, Gap junction messenger RNA expression by vascular wall cells. Circ Res, 1990. 66(4): p. 1074-80.

87. Little, T.L., E.C. Beyer, and B.R. Duling, Connexin 43 and connexin 40 gap junctional proteins are present in arteriolar smooth muscle and endothelium in vivo. Am J Physiol, 1995. 268(2 Pt 2): p. H729-39.

88. Reed, K.E., et al., Molecular cloning and functional expression of human connexin37, an endothelial cell gap junction protein. J Clin Invest, 1993. 91(3): p. 997-1004.

89. Van Rijen, H., et al., Gap junctions in human umbilical cord endothelial cells contain multiple connexins. Am J Physiol, 1997. 272(1 Pt 1): p. C117-30.

90. Beblo, D.A. and R.D. Veenstra, Monovalent cation permeation through the connexin40 gap junction channel. Cs, Rb, K, Na, Li, TEA, TMA, TBA, and effects of anions Br, Cl, F, acetate, aspartate, glutamate, and NO3. J Gen Physiol, 1997. 109(4): p. 509-22.

91. Bruzzone, R., T.W. White, and D.A. Goodenough, The cellular Internet: on-line with connexins. Bioessays, 1996. 18(9): p. 709-18.

92. Bruzzone, R., T.W. White, and D.L. Paul, Connections with connexins: the molecular basis of direct intercellular signaling. Eur J Biochem, 1996. 238(1): p. 1-27.

93. Elfgang, C., et al., Specific permeability and selective formation of gap junction channels in connexin-transfected HeLa cells. J Cell Biol, 1995. 129(3): p. 805-17.

94. Veenstra, R.D., Size and selectivity of gap junction channels formed from different connexins. J Bioenerg Biomembr, 1996. 28(4): p. 327-37.

95. Wang, H.Z. and R.D. Veenstra, Monovalent ion selectivity sequences of the rat connexin43 gap junction channel. J Gen Physiol, 1997. 109(4): p. 491-507.

96. White, T.W. and R. Bruzzone, Multiple connexin proteins in single intercellular channels: connexin compatibility and functional consequences. J Bioenerg Biomembr, 1996. 28(4): p. 339-50.

Connexin 37, 40, and 43 (Cx37, Cx40, Cx43, respectively) are the major gap junction proteins expressed in vascular endothelial cells (7, 32, 34, 39, 45). These proteins are very dynamic, exhibiting rapid turnover times and variable expression patterns. Because of the unique gating and permselective characteristics of Cx37, Cx40, and Cx43, different combinations of these connexin isoforms contribute to homo- or heteromeric connexons and homo- or heterotypic gap junctions leading to a variety of channel types with different functional properties (1, 8, 9, 19, 28, 47–49).

1. Beblo DA and Veenstra RD. Monovalent cation permeation through the connexin40 gap junction channel: Cs, Rb, K, Na, Li, TEA, TMA, TBA, and effects of anions Br, Cl, F, acetate, aspartate, glutamate, and NO3. J Gen Physiol 109: 509–522, 1997.

7. Bruzzone R, Haefliger JA, Gimlich RL, and Paul DL. Connexin40, a component of gap junctions in vascular endothelium, is restricted in its ability to interact with other connexins. Mol Biol Cell 4: 7–20, 1993.

8. Bruzzone R, White TW, and Goodenough DA. The cellular internet: on-line with connexins. Bioessays 18: 709–718, 1996.

9. Bruzzone R, White TW, and Paul DL. Connections with connexins: the molecular basis of direct intercellular signaling. Eur J Biochem 238: 1–27, 1996.

19. Elfgang C, Eckert R, Lichtenberg-Frate´ H, Butterweck A, Traub O, Klein TA, Hüsler DF, and Willecke K. Specific permeability and selective formation of gap junction channels in connexin-transfected HeLa cells. J Cell Biol 129: 805–817, 1995.

28. Kumar NM and Gilula NB. The gap junction communication channel. Cell 84: 381–388, 1996.

29. Kwak BR and Jongsma HJ. Selective inhibition of gap junction channel activity by synthetic peptides. J Physiol 516: 679–685, 1999.

32. Larson DM, Haudenschild CC, and Beyer EC. Gap junction messenger RNA expression by vascular wall cells. Circ Res 66: 1074–1080, 1990.

34. Little TL, Beyer EC, and Duling BR. Connexin 43 and connexin 40 gap junctional proteins are present in arteriolar smooth muscle and endothelium in vivo. Am J Physiol Heart Circ Physiol 268: H729–H739, 1995.

39. Reed KE, Westphale EM, Larson DM, Wang HZ, Veenstra RD, and Beyer EC. Molecular cloning and functional expression of human connexin37, an endothelial cell gap junction protein. J Clin Invest 91: 997–1004, 1993.

45. Van Rijen H, van Kempen MJ, Analbers LJ, Rook MB, van Ginneken AC, Gros D, and Jongsma HJ. Gap junctions in human umbilical cord endothelial cells contain multiple connexins. Am J Physiol Cell Physiol 272: C117–C130, 1997.

47. Veenstra RD. Size and selectivity of gap junction channels formed from different connexins. J Bioenerg Biomembr 28:b 327–337, 1996.

48. Wang HZ and Veenstra RD. Monovalent ion selectivity sequences of the rat connexin43 gap junction channel. J Gen Physiol 109: 491–507, 1997.

49. White TW and Bruzzone R. Multiple connexin proteins in single intercellular channels: connexin compatibility and functional consequences. J Bioenerg Biomembr 28: 339–350, 1996.

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(Hindemith), SleepyHollow02

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