Protein kinase C-dependent regulation of connexin43 gap junctions and hemichannels

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Protein kinase C-dependent regulation of connexin43 gap junctions and hemichannels. / Alstrøm, Jette Skov; Stroemlund, Line Waring; Nielsen, Morten Schak; MacAulay, Nanna.

In: Biochemical Society Transactions, Vol. 43, No. 3, 06.2015, p. 519-23.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Alstrøm, JS, Stroemlund, LW, Nielsen, MS & MacAulay, N 2015, 'Protein kinase C-dependent regulation of connexin43 gap junctions and hemichannels', Biochemical Society Transactions, vol. 43, no. 3, pp. 519-23. https://doi.org/10.1042/BST20150040

APA

Alstrøm, J. S., Stroemlund, L. W., Nielsen, M. S., & MacAulay, N. (2015). Protein kinase C-dependent regulation of connexin43 gap junctions and hemichannels. Biochemical Society Transactions, 43(3), 519-23. https://doi.org/10.1042/BST20150040

Vancouver

Alstrøm JS, Stroemlund LW, Nielsen MS, MacAulay N. Protein kinase C-dependent regulation of connexin43 gap junctions and hemichannels. Biochemical Society Transactions. 2015 Jun;43(3):519-23. https://doi.org/10.1042/BST20150040

Author

Alstrøm, Jette Skov ; Stroemlund, Line Waring ; Nielsen, Morten Schak ; MacAulay, Nanna. / Protein kinase C-dependent regulation of connexin43 gap junctions and hemichannels. In: Biochemical Society Transactions. 2015 ; Vol. 43, No. 3. pp. 519-23.

Bibtex

@article{02091c642b14458d89272f9fa1351291,
title = "Protein kinase C-dependent regulation of connexin43 gap junctions and hemichannels",
abstract = "Connexin43 (Cx43) generates intercellular gap junction channels involved in, among others, cardiac and brain function. Gap junctions are formed by the docking of two hemichannels from neighbouring cells. Undocked Cx43 hemichannels can upon different stimuli open towards the extracellular matrix and allow transport of molecules such as fluorescent dyes and ATP. A range of phosphorylated amino acids have been detected in the C-terminus of Cx43 and their physiological role has been intensively studied both in the gap junctional form of Cx43 and in its hemichannel configuration. We present the current knowledge of protein kinase C (PKC)-dependent regulation of Cx43 and discuss the divergent results.",
author = "Alstr{\o}m, {Jette Skov} and Stroemlund, {Line Waring} and Nielsen, {Morten Schak} and Nanna MacAulay",
year = "2015",
month = jun,
doi = "10.1042/BST20150040",
language = "English",
volume = "43",
pages = "519--23",
journal = "Biochemical Society Transactions",
issn = "0300-5127",
publisher = "Portland Press Ltd.",
number = "3",

}

RIS

TY - JOUR

T1 - Protein kinase C-dependent regulation of connexin43 gap junctions and hemichannels

AU - Alstrøm, Jette Skov

AU - Stroemlund, Line Waring

AU - Nielsen, Morten Schak

AU - MacAulay, Nanna

PY - 2015/6

Y1 - 2015/6

N2 - Connexin43 (Cx43) generates intercellular gap junction channels involved in, among others, cardiac and brain function. Gap junctions are formed by the docking of two hemichannels from neighbouring cells. Undocked Cx43 hemichannels can upon different stimuli open towards the extracellular matrix and allow transport of molecules such as fluorescent dyes and ATP. A range of phosphorylated amino acids have been detected in the C-terminus of Cx43 and their physiological role has been intensively studied both in the gap junctional form of Cx43 and in its hemichannel configuration. We present the current knowledge of protein kinase C (PKC)-dependent regulation of Cx43 and discuss the divergent results.

AB - Connexin43 (Cx43) generates intercellular gap junction channels involved in, among others, cardiac and brain function. Gap junctions are formed by the docking of two hemichannels from neighbouring cells. Undocked Cx43 hemichannels can upon different stimuli open towards the extracellular matrix and allow transport of molecules such as fluorescent dyes and ATP. A range of phosphorylated amino acids have been detected in the C-terminus of Cx43 and their physiological role has been intensively studied both in the gap junctional form of Cx43 and in its hemichannel configuration. We present the current knowledge of protein kinase C (PKC)-dependent regulation of Cx43 and discuss the divergent results.

U2 - 10.1042/BST20150040

DO - 10.1042/BST20150040

M3 - Journal article

C2 - 26009201

VL - 43

SP - 519

EP - 523

JO - Biochemical Society Transactions

JF - Biochemical Society Transactions

SN - 0300-5127

IS - 3

ER -

ID: 143665697