Patch-clamp measurement of ICRAC and ORAI channel activity.

Alansary, Dalia; Kilch, Tatiana; Holzmann, Christian; Peinelt, Christine; Hoth, Markus; Lis, Annette (2014). Patch-clamp measurement of ICRAC and ORAI channel activity. Cold Spring Harbor protocols, 2014(6), pp. 602-607. Cold Spring Harbor Laboratory 10.1101/pdb.top066795

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Depletion of internal Ca(2+) stores activates store-operated Ca(2+) channels. The most prominent members of this class of channels are Ca(2+) release-activated Ca(2+) (CRAC) channels, which are present in a variety of cell types including immune cells. CRAC channels are composed of ORAI proteins, which are activated by endoplasmic reticulum-bound STIM proteins on Ca(2+) store depletion. The underlying Ca(2+) current is called ICRAC, which is required for many cellular functions including T-cell activation, mast cell activation, Ca(2+)-dependent gene expression, and refilling of internal Ca(2+) stores. To analyze ICRAC or the Ca(2+) current through heterologously expressed ORAI channels, whole-cell patch clamp is the technique of choice. It allows the direct analysis of ion currents through CRAC/ORAI channels. The patch-clamp technique has been used to determine selectivity, permeability, rectification, inactivation, and several other biophysical and pharmacological properties of the channels, and is the most direct and reliable technique to analyze ICRAC.

Item Type:

Journal Article (Original Article)

Division/Institute:

04 Faculty of Medicine > Pre-clinic Human Medicine > Institute of Biochemistry and Molecular Medicine

UniBE Contributor:

Peinelt, Christine

Subjects:

500 Science > 570 Life sciences; biology
600 Technology > 610 Medicine & health

ISSN:

1940-3402

Publisher:

Cold Spring Harbor Laboratory

Language:

English

Submitter:

Christine Peinelt

Date Deposited:

18 Jun 2018 14:35

Last Modified:

18 Jun 2018 14:35

Publisher DOI:

10.1101/pdb.top066795

PubMed ID:

24890214

BORIS DOI:

10.7892/boris.97451

URI:

https://boris.unibe.ch/id/eprint/97451

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