Proteome landscape and interactome of voltage-gated potassium channel 1.6 (Kv1.6) of the murine ophthalmic artery and neuroretina.

Autor: Perumal N; Department of Ophthalmology, University Medical Centre of the Johannes Gutenberg University Mainz, Mainz, Germany., Yurugi H; Cell Biology Unit, University Medical Centre of the Johannes Gutenberg University Mainz, Germany., Dahm K; Cell Biology Unit, University Medical Centre of the Johannes Gutenberg University Mainz, Germany., Rajalingam K; Cell Biology Unit, University Medical Centre of the Johannes Gutenberg University Mainz, Germany., Grus FH; Department of Ophthalmology, University Medical Centre of the Johannes Gutenberg University Mainz, Mainz, Germany., Pfeiffer N; Department of Ophthalmology, University Medical Centre of the Johannes Gutenberg University Mainz, Mainz, Germany., Manicam C; Department of Ophthalmology, University Medical Centre of the Johannes Gutenberg University Mainz, Mainz, Germany. Electronic address: caroline.manicam@unimedizin-mainz.de.
Jazyk: angličtina
Zdroj: International journal of biological macromolecules [Int J Biol Macromol] 2024 Feb; Vol. 257 (Pt 1), pp. 128464. Date of Electronic Publication: 2023 Dec 02.
DOI: 10.1016/j.ijbiomac.2023.128464
Abstrakt: The voltage-gated potassium channel 1.6 (Kv1.6) plays a vital role in ocular neurovascular beds and exerts its modulatory functions via interaction with other proteins. However, the interactome and their potential roles remain unknown. Here, the global proteome landscape of the ophthalmic artery (OA) and neuroretina was mapped, followed by the determination of Kv1.6 interactome and validation of its functionality and cellular localization. Microfluorimetric analysis of intracellular [K + ] and Western blot validated the native functionality and cellular expression of the recombinant Kv1.6 channel protein. A total of 54, 9 and 28 Kv1.6-interacting proteins were identified in the mouse OA and, retina of mouse and rat, respectively. The Kv1.6-protein partners in the OA, namely actin cytoplasmic 2, alpha-2-macroglobulin and apolipoprotein A-I, were implicated in the maintenance of blood vessel integrity by regulating integrin-mediated adhesion to extracellular matrix and Ca 2+ flux. Many retinal protein interactors, particularly the ADP/ATP translocase 2 and cytoskeleton protein tubulin, were involved in endoplasmic reticulum stress response and cell viability. Three common interactors were found in all samples comprising heat shock cognate 71 kDa protein, Ig heavy constant gamma 1 and Kv1.6 channel. This foremost in-depth investigation enriched and identified the elusive Kv1.6 channel and, elucidated its complex interactome.
Competing Interests: Declaration of competing interest None.
(Copyright © 2023 The Author(s). Published by Elsevier B.V. All rights reserved.)
Databáze: MEDLINE
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