Results 161 to 170 of about 5,262 (204)

Depression exacerbates AD pathology through lactate-dependent activation of microglial Kv1.3 to promote Aβ-containing exosome spreading. [PDF]

J Neuroinflammation
Liu X, Wang H, Tian X, Luo Y, Ma M, Zheng Z, Wang Y, Feng S, Wang Q, Xu Z, Yao W, Ren S.   +11 more
europepmc   +1 more source

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Transmembrane Biogenesis of Kv1.3

Biochemistry, 2000
Using a combination of protease protection, glycosylation, and carbonate extraction assays, we have characterized the topogenic determinants encoded by Kv1.3 segments that mediate translocation events during endoplasmic reticulum (ER) biogenesis. Transmembrane segments S1, S2, S3, S5, and S6 initiate translocation, only S1 and S2 strongly (>60%) anchor
L, Tu, J, Wang, A, Helm, W R, Skach, C, Deutsch   +4 more
openaire   +2 more sources

Immunosuppressive effects of a Kv1.3 inhibitor

Cellular Immunology, 2003
The voltage gated potassium channel (Kv1.3) has been shown to play a role in immune responsiveness. Blockade of the channel led to diminution of T cell activation and delayed type hypersensitivity. Previous in vitro studies of the blockade were focused on T cell activation and proliferation. In this study we examined other T and monocytic cell mediated
Kashmira, Shah, J, Tom Blake, Christopher, Huang, Paul, Fischer, Gloria C, Koo   +4 more
openaire   +2 more sources

Open channel block of Kv1.3 by rosiglitazone and troglitazone: Kv1.3 as the pharmacological target for rosiglitazone

Naunyn-Schmiedeberg's Archives of Pharmacology, 2006
The effects of rosiglitazone and troglitazone were examined on cloned Kv1.3 channels stably expressed in Chinese hamster ovary cells using the whole-cell configuration of the patch-clamp technique. Rosiglitazone decreased the Kv1.3 currents and accelerated the decay rate of current inactivation in a concentration-dependent manner with an IC(50) of 18.6
Hye Sook, Ahn, Sung Eun, Kim, Hyun-Jong, Jang, Myung-Jun, Kim, Duck-Joo, Rhie, Shin-Hee, Yoon, Yang-Hyeok, Jo, Myung-Suk, Kim, Ki-Wug, Sung, Seong Yun, Kim, Sang June, Hahn   +10 more
openaire   +2 more sources

Molecular Determinants of Kv1.3 Potassium Channels-Induced Proliferation [PDF]

Journal of Biological Chemistry, 2016
Changes in voltage-dependent potassium channels (Kv channels) associate to proliferation in many cell types, including transfected HEK293 cells. In this system Kv1.5 overexpression decreases proliferation, whereas Kv1.3 expression increases it independently of K(+) fluxes.
Inés Alvarez-Miguel, Maria Teresa Pérez-García, José Ramón López López   +2 more
exaly   +5 more sources

Kv1.3 potassium channels in human alveolar macrophages

American Journal of Physiology-Lung Cellular and Molecular Physiology, 2003
Human alveolar macrophages were obtained from macroscopically normal lung tissue obtained at surgical resections, isolated by adherence, and identified by morphology. Whole cell recordings were made from cells 1-3 h in culture, using electrodes containing potassium chloride.
Mackenzie, Amanda B., Chirakkal, Hari, North, R. Alan   +2 more
openaire   +3 more sources

Novel Kv1.3 blockers for immunosuppression: WO2012155199

Expert Opinion on Therapeutic Patents, 2013
A recent patent application from Bionomics/Merck Serono describes novel compounds as blockers of the voltage-gated Kv1.3 ion channel. The blockade of this channel shows great promise as a new therapeutic target for the treatment of autoimmune disorders such as multiple sclerosis, psoriasis, diabetes and rheumatoid arthritis.
openaire   +2 more sources

Kv1.3 in the spotlight for treating immune diseases

Expert Opinion on Therapeutic Targets
Kv1.3 is the main voltage-gated potassium channel of leukocytes from both the innate and adaptive immune systems. Channel function is required for common processes such as Ca2+ signaling but also for cell-specific events. In this context, alterations in Kv1.3 are associated with multiple immune disorders.
María, Navarro-Pérez, Jesusa, Capera, Anna, Benavente-Garcia, Silvia, Cassinelli, Magalí, Colomer-Molera, Antonio, Felipe   +5 more
openaire   +2 more sources

Pegylation:  A Method for Assessing Topological Accessibilities in Kv1.3

Biochemistry, 2001
Each subunit of a voltage-gated potassium channel (Kv) contains six putative transmembrane segments, S1-S6, and a cytosolic N-terminal recognition domain, T1. Although it is well-established that Kv channels are tetrameric structures, the protein-protein, protein-lipid, and protein-aqueous interfaces are not precisely mapped.
J, Lu, C, Deutsch
openaire   +2 more sources