U.S. flag

An official website of the United States government

Format

Send to:

Choose Destination
    • Showing Current items.

    KCNMB1 potassium calcium-activated channel subfamily M regulatory beta subunit 1 [ Homo sapiens (human) ]

    Gene ID: 3779, updated on 10-Dec-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    that epigenetic upregulation of KCNMB1 contributes to increased large-conductance (Big) potassium channel activity in idiopathic pulmonary fibrosis fibroblasts

    The Role of KCNMB1 and BK Channels in Myofibroblast Differentiation and Pulmonary Fibrosis.
    Scruggs AM, Grabauskas G, Huang SK., Free PMC Article

    05/16/2020
    Decreased protein expression and altered intrinsic properties of BKbeta1 channels mediates abnormal vasodilation in the coronary microvasculature of type 2 diabetics.

    Downregulation of BK channel function and protein expression in coronary arteriolar smooth muscle cells of type 2 diabetic patients.
    Lu T, Chai Q, Jiao G, Wang XL, Sun X, Furuseth JD, Stulak JM, Daly RC, Greason KL, Cha YM, Lee HC., Free PMC Article

    02/1/2020
    Expression of vascular large-conductance calcium-activated potassium channel Kcnmb1 is regulated by Nrf2 signaling.

    Regulation of vascular large-conductance calcium-activated potassium channels by Nrf2 signalling.
    Li Y, Wang XL, Sun X, Chai Q, Li J, Thompson B, Shen WK, Lu T, Lee HC.

    12/16/2017
    These results provide further insights into the mechanism of modulation of the different N-terminal regions of the BKCa channel by beta-subunits.

    The unique N-terminal sequence of the BKCa channel α-subunit determines its modulation by β-subunits.
    Lorca RA, Ma X, England SK., Free PMC Article

    10/7/2017
    By introducing lanthanide binding tags in the extracellular region of the alpha- or beta1-subunit, we determined (i) a basic extracellular map of the BK channel, (ii) beta1-subunit-induced rearrangements of the voltage sensor in alpha-subunits, and (iii) the relative position of the beta1-subunit within the alpha/beta1-subunit complex.

    β1-subunit-induced structural rearrangements of the Ca2+- and voltage-activated K+ (BK) channel.
    Castillo JP, Sánchez-Rodríguez JE, Hyde HC, Zaelzer CA, Aguayo D, Sepúlveda RV, Luk LY, Kent SB, Gonzalez-Nilo FD, Bezanilla F, Latorre R., Free PMC Article

    01/28/2017
    The study demonstrates that both transmembrane domains of BKbeta1 are required to provide the characteristic ion current phenotype of beta1-containing BK channels.

    Both transmembrane domains of BK β1 subunits are essential to confer the normal phenotype of β1-containing BK channels.
    Kuntamallappanavar G, Toro L, Dopico AM., Free PMC Article

    12/26/2015
    Data show that two lysine residues that are unique to the N terminus of calcium-activated potassium channel subunit beta-1 were identified to be sufficient for voltage-sensor modulation.

    Molecular mechanism underlying β1 regulation in voltage- and calcium-activated potassium (BK) channels.
    Castillo K, Contreras GF, Pupo A, Torres YP, Neely A, González C, Latorre R., Free PMC Article

    07/25/2015
    To determine the relationship between atherosclerosis and KCNMB1, we studied some atherogenic factors affecting vascular tone. Blood of atherosclerotic patients shows increased concentration of 7-ketocholesterol, possibly a harmful lipid to blood vessels.

    7-Ketocholesterol induces the reduction of KCNMB1 in atherosclerotic blood vessels.
    Son Y, Chun W, Ahn YT, Kim K, Lee CW, Kim JM, Lee C, An WG.

    07/25/2015
    Bisphenol A activates BK alpha via an extracellular site and that Bisphenol A-sensitivity is increased by the beta1 subunit.

    Bisphenol A activates BK channels through effects on α and β1 subunits.
    Rottgen TS, Fancher IS, Asano S, Widlanski TS, Dick GM., Free PMC Article

    06/20/2015
    N-terminal isoforms of the large-conductance Ca(2)-activated K channel are differentially modulated by the auxiliary beta1-subunit.

    N-terminal isoforms of the large-conductance Ca²⁺-activated K⁺ channel are differentially modulated by the auxiliary β1-subunit.
    Lorca RA, Stamnes SJ, Pillai MK, Hsiao JJ, Wright ME, England SK., Free PMC Article

    05/31/2014
    In large-conductance calcium-dependent potassium channels, beta1 and beta2 subunits alter the voltage sensing domain-cytosolic domain interface.

    The interface between membrane-spanning and cytosolic domains in Ca²+-dependent K+ channels is involved in β subunit modulation of gating.
    Sun X, Shi J, Delaloye K, Yang X, Yang H, Zhang G, Cui J., Free PMC Article

    10/19/2013
    The results indicate that the beta1-subunit can form a tripartite complex with TP and MaxiKalpha, has the ability to associate with each protein independently.

    The β1-subunit of the MaxiK channel associates with the thromboxane A2 receptor and reduces thromboxane A2 functional effects.
    Li M, Zhang Z, Koh H, Lu R, Jiang Z, Alioua A, Garcia-Valdes J, Stefani E, Toro L., Free PMC Article

    03/30/2013
    HIF-1alpha increases KCNMB1 expression in response to hypoxia in human pulmonary artery smooth muscle cells by binding to two hypoxia response elements located at -3,540 to -3,311 of the KCNMB1 promoter

    Hypoxia-inducible factor-1α regulates KCNMB1 expression in human pulmonary artery smooth muscle cells.
    Ahn YT, Kim YM, Adams E, Lyu SC, Alvira CM, Cornfield DN., Free PMC Article

    03/24/2012
    Cloned BK(Ca) channel directly regulated apoptosis and proliferation of HEK293 cell under hyperglycemia condition.

    High glucose alters apoptosis and proliferation in HEK293 cells by inhibition of cloned BK Ca channel.
    Chang H, Ma YG, Wang YY, Song Z, Li Q, Yang N, Zhao HZ, Feng HZ, Chang YM, Ma J, Yu ZB, Xie MJ.

    05/21/2011
    Here we found that KCNMB1 common variant Glu65Lys influences glomerular filtration rate across multiple populations of different clinical characteristics and biogeographic ancestries.

    Common charge-shift mutation Glu65Lys in K+ channel β₁-Subunit KCNMB1: pleiotropic consequences for glomerular filtration rate and progressive renal disease.
    Chen Y, Salem RM, Rao F, Fung MM, Bhatnagar V, Pandey B, Mahata M, Waalen J, Nievergelt CM, Lipkowitz MS, Hamilton BA, Mahata SK, O'Connor DT., Free PMC Article

    03/19/2011
    downregulation of vascular BK-beta(1) expression in diabetes and in high-glucose culture conditions was associated with FOXO-3a/FBXO-dependent increase in BK-beta(1) degradation.

    Muscle-specific f-box only proteins facilitate bk channel β(1) subunit downregulation in vascular smooth muscle cells of diabetes mellitus.
    Zhang DM, He T, Katusic ZS, Lee HC, Lu T., Free PMC Article

    01/29/2011
    In transfected HEK293 cells, activation of cloned BK(Ca) channel induced apoptosis, whereas inhibition of cloned BK(Ca) channel decreased apoptosis.

    Activation of BKCa channel is associated with increased apoptosis of cerebrovascular smooth muscle cells in simulated microgravity rats.
    Xie MJ, Ma YG, Gao F, Bai YG, Cheng JH, Chang YM, Yu ZB, Ma J.

    06/28/2010
    The expressed hSloalpha + beta1 subunit complex demonstrated to be fully functional for its typical single-channel traces, Ca(2+)-sensitivity, voltage-dependency, high conductance (151 +/- 7 pS), and its pharmacological activation and inhibition.

    Coexpression and characterization of the human large-conductance Ca(2+)-activated K (+) channel alpha + beta1 subunits in HEK293 cells.
    Li J, Deng CL, Gao F, Cheng JH, Yu ZB, Liu L, Xie MJ.

    01/25/2010
    Results reveal the first ion channel subunit as a direct target of SRF-MYOCD transactivation, providing further insight into the role of MYOCD as a master regulator of the SMC contractile phenotype.

    The smooth muscle cell-restricted KCNMB1 ion channel subunit is a direct transcriptional target of serum response factor and myocardin.
    Long X, Tharp DL, Georger MA, Slivano OJ, Lee MY, Wamhoff BR, Bowles DK, Miano JM., Free PMC Article

    01/25/2010
    Cell membrane stretch and cell volume sensitivity are independently regulated by KCNMB1 (BK) and KCNQ1 channels, respectively.

    Cell volume and membrane stretch independently control K+ channel activity.
    Hammami S, Willumsen NJ, Olsen HL, Morera FJ, Latorre R, Klaerke DA., Free PMC Article

    01/21/2010
    Report beta subunit (KNMB1-4)-specific modulations of BK channel function by a Slo1 mutation associated with epilepsy and dyskinesia.

    {beta} subunit-specific modulations of BK channel function by a mutation associated with epilepsy and dyskinesia.
    Lee US, Cui J., Free PMC Article

    01/21/2010
    genetic polymorphism shows sex-specific association with asthma severity in male african population

    Gene-environmental interaction in the development of atopic asthma: new developments.
    Le Souëf PN.

    01/21/2010
    maxi-K(+) beta1-subunit could contribute to vascular dysregulation in severe obstructive sleep apnea syndrome patients. Leukocyte beta1 expression may be independent readout of hypoxemia that could be useful as molecular marker for impending hypertension.

    Maxi-K+ channel beta1 expression in sleep apnea patients and its modulation by CPAP treatment.
    Navarro-Antolín J, Carmona-Bernal C, Rivero-Valdenebro V, Villar J, Capote F, López-Barneo J.

    01/21/2010
    The KCNMB1 E65K variant is associated with reduced central pulse pressure.

    The KCNMB1 E65K variant is associated with reduced central pulse pressure in the community-based Framingham Offspring Cohort.
    Kelley-Hedgepeth A, Peter I, Montefusco MC, Levy D, Benjamin EJ, Vasan RS, Mendelsohn ME, Housman D, Huggins GS, Mitchell GF., Free PMC Article

    01/21/2010
    The protective effect of KCNMB1 E65K against hypertension is restricted to blood pressure treatment with beta-blockade.

    The protective effect of KCNMB1 E65K against hypertension is restricted to blood pressure treatment with beta-blockade.
    Kelley-Hedgepeth A, Peter I, Kip K, Montefusco M, Kogan S, Cox D, Ordovas J, Levy D, Reis S, Mendelsohn M, Housman D, Huggins G., Free PMC Article

    01/21/2010
    firstprevious page of 2 nextlast