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Artículos de revistas sobre el tema "CaVβ1"

Autor: Grafiati

Publicado: 14 de diciembre de 2024

Última modificación: 31 de julio de 2025

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1

Cohen, Risa M., Jason D. Foell, Ravi C. Balijepalli, Vaibhavi Shah, Johannes W. Hell та Timothy J. Kamp. "Unique modulation of L-type Ca2+ channels by short auxiliary β1d subunit present in cardiac muscle". American Journal of Physiology-Heart and Circulatory Physiology 288, № 5 (2005): H2363—H2374. http://dx.doi.org/10.1152/ajpheart.00348.2004.

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Recent studies have identified a growing diversity of splice variants of auxiliary Ca2+ channel Cavβ subunits. The Cavβ1d isoform encodes a putative protein composed of the amino-terminal half of the full-length Cavβ1 isoform and thus lacks the known high-affinity binding site that recognizes the Ca2+ channel α1-subunit, the α-binding pocket. The present study investigated whether the Cavβ1d subunit is expressed at the protein level in heart, and whether it exhibits any of the functional properties typical of full-length Cavβ subunits. On Western blots, an antibody directed against the unique

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2

Foell, Jason D., Ravi C. Balijepalli, Brian P. Delisle та ін. "Molecular heterogeneity of calcium channel β-subunits in canine and human heart: evidence for differential subcellular localization". Physiological Genomics 17, № 2 (2004): 183–200. http://dx.doi.org/10.1152/physiolgenomics.00207.2003.

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Multiple Ca2+ channel β-subunit (Cavβ) isoforms are known to differentially regulate the functional properties and membrane trafficking of high-voltage-activated Ca2+ channels, but the precise isoform expression pattern of Cavβ subunits in ventricular muscle has not been fully characterized. Using sequence data from the Human Genome Project to define the intron/exon structure of the four known Cavβ genes, we designed a systematic RT-PCR strategy to screen human and canine left ventricular myocardial samples for all known Cavβ isoforms. A total of 18 different Cavβ isoforms were detected in bot

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3

Despang, Patrick, Sarah Salamon, Alexandra Breitenkamp, Elza Kuzmenkina та Jan Matthes. "Inhibitory effects on L- and N-type calcium channels by a novel CaVβ1 variant identified in a patient with autism spectrum disorder". Naunyn-Schmiedeberg's Archives of Pharmacology 395, № 4 (2022): 459–70. http://dx.doi.org/10.1007/s00210-022-02213-7.

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AbstractVoltage-gated calcium channel (VGCC) subunits have been genetically associated with autism spectrum disorders (ASD). The properties of the pore-forming VGCC subunit are modulated by auxiliary β-subunits, which exist in four isoforms (CaVβ1-4). Our previous findings suggested that activation of L-type VGCCs is a common feature of CaVβ2 subunit mutations found in ASD patients. In the current study, we functionally characterized a novel CaVβ1b variant (p.R296C) identified in an ASD patient. We used whole-cell and single-channel patch clamp to study the effect of CaVβ1b_R296C on the functi

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4

Traoré, Massiré, Christel Gentil, Chiara Benedetto та ін. "An embryonic CaVβ1 isoform promotes muscle mass maintenance via GDF5 signaling in adult mouse". Science Translational Medicine 11, № 517 (2019): eaaw1131. http://dx.doi.org/10.1126/scitranslmed.aaw1131.

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Deciphering the mechanisms that govern skeletal muscle plasticity is essential to understand its pathophysiological processes, including age-related sarcopenia. The voltage-gated calcium channel CaV1.1 has a central role in excitation-contraction coupling (ECC), raising the possibility that it may also initiate the adaptive response to changes during muscle activity. Here, we revealed the existence of a gene transcription switch of the CaV1.1 β subunit (CaVβ1) that is dependent on the innervation state of the muscle in mice. In a mouse model of sciatic denervation, we showed increased expressi

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5

Belkacemi, Anouar, Andreas Beck, Barbara Wardas, Petra Weissgerber та Veit Flockerzi. "IP3-dependent Ca2+ signals are tightly controlled by Cavβ3, but not by Cavβ1, 2 and 4". Cell Calcium 104 (червень 2022): 102573. http://dx.doi.org/10.1016/j.ceca.2022.102573.

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6

Heneghan, John F., Tora Mitra-Ganguli, Lee F. Stanish, Liwang Liu, Rubing Zhao та Ann R. Rittenhouse. "The Ca2+ channel β subunit determines whether stimulation of Gq-coupled receptors enhances or inhibits N current". Journal of General Physiology 134, № 5 (2009): 369–84. http://dx.doi.org/10.1085/jgp.200910203.

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In superior cervical ganglion (SCG) neurons, stimulation of M1 receptors (M1Rs) produces a distinct pattern of modulation of N-type calcium (N-) channel activity, enhancing currents elicited with negative test potentials and inhibiting currents elicited with positive test potentials. Exogenously applied arachidonic acid (AA) reproduces this profile of modulation, suggesting AA functions as a downstream messenger of M1Rs. In addition, techniques that diminish AA's concentration during M1R stimulation minimize N-current modulation. However, other studies suggest depletion of phosphatidylinositol

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7

Brown, Betty, M. Steven Oberste, Kaija Maher, and Mark A. Pallansch. "Complete Genomic Sequencing Shows that Polioviruses and Members of Human Enterovirus Species C Are Closely Related in the Noncapsid Coding Region." Journal of Virology 77, no. 16 (2003): 8973–84. http://dx.doi.org/10.1128/jvi.77.16.8973-8984.2003.

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ABSTRACT The 65 human enterovirus serotypes are currently classified into five species: Poliovirus (3 serotypes), Human enterovirus A (HEV-A) (12 serotypes), HEV-B (37 serotypes), HEV-C (11 serotypes), and HEV-D (2 serotypes). Coxsackie A virus (CAV) serotypes 1, 11, 13, 15, 17, 18, 19, 20, 21, 22, and 24 constitute HEV-C. We have determined the complete genome sequences for the remaining nine HEV-C serotypes and compared them with the complete sequences of CAV21, CAV24, and the polioviruses. The viruses were most diverse in the capsid region (4 to 36% amino acid difference). A high degree of

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8

Taylor, Jackson, Tan Zhang, Laura Messi та ін. "The Cavβ1 Subunit Regulates Gene Expression in Muscle Progenitor Cells". Biophysical Journal 102, № 3 (2012): 365a. http://dx.doi.org/10.1016/j.bpj.2011.11.1993.

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9

Traore, M., C. Gentil, C. Benedetto та ін. "P.133A novel CaVβ1 isoform connecting voltage sensing with muscle mass homeostasis". Neuromuscular Disorders 29 (жовтень 2019): S87. http://dx.doi.org/10.1016/j.nmd.2019.06.189.

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10

Buraei, Zafir, та Jian Yang. "The β Subunit of Voltage-Gated Ca2+ Channels". Physiological Reviews 90, № 4 (2010): 1461–506. http://dx.doi.org/10.1152/physrev.00057.2009.

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Calcium regulates a wide spectrum of physiological processes such as heartbeat, muscle contraction, neuronal communication, hormone release, cell division, and gene transcription. Major entryways for Ca2+ in excitable cells are high-voltage activated (HVA) Ca2+ channels. These are plasma membrane proteins composed of several subunits, including α1, α2δ, β, and γ. Although the principal α1 subunit (Cavα1) contains the channel pore, gating machinery and most drug binding sites, the cytosolic auxiliary β subunit (Cavβ) plays an essential role in regulating the surface expression and gating proper

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11

Park, Won Sun, Soon Chul Heo, Eun Su Jeon та ін. "Functional expression of smooth muscle-specific ion channels in TGF-β1-treated human adipose-derived mesenchymal stem cells". American Journal of Physiology-Cell Physiology 305, № 4 (2013): C377—C391. http://dx.doi.org/10.1152/ajpcell.00404.2012.

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Human adipose tissue-derived mesenchymal stem cells (hASCs) have the power to differentiate into various cell types including chondrocytes, osteocytes, adipocytes, neurons, cardiomyocytes, and smooth muscle cells. We characterized the functional expression of ion channels after transforming growth factor-β1 (TGF-β1)-induced differentiation of hASCs, providing insights into the differentiation of vascular smooth muscle cells. The treatment of hASCs with TGF-β1 dramatically increased the contraction of a collagen-gel lattice and the expression levels of specific genes for smooth muscle including

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12

Xie, Mian, Xiang Li, Jing Han та ін. "Facilitation versus depression in cultured hippocampal neurons determined by targeting of Ca2+ channel Cavβ4 versus Cavβ2 subunits to synaptic terminals". Journal of Cell Biology 178, № 3 (2007): 489–502. http://dx.doi.org/10.1083/jcb.200702072.

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Ca2+ channel β subunits determine the transport and physiological properties of high voltage–activated Ca2+ channel complexes. Our analysis of the distribution of the Cavβ subunit family members in hippocampal neurons correlates their synaptic distribution with their involvement in transmitter release. We find that exogenously expressed Cavβ4b and Cavβ2a subunits distribute in clusters and localize to synapses, whereas Cavβ1b and Cavβ3 are homogenously distributed. According to their localization, Cavβ2a and Cavβ4b subunits modulate the synaptic plasticity of autaptic hippocampal neurons (i.e.

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13

Béguin, Pascal, Kazuaki Nagashima, Ramasubbu N. Mahalakshmi, et al. "BARP suppresses voltage-gated calcium channel activity and Ca2+-evoked exocytosis." Journal of Cell Biology 205, no. 2 (2014): 233–49. http://dx.doi.org/10.1083/jcb.201304101.

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Voltage-gated calcium channels (VGCCs) are key regulators of cell signaling and Ca2+-dependent release of neurotransmitters and hormones. Understanding the mechanisms that inactivate VGCCs to prevent intracellular Ca2+ overload and govern their specific subcellular localization is of critical importance. We report the identification and functional characterization of VGCC β-anchoring and -regulatory protein (BARP), a previously uncharacterized integral membrane glycoprotein expressed in neuroendocrine cells and neurons. BARP interacts via two cytosolic domains (I and II) with all Cavβ subunit

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14

Sandoval, Alejandro, Alejandra Corzo-López, Paz Duran та ін. "The Leucine-Rich Repeat Kinase 2 Variant LRRK2G2019S Up-Regulates L-Type (CaV1.3) Calcium Channel via the CaVβ3 Subunit: Possible Role in the Pathogenesis of Parkinson’s Disease". International Journal of Molecular Sciences 26, № 7 (2025): 3229. https://doi.org/10.3390/ijms26073229.

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Voltage-gated Ca2+ (CaV) channels are transmembrane proteins comprising the pore-forming subunit CaVα1 and the ancillary proteins CaVα2δ and CaVβ. They are expressed in various tissues, including the nervous system, where they regulate Ca2+ entry in response to membrane potential changes. The increase in intracellular Ca2+ allows for regulating cell excitability and releasing neurotransmitters, among other cellular events. Leucine-rich repeat kinase 2 (LRRK2) is a serine–threonine kinase involved in vesicular mobilization. Previously, it has been shown that LRRK2 regulates neurotransmission by

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15

Findeisen, Felix, and Daniel L. Minor. "Disruption of the IS6-AID Linker Affects Voltage-gated Calcium Channel Inactivation and Facilitation." Journal of General Physiology 133, no. 3 (2009): 327–43. http://dx.doi.org/10.1085/jgp.200810143.

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Two processes dominate voltage-gated calcium channel (CaV) inactivation: voltage-dependent inactivation (VDI) and calcium-dependent inactivation (CDI). The CaVβ/CaVα1-I-II loop and Ca2+/calmodulin (CaM)/CaVα1–C-terminal tail complexes have been shown to modulate each, respectively. Nevertheless, how each complex couples to the pore and whether each affects inactivation independently have remained unresolved. Here, we demonstrate that the IS6–α-interaction domain (AID) linker provides a rigid connection between the pore and CaVβ/I-II loop complex by showing that IS6-AID linker polyglycine mutat

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16

Gonzalez-Gutierrez, Giovanni, Erick Miranda-Laferte, David Naranjo, Patricia Hidalgo та Alan Neely. "Mutations of Nonconserved Residues within the Calcium Channel α1-interaction Domain Inhibit β-Subunit Potentiation". Journal of General Physiology 132, № 3 (2008): 383–95. http://dx.doi.org/10.1085/jgp.200709901.

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Voltage-dependent calcium channels consist of a pore-forming subunit (CaVα1) that includes all the molecular determinants of a voltage-gated channel, and several accessory subunits. The ancillary β-subunit (CaVβ) is a potent activator of voltage-dependent calcium channels, but the mechanisms and structural bases of this regulation remain elusive. CaVβ binds reversibly to a conserved consensus sequence in CaVα1, the α1-interaction domain (AID), which forms an α-helix when complexed with CaVβ. Conserved aromatic residues face to one side of the helix and strongly interact with a hydrophobic pock

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17

Romano, Antonella, Antonia Feola, Antonio Porcellini, et al. "Estrogen Induces Selective Transcription of Caveolin1 Variants in Human Breast Cancer through Estrogen Responsive Element-Dependent Mechanisms." International Journal of Molecular Sciences 21, no. 17 (2020): 5989. http://dx.doi.org/10.3390/ijms21175989.

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The estrogen receptor (ER) signaling regulates numerous physiological processes mainly through activation of gene transcription (genomic pathways). Caveolin1 (CAV1) is a membrane-resident protein that behaves as platform to enable different signaling molecules and receptors for membrane-initiated pathways. CAV1 directly interacts with ERs and allows their localization on membrane with consequent activation of ER-non-genomic pathways. Loss of CAV1 function is a common feature of different types of cancers, including breast cancer. Two protein isoforms, CAV1α and CAV1β, derived from two alternat

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18

Jha, Mithilesh, Archana Jha, Ashish Singh та ін. "Essential role of Cavβ2 in T Cell development and homeostasis. (LYM7P.715)". Journal of Immunology 192, № 1_Supplement (2014): 193.3. http://dx.doi.org/10.4049/jimmunol.192.supp.193.3.

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Abstract Although many of the molecular components that regulate TCR signaling and thymocyte development are well characterized, the interactions between these molecules and their assembly in signaling complexes have remained elusive. Here, we report a novel and intriguing role of β2 regulatory subunit of voltage gated calcium channels (Cavβ2) during T cells development in thymus. We found that the T cell specific ablation of Cavβ2 resulted in severe reduction in thymocytes. Cavβ2-deficient DN and DP thymocytes were prone to die spontaneously. Consequently, the lack of Cavβ2 led to substantial

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19

Taylor, Jackson, Andrea Pereyra, Tan Zhang та ін. "The Cavβ1a subunit regulates gene expression and suppresses myogenin in muscle progenitor cells". Journal of Cell Biology 205, № 6 (2014): 829–46. http://dx.doi.org/10.1083/jcb.201403021.

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Voltage-gated calcium channel (Cav) β subunits are auxiliary subunits to Cavs. Recent reports show Cavβ subunits may enter the nucleus and suggest a role in transcriptional regulation, but the physiological relevance of this localization remains unclear. We sought to define the nuclear function of Cavβ in muscle progenitor cells (MPCs). We found that Cavβ1a is expressed in proliferating MPCs, before expression of the calcium conducting subunit Cav1.1, and enters the nucleus. Loss of Cavβ1a expression impaired MPC expansion in vitro and in vivo and caused widespread changes in global gene expre

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20

An, Mingwei, Xueling Chen, Zhuhong Yang, Jianyu Zhou, Shan Ye та Zhong Ding. "Co-Silencing of the Voltage-Gated Calcium Channel β Subunit and High-Voltage Activated α1 Subunit by dsRNA Soaking Resulted in Enhanced Defects in Locomotion, Stylet Thrusting, Chemotaxis, Protein Secretion, and Reproduction in Ditylenchus destructor". International Journal of Molecular Sciences 23, № 2 (2022): 784. http://dx.doi.org/10.3390/ijms23020784.

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The voltage-gated calcium channel (VGCC) β subunit (Cavβ) protein is a kind of cytosolic auxiliary subunit that plays an important role in regulating the surface expression and gating characteristics of high-voltage-activated (HVA) calcium channels. Ditylenchus destructor is an important plant-parasitic nematode. In the present study, the putative Cavβ subunit gene of D. destructor, namely, DdCavβ, was subjected to molecular characterization. In situ hybridization assays showed that DdCavβ was expressed in all nematode tissues. Transcriptional analyses showed that DdCavβ was expressed during e

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21

Catalucci, Daniele, Deng-Hong Zhang, Jaime DeSantiago та ін. "Akt regulates L-type Ca2+ channel activity by modulating Cavα1 protein stability". Journal of Cell Biology 184, № 6 (2009): 923–33. http://dx.doi.org/10.1083/jcb.200805063.

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The insulin IGF-1–PI3K–Akt signaling pathway has been suggested to improve cardiac inotropism and increase Ca2+ handling through the effects of the protein kinase Akt. However, the underlying molecular mechanisms remain largely unknown. In this study, we provide evidence for an unanticipated regulatory function of Akt controlling L-type Ca2+ channel (LTCC) protein density. The pore-forming channel subunit Cavα1 contains highly conserved PEST sequences (signals for rapid protein degradation), and in-frame deletion of these PEST sequences results in increased Cavα1 protein levels. Our findings s

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22

Puckerin, Akil A., Donald D. Chang, Zunaira Shuja, Papiya Choudhury, Joachim Scholz, and Henry M. Colecraft. "Engineering selectivity into RGK GTPase inhibition of voltage-dependent calcium channels." Proceedings of the National Academy of Sciences 115, no. 47 (2018): 12051–56. http://dx.doi.org/10.1073/pnas.1811024115.

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Genetically encoded inhibitors for voltage-dependent Ca2+ (CaV) channels (GECCIs) are useful research tools and potential therapeutics. Rad/Rem/Rem2/Gem (RGK) proteins are Ras-like G proteins that potently inhibit high voltage-activated (HVA) Ca2+ (CaV1/CaV2 family) channels, but their nonselectivity limits their potential applications. We hypothesized that nonselectivity of RGK inhibition derives from their binding to auxiliary CaVβ-subunits. To investigate latent CaVβ-independent components of inhibition, we coexpressed each RGK individually with CaV1 (CaV1.2/CaV1.3) or CaV2 (CaV2.1/CaV2.2)

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23

Mitra-Ganguli, Tora, Iuliia Vitko, Edward Perez-Reyes та Ann R. Rittenhouse. "Orientation of palmitoylated CaVβ2a relative to CaV2.2 is critical for slow pathway modulation of N-type Ca2+ current by tachykinin receptor activation". Journal of General Physiology 134, № 5 (2009): 385–96. http://dx.doi.org/10.1085/jgp.200910204.

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The Gq-coupled tachykinin receptor (neurokinin-1 receptor [NK-1R]) modulates N-type Ca2+ channel (CaV2.2 or N channel) activity at two distinct sites by a pathway involving a lipid metabolite, most likely arachidonic acid (AA). In another study published in this issue (Heneghan et al. 2009. J. Gen Physiol. doi:10.1085/jgp.200910203), we found that the form of modulation observed depends on which CaVβ is coexpressed with CaV2.2. When palmitoylated CaVβ2a is coexpressed, activation of NK-1Rs by substance P (SP) enhances N current. In contrast, when CaVβ3 is coexpressed, SP inhibits N current. Ho

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24

Meissner, Marcel, Petra Weissgerber, Juan E. Camacho Londoño, et al. "Moderate Calcium Channel Dysfunction in Adult Mice with Inducible Cardiomyocyte-specific Excision of the cacnb2 Gene." Journal of Biological Chemistry 286, no. 18 (2011): 15875–82. http://dx.doi.org/10.1074/jbc.m111.227819.

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The major L-type voltage-gated calcium channels in heart consist of an α1C (CaV1.2) subunit usually associated with an auxiliary β subunit (CaVβ2). In embryonic cardiomyocytes, both the complete and the cardiac myocyte-specific null mutant of CaVβ2 resulted in reduction of L-type calcium currents by up to 75%, compromising heart function and causing defective remodeling of intra- and extra-embryonic blood vessels followed by embryonic death. Here we conditionally excised the CaVβ2 gene (cacnb2) specifically in cardiac myocytes of adult mice (KO). Upon gene deletion, CaVβ2 protein expression de

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Chen, Xingjuan, Degang Liu, Donghui Zhou та ін. "Small-molecule CaVα1⋅CaVβ antagonist suppresses neuronal voltage-gated calcium-channel trafficking". Proceedings of the National Academy of Sciences 115, № 45 (2018): E10566—E10575. http://dx.doi.org/10.1073/pnas.1813157115.

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Extracellular calcium flow through neuronal voltage-gated CaV2.2 calcium channels converts action potential-encoded information to the release of pronociceptive neurotransmitters in the dorsal horn of the spinal cord, culminating in excitation of the postsynaptic central nociceptive neurons. The CaV2.2 channel is composed of a pore-forming α1subunit (CaVα1) that is engaged in protein–protein interactions with auxiliary α2/δ and β subunits. The high-affinity CaV2.2α1⋅CaVβ3protein–protein interaction is essential for proper trafficking of CaV2.2 channels to the plasma membrane. Here, structure-b

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Al Katat, Aya, Juan Zhao, Angelino Calderone та Lucie Parent. "Sympathetic Stimulation Upregulates the Ca2+ Channel Subunit, CaVα2δ1, via the β1 and ERK 1/2 Pathway in Neonatal Ventricular Cardiomyocytes". Cells 11, № 2 (2022): 188. http://dx.doi.org/10.3390/cells11020188.

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Intracellular Ca2+ overload secondary to chronic hemodynamic stimuli promotes the recruitment of Ca2+-dependent signaling implicated in cardiomyocyte hypertrophy. The present study tested the hypothesis that sympathetic-mediated hypertrophy of neonatal rat ventricular cardiomyocytes (NRVMs) translated to an increase in calcium influx secondary to the upregulation of CaV1.2 channel subunits. Confocal imaging of norepinephrine (NE)-treated NRVMs revealed a hypertrophic response compared to untreated NRVMs. L-type CaV1.2 peak current density was increased 4-fold following a 24-h stimulation with

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27

Jangsangthong, Wanchana, Elza Kuzmenkina, Ann Kristin Böhnke та Stefan Herzig. "Single-Channel Monitoring of Reversible L-Type Ca2+ Channel CaVα1-CaVβ Subunit Interaction". Biophysical Journal 101, № 11 (2011): 2661–70. http://dx.doi.org/10.1016/j.bpj.2011.09.063.

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Jha, Archana, Ashish K. Singh, Petra Weissgerber та ін. "Essential roles for Cavβ2 and Cav1 channels in thymocyte development and T cell homeostasis". Science Signaling 8, № 399 (2015): ra103. http://dx.doi.org/10.1126/scisignal.aac7538.

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29

Roberts-Crowley, Mandy L., та Ann R. Rittenhouse. "Arachidonic acid inhibition of L-type calcium (CaV1.3b) channels varies with accessory CaVβ subunits". Journal of General Physiology 133, № 4 (2009): 387–403. http://dx.doi.org/10.1085/jgp.200810047.

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Arachidonic acid (AA) inhibits the activity of several different voltage-gated Ca2+ channels by an unknown mechanism at an unknown site. The Ca2+ channel pore-forming subunit (CaVα1) is a candidate for the site of AA inhibition because T-type Ca2+ channels, which do not require accessory subunits for expression, are inhibited by AA. Here, we report the unanticipated role of accessory CaVβ subunits on the inhibition of CaV1.3b L-type (L-) current by AA. Whole cell Ba2+ currents were measured from recombinant channels expressed in human embryonic kidney 293 cells at a test potential of −10 mV fr

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Bennett, Robert. "Reflecting on Editorial and Publishing Challenges: Government and Policy; The First 25 Years." Environment and Planning C: Government and Policy 26, no. 1 (2008): 1–16. http://dx.doi.org/10.1068/cav1.

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Park, Heonyong, Young-Mi Go, Ritesh Darji, et al. "Caveolin-1 regulates shear stress-dependent activation of extracellular signal-regulated kinase." American Journal of Physiology-Heart and Circulatory Physiology 278, no. 4 (2000): H1285—H1293. http://dx.doi.org/10.1152/ajpheart.2000.278.4.h1285.

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Fluid shear stress activates a member of the mitogen-activated protein (MAP) kinase family, extracellular signal-regulated kinase (ERK), by mechanisms dependent on cholesterol in the plasma membrane in bovine aortic endothelial cells (BAEC). Caveolae are microdomains of the plasma membrane that are enriched with cholesterol, caveolin, and signaling molecules. We hypothesized that caveolin-1 regulates shear activation of ERK. Because caveolin-1 is not exposed to the outside, cells were minimally permeabilized by Triton X-100 (0.01%) to deliver a neutralizing, polyclonal caveolin-1 antibody (pCa

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32

Van Petegem, Filip, Karl E. Duderstadt, Kimberly A. Clark, Michelle Wang та Daniel L. Minor. "Alanine-Scanning Mutagenesis Defines a Conserved Energetic Hotspot in the CaVα1 AID-CaVβ Interaction Site that Is Critical for Channel Modulation". Structure 16, № 2 (2008): 280–94. http://dx.doi.org/10.1016/j.str.2007.11.010.

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Colvin, Robert B. "CADI, Canti, Cavi1." Transplantation 83, no. 6 (2007): 677–78. http://dx.doi.org/10.1097/01.tp.0000262011.05196.a1.

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Bernardo, José F., Clara E. Magyar, W. Bruce Sneddon та Peter A. Friedman. "Impaired renal calcium absorption in mice lacking calcium channel β3 subunits". Canadian Journal of Physiology and Pharmacology 87, № 7 (2009): 522–30. http://dx.doi.org/10.1139/y09-035.

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Transgenic mice lacking calcium channel β3 subunits (CaVβ3) were used to determine the involvement of a multimeric calcium channel in mediating stimulated renal calcium absorption. We measured the ability of calcium channel β3 subunit-null (CaVβ3−/−) and wild-type (CaVβ3+/+) mice to increase renal calcium absorption in response to the calcium-sparing diuretic chlorothiazide (CTZ). Control rates of fractional sodium excretion were comparable in CaVβ3−/− and CaVβ3+/+ mice and CTZ increased sodium excretion similarly in both groups. CTZ enhanced calcium absorption only in wild-type CaVβ3+/+ mice.

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35

Croager, Emma. "CAV1 connection." Nature Reviews Cancer 4, no. 2 (2004): 90–91. http://dx.doi.org/10.1038/nrc1283.

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Copeland, Courtney A., Bing Han, Ajit Tiwari, et al. "A disease-associated frameshift mutation in caveolin-1 disrupts caveolae formation and function through introduction of a de novo ER retention signal." Molecular Biology of the Cell 28, no. 22 (2017): 3095–111. http://dx.doi.org/10.1091/mbc.e17-06-0421.

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Caveolin-1 (CAV1) is an essential component of caveolae and is implicated in numerous physiological processes. Recent studies have identified heterozygous mutations in the CAV1 gene in patients with pulmonary arterial hypertension (PAH), but the mechanisms by which these mutations impact caveolae assembly and contribute to disease remain unclear. To address this question, we examined the consequences of a familial PAH-associated frameshift mutation in CAV1, P158PfsX22, on caveolae assembly and function. We show that C-terminus of the CAV1 P158 protein contains a functional ER-retention signal

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El-Yazbi, Ahmed F., Woo Jung Cho, Richard Schulz та Edwin E. Daniel. "Caveolin-1 knockout alters β-adrenoceptors function in mouse small intestine". American Journal of Physiology-Gastrointestinal and Liver Physiology 291, № 6 (2006): G1020—G1030. http://dx.doi.org/10.1152/ajpgi.00159.2006.

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β-Adrenoceptors are G protein-coupled receptors whose functions are closely associated with caveolae in the heart and cultured cell lines. In the gut, they are responsible, at least in part, for the mediation of the sympathetic stimulation that might lead to intestinal paralysis postoperatively. We examined the effect of caveolin-1 knockout on the β-adrenoceptor response in mouse small intestine. The relaxation response to (−)-isoprenaline in carbachol-contracted small intestinal tissue segments was reduced in caveolin-1 knockout mice (cav1−/−) compared with their genetic controls (cav1+/+). I

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Rathor, Navneeta, Ran Zhuang, Jian-Ying Wang, James M. Donahue, Douglas J. Turner, and Jaladanki N. Rao. "Src-mediated caveolin-1 phosphorylation regulates intestinal epithelial restitution by altering Ca2+ influx after wounding." American Journal of Physiology-Gastrointestinal and Liver Physiology 306, no. 8 (2014): G650—G658. http://dx.doi.org/10.1152/ajpgi.00003.2014.

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Early mucosal restitution occurs as a consequence of intestinal epithelial cell (IEC) migration to reseal superficial wounds, but its exact mechanism remains largely unknown. Caveolin-1 (Cav1), a major component associated with caveolar lipid rafts in the plasma membrane, is implicated in many aspects of cellular functions. This study determined if c-Src kinase (Src)-induced Cav1 phosphorylation promotes intestinal epithelial restitution after wounding by activating Cav1-mediated Ca2+ signaling. Src directly interacted with Cav1, formed Cav1-Src complexes, and phosphorylated Cav1 in IECs. Inhi

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Geletu, Mulu, Zaid Taha, Rozanne Arulanandam, et al. "Effect of caveolin-1 on Stat3-ptyr705 levels in breast and lung carcinoma cells." Biochemistry and Cell Biology 97, no. 5 (2019): 638–46. http://dx.doi.org/10.1139/bcb-2018-0367.

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We recently demonstrated that Cav1 (caveolin-1) is a negative regulator of Stat3 (signal transducer and activator of transcription-3) activity in mouse fibroblasts and human lung carcinoma SHP77 cells. We now examined whether the cellular context may affect their levels as well as the relationship between them, by assessing Cav1 and Stat3-ptyr705 amounts in different cell lines. In MDA-MB-231, A549, and HaCat cells, Cav1 levels were high and Stat3-ptyr705 levels were low, consistent with the notion of a negative effect of endogenous Cav1 on Stat3-ptyr705 levels in these lines. In addition, man

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Godina, Christopher, Somayeh Khazaei, Mattias Belting, et al. "Abstract A006: Spatial localization of Caveolin-1 protein in triple negative breast cancer is related to different molecular features." Cancer Research 84, no. 3_Supplement_1 (2024): A006. http://dx.doi.org/10.1158/1538-7445.advbc23-a006.

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Abstract Background: Triple negative breast cancer (TNBC) is an aggressive and heterogeneous form of breast cancer with few targeted therapies and clinically used biomarkers. Caveolin-1 (CAV1) is a marker of stromal activation and vascularization. Molecular features of the tumor microenvironment (TME), important for tumor metastasis, may improve precision oncology in TNBC. CAV1 protein levels have previously been reported as a potential biomarker in breast cancer depending on their localization. Therefore, we aimed to investigate CAV1 protein levels in malignant and stromal cells of TNBC and t

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Joshi, Bharat, Michele Bastiani, Scott S. Strugnell, Cecile Boscher, Robert G. Parton, and Ivan R. Nabi. "Phosphocaveolin-1 is a mechanotransducer that induces caveola biogenesis via Egr1 transcriptional regulation." Journal of Cell Biology 199, no. 3 (2012): 425–35. http://dx.doi.org/10.1083/jcb.201207089.

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Caveolin-1 (Cav1) is an essential component of caveolae whose Src kinase-dependent phosphorylation on tyrosine 14 (Y14) is associated with regulation of focal adhesion dynamics. However, the relationship between these disparate functions remains to be elucidated. Caveola biogenesis requires expression of both Cav1 and cavin-1, but Cav1Y14 phosphorylation is dispensable. In this paper, we show that Cav1 tyrosine phosphorylation induces caveola biogenesis via actin-dependent mechanotransduction and inactivation of the Egr1 (early growth response-1) transcription factor, relieving inhibition of e

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Tang, Wenqing, Xuemei Feng, Si Zhang, et al. "Caveolin-1 Confers Resistance of Hepatoma Cells to Anoikis by Activating IGF-1 Pathway." Cellular Physiology and Biochemistry 36, no. 3 (2015): 1223–36. http://dx.doi.org/10.1159/000430292.

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Background/Aims: Anoikis resistance is a prerequisite for hepatocellular carcinoma (HCC) metastasis. The role of Caveolin-1 (CAV1) in anoikis resistance of HCC remains unclear. Methods: The oncogenic effect of CAV1 on anchor-independent growth and anoikis resistance was investigated by overexpression and knockdown of CAV1 in hepatoma cells. IGF-1 pathway and its downstream signals were detected by immunoblot analysis. Caveolae invagination and IGF-1R internalization was studied by electron microscopy and 125I-IGF1 internalization assay, respectively. The role of IGF-1R and tyrosine-14 residue

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Feldman, Rebecca, Zoran Gatalica, Sandeep K. Reddy, Michael Castro, and Jasgit C. Sachdev. "Caveolin-1: Oncogenic role in breast cancer? Clues from molecular profiling." Journal of Clinical Oncology 33, no. 28_suppl (2015): 134. http://dx.doi.org/10.1200/jco.2015.33.28_suppl.134.

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134 Background: Caveolin-1 (CAV1) is the structural component of caveolae, compartments within the plasma membrane that sequester signaling molecules, thus facilitating molecular “hot spots”. The role of CAV1 in breast cancer is an active area of investigation. We sought to understand the clinical and pathological characteristics of CAV1 positive tumors (CAV 1+) through a retrospective analysis of molecularly-profiled breast cancer patients. Methods: 2,728 breast cancer patients molecularly profiled with a commercial assay (Caris Life Sciences) were evaluated retrospectively for expression of

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Cai, Ting, Haojie Wang, Yiliang Chen, et al. "Regulation of caveolin-1 membrane trafficking by the Na/K-ATPase." Journal of Cell Biology 182, no. 6 (2008): 1153–69. http://dx.doi.org/10.1083/jcb.200712022.

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Here, we show that the Na/K-ATPase interacts with caveolin-1 (Cav1) and regulates Cav1 trafficking. Graded knockdown of Na/K-ATPase decreases the plasma membrane pool of Cav1, which results in a significant reduction in the number of caveolae on the cell surface. These effects are independent of the pumping function of Na/K-ATPase, and instead depend on interaction between Na/K-ATPase and Cav1 mediated by an N-terminal caveolin-binding motif within the ATPase α1 subunit. Moreover, knockdown of the Na/K-ATPase increases basal levels of active Src and stimulates endocytosis of Cav1 from the plas

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Avchalumov, Yosef, Alison D. Kreisler, Wulfran Trenet, et al. "Caveolin-1 Expression in the Dorsal Striatum Drives Methamphetamine Addiction-Like Behavior." International Journal of Molecular Sciences 22, no. 15 (2021): 8219. http://dx.doi.org/10.3390/ijms22158219.

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Dopamine D1 receptor (D1R) function is regulated by membrane/lipid raft-resident protein caveolin-1 (Cav1). We examined whether altered expression of Cav1 in the dorsal striatum would affect self-administration of methamphetamine, an indirect agonist at the D1Rs. A lentiviral construct expressing Cav1 (LV-Cav1) or containing a short hairpin RNA against Cav1 (LV-shCav1) was used to overexpress or knock down Cav1 expression respectively, in the dorsal striatum. Under a fixed-ratio schedule, LV-Cav1 enhanced and LV-shCav1 reduced responding for methamphetamine in an extended access paradigm compa

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Godina, Christopher, Somayeh Khazaei, Mattias Belting, et al. "High Caveolin-1 mRNA expression in triple-negative breast cancer is associated with an aggressive tumor microenvironment, chemoresistance, and poor clinical outcome." PLOS ONE 19, no. 7 (2024): e0305222. http://dx.doi.org/10.1371/journal.pone.0305222.

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Background Currently, there are few treatment-predictive and prognostic biomarkers in triple-negative breast cancer (TNBC). Caveolin-1 (CAV1) is linked to chemoresistance and several important processes involved in tumor progression and metastasis, such as epithelial-mesenchymal transition (EMT). Herein, we report that high CAV1 gene expression is an independent factor of poor prognosis in TNBC. Methods CAV1 gene expression was compared across different molecular features (e.g., PAM50 subtypes). CAV1 expression was assessed in relation to clinical outcomes using Cox regression adjusted for cli

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Zimnicka, Adriana M., Yawer S. Husain, Ayesha N. Shajahan, et al. "Src-dependent phosphorylation of caveolin-1 Tyr-14 promotes swelling and release of caveolae." Molecular Biology of the Cell 27, no. 13 (2016): 2090–106. http://dx.doi.org/10.1091/mbc.e15-11-0756.

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Caveolin 1 (Cav1) is a required structural component of caveolae, and its phosphorylation by Src is associated with an increase in caveolae-mediated endocytosis. Here we demonstrate, using quantitative live-cell 4D, TIRF, and FRET imaging, that endocytosis and trafficking of caveolae are associated with a Cav1 Tyr-14 phosphorylation-dependent conformational change, which spatially separates, or loosens, Cav1 molecules within the oligomeric caveolar coat. When tracked by TIRF and spinning-disk microscopy, cells expressing phosphomimicking Cav1 (Y14D) mutant formed vesicles that were greater in

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Al Madhoun, Ashraf, Shihab Kochumon, Dania Haddad та ін. "Adipose Tissue Caveolin-1 Upregulation in Obesity Involves TNF-α/NF-κB Mediated Signaling". Cells 12, № 7 (2023): 1019. http://dx.doi.org/10.3390/cells12071019.

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Obesity is characterized by chronic low-grade inflammation. Obese people have higher levels of caveolin-1 (CAV1), a structural and functional protein present in adipose tissues (ATs). We aimed to define the inflammatory mediators that influence CAV1 gene regulation and the associated mechanisms in obesity. Using subcutaneous AT from 27 (7 lean and 20 obese) normoglycemic individuals, in vitro human adipocyte models, and in vivo mice models, we found elevated CAV1 expression in obese AT and a positive correlation between the gene expression of CAV1, tumor necrosis factor-alpha (TNF-α), and the

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Lobos-González, Lorena, Lorena Oróstica, Natalia Díaz-Valdivia, et al. "Prostaglandin E2 Exposure Disrupts E-Cadherin/Caveolin-1-Mediated Tumor Suppression to Favor Caveolin-1-Enhanced Migration, Invasion, and Metastasis in Melanoma Models." International Journal of Molecular Sciences 24, no. 23 (2023): 16947. http://dx.doi.org/10.3390/ijms242316947.

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Caveolin-1 (CAV1) is a membrane-bound protein that suppresses tumor development yet also promotes metastasis. E-cadherin is important in CAV1-dependent tumor suppression and prevents CAV1-enhanced lung metastasis. Here, we used murine B16F10 and human A375 melanoma cells with low levels of endogenous CAV1 and E-cadherin to unravel how co-expression of E-cadherin modulates CAV1 function in vitro and in vivo in WT C57BL/6 or Rag−/− immunodeficient mice and how a pro-inflammatory environment generated by treating cells with prostaglandin E2 (PGE2) alters CAV1 function in the presence of E-cadheri

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Gairhe, Salina, Keytam S. Awad, Edward J. Dougherty, et al. "Type I interferon activation and endothelial dysfunction in caveolin-1 insufficiency-associated pulmonary arterial hypertension." Proceedings of the National Academy of Sciences 118, no. 11 (2021): e2010206118. http://dx.doi.org/10.1073/pnas.2010206118.

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Interferonopathies, interferon (IFN)-α/β therapy, and caveolin-1 (CAV1) loss-of-function have all been associated with pulmonary arterial hypertension (PAH). Here, CAV1-silenced primary human pulmonary artery endothelial cells (PAECs) were proliferative and hypermigratory, with reduced cytoskeletal stress fibers. Signal transducers and activators of transcription (STAT) and phosphoinositide 3-kinase (PI3K)/protein kinase B (AKT) were both constitutively activated in these cells, resulting in a type I IFN-biased inflammatory signature. Cav1−/− mice that spontaneously develop pulmonary hypertens

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