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The protein encoded by PANX1 belongs to the innexin family.
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Extracellular ATP hydrolysis via NTPDase1 (show ENTPD1 Antibodies) action inhibits synaptic transmission by pannexin 1-mediated increase in pH buffering of the synaptic cleft.
The existence of two Panx1 proteins in zebrafish displaying distinct tissue distribution, protein modification and electrophysiological properties, suggests that both proteins fulfill different functions in vivo.
The function of panx1 channel is significantly reduced following mutation of a single cysteine residue (C282W) in the fourth transmembrane region of panx1.
Pannexin1 (Panx1) was suggested to be functionally associated with purinergic P2X and N-methyl-D-aspartate (NMDA) receptor channels. Activation of these receptor channels by their endogenous ligands leads to cross-activation of Panx1 channels. This in turn potentiates P2X and NMDA receptor channel signaling.
The ubiquitous expression, as well as its function as a major ATP release and nucleotide permeation channel, makes Panx1 a primary candidate for participating in the pathophysiology of CNS disorders.
Panx1 was mainly distributed in microcolumn neurons, dysmorphic neurons, balloon cells and reactive astrocytes in cortical lesions from intractable epilepsy patients with focal cortical dysplasia.
ATP release from red blood cells is not mediated by the cAMP-mediated Panx1 pathway.
Panx1 channels are involved in beta-toxin-induced cell death.
Pannexin1 is a mediator of inflammation and cell death. (Review)
Panx1 channels promote skeletal muscle myoblast differentiation and fusion. (Review)
presence of the Panx1-400C allele was not associated with platelet reactivity in stable cardiovascular patients.
Overactive Panx-1 promotes cancer cell survival in the context of mechanical deformation. Panx-1 inhibitors can be used to treat highly metastatic cancer. Mechanosensitive Panx-1 channels will be a new target for the prevention of metastasis and stress-induced diseases.
The results of this study do not support a major contribution of PANX1-3 to disease risk of schizophrenia according to DSM-5.
These novel findings reveal unique roles for GFAP (show GFAP Antibodies)-positive glial and neuronal Panx1 and describe new chronic pain targets for cell-type specific intervention in this often intractable disease.
Panx-1 modulation may be interesting to amplify the clinical effect of cisplatin (DDP (show TIMM8A Antibodies)) and reverse the resistance of testicular cancer cells to DDP (show TIMM8A Antibodies).
Pannexin1 may play a role in the pathogenesis of liver disease.
Findings indicate a deleterious role for membrane channel Pannexin 1 (Panx1) in response to permanent permanent middle cerebral artery (MCA (show RSPH1 Antibodies)) occlusion, that is unique to females.
blocking Panx1 and/or Casp4 (show CASP4 Antibodies) activities is a beneficial strategy to enhance donor cell engraftment and LG regeneration through the reduction of inflammation.
found a significant increase in waking and a correspondent decrease in slow wave sleep percentages in the Panx1-/- animals.
Diabetic C57BL/6J-Ins2Akita mice were used to evaluate in vivo effects of high glucose on P2R and Panx1
Pharmacological blockade or genetic deletion of Panx1 channels inhibits CD4 (show CD4 Antibodies)+ T lymphocyte polarization and migration induced by the chemokine (show CCL1 Antibodies) SDF-1alpha/CXCL12 (show CXCL12 Antibodies). Panx1 deficiency delayed experimental autoimmune encephalomyelitis symptoms because of the decreased infiltration of CD4 (show CD4 Antibodies)+ T lymphocytes into the CNS.
data suggest that Panx1 and Panx3 (show PANX3 Antibodies) are not essential for baseline hearing in mice tested, but the therapeutic targeting of Panx3 (show PANX3 Antibodies) may prove protective against mid-high-frequency hearing loss caused by loud NE.
The protein encoded by this gene belongs to the innexin family. Innexin family members are the structural components of gap junctions. This protein and pannexin 2 are abundantly expressed in central nerve system (CNS) and are coexpressed in various neuronal populations. Studies in Xenopus oocytes suggest that this protein alone and in combination with pannexin 2 may form cell type-specific gap junctions with distinct properties.