GIPC3 antibody
- Known as:
- GIPC3 (anti-)
- Catalog number:
- orb41409
- Product Quantity:
- EUR
- Category:
- -
- Supplier:
- Biorbyt biorb
- Gene target:
- GIPC3 antibody
Related genes to: GIPC3 antibody
- Gene:
- GIPC3 NIH gene
- Name:
- GIPC PDZ domain containing family member 3
- Previous symbol:
- C19orf64, DFNB72, DFNB15
- Synonyms:
- DFNB95
- Chromosome:
- 19p13.3
- Locus Type:
- gene with protein product
- Date approved:
- 2005-06-28
- Date modifiied:
- 2015-11-18
Related products to: GIPC3 antibody
Related articles to: GIPC3 antibody
- Sensorineural hearing loss (SNHL) has a high degree of genetic heterogeneity, with numerous mutated genes that contribute to deafness. GIPC3 gene is one of the mutated genes that can cause congenital hearing loss, which has been identified in recent years; however, the exact mechanism behind this condition remains unclear. Mitophagy is the process of selectively encapsulating and lysing damaged or dysfunctional mitochondria in order to prevent the accumulation of damaged mitochondria from damaging the cells and is of great importance in the maintenance of homeostasis in the inner ear. This paper aims to investigate the potential mechanism of sensorineural hearing loss brought on by Gipc3 mutations by observing the impact of Gipc3 expression on mitochondrial metabolism and autophagy in inner ear hair cells. In this study, The House Ear Institute Organ of Corti 1(HEI-OC1) cells and cochlear explants were cultured to change the expression level of Gipc3 by transfection, and the knockdown efficiency was examined by quantitative polymerase chain reaction (qPCR) and Western blot. Knockdown of Gipc3 inhibited cell viability and its proliferation ability. When tert-butyl hydroperoxide (t-BHP) was used to induce oxidative stress injury and knockdown of Gipc3, inner ear hair cells had a weakened ability to resist oxidative stress injury, mitochondrial metabolism was altered, and there was an accumulation of reactive oxygen species (ROS) and a reduction of mitochondrial membrane potential. Immunofluorescence and Western blot techniques demonstrated autophagy abnormalities in the mitophagy-related proteins LC3B and p62. Early endosome-dependent mitophagy is mediated by a PH domain and leucine zipper motif 1 (APPL1), and mitophagy is hampered by APPL1 deletion. We discovered that there is probably co-localization between Gipc3 and APPL1 by confocal microscopy imaging and that their trends show a positive association. In summary, Gipc3 mutations may lead to decreased mitochondrial function by inhibiting the APPL1-mediated mitophagy process. This may lead to a reduction in oxidative metabolism in hair cells, which is one potential mechanism via which Gipc3 mutations suppress mitophagy. - Source: PubMed
Publication date: 2025/07/14
Li XinxinWang JingShi LinWang Liang - Lung Squamous Cell Carcinoma (LUSC), a major subtype of non-small cell lung cancer, presents significant treatment challenges due to limited targeted therapy options. This study aims to identify novel therapeutic targets to improve therapeutic strategies for LUSC. - Source: PubMed
Chen YoupengLi EnzhongChang ZhenglinXie YifeiChen XiaoyiSun JunquanLai XuntaoCheng Zhangkai JSun Baoqing - Morphological mouse phenotyping plays a pivotal role in the translational setting and even more in the area of auditory research, where mouse is a central model organism due to the evolutionary genetic relationship and morpho-functional analogies with the human auditory system. However, some results obtained in murine models cannot be translated to humans due to the inadequate description of experimental conditions underlying poor reproducibility. We approach the characterization of the aging process of the mouse cochlea in animals up to 18 months of age belonging to two of the most used outbred (CD1) and inbred (C57BL/6N) strains. Striving to reduce any environmental variable we performed our study compliantly to the ARRIVE guidelines. We integrated instrumental data (auditory brainstem response test), with morphological analyses to correlate functional discrepancies to morphological changes and track the differences in the evolution of sensorineural hearing loss in the two strains. We featured the localization of Gipc3, Myosin VIIa, and TMC1 in hair cells of the Corti organ as well as NF 200 and the density of type I neuron in the spiral ganglion. We outlined age-related hearing loss (ARHL) in both strains, and a clear drop in the selected marker localization. However, in CD1 we detected a different trend allowing the identification of potential strain-specific mechanisms, namely an increase in myosin VIIa in 6 months aging mice in comparison to 2 months old animals. Our findings represent an asset to investigate the strain-dependent physiological trigger of ARHL providing new insights in the translational area. - Source: PubMed
Publication date: 2024/10/31
Attanasio ChiaraPalladino AntonioGiaquinto DanielaScavizzi FerdinandoRaspa MarcelloPeres ChiaraAnastasio CamillaScocco PaolaLucini Carlade Girolamo PaoloD'Angelo LiviaDe Felice Elena - GIPC3 has been implicated in auditory function. Here, we establish that GIPC3 is initially localized to the cytoplasm of inner and outer hair cells of the cochlea and then is increasingly concentrated in cuticular plates and at cell junctions during postnatal development. Early postnatal Gipc3KO/KO mice had mostly normal mechanotransduction currents, but had no auditory brainstem response at 1 month of age. Cuticular plates of Gipc3KO/KO hair cells did not flatten during development as did those of controls; moreover, hair bundles were squeezed along the cochlear axis in mutant hair cells. Junctions between inner hair cells and adjacent inner phalangeal cells were also severely disrupted in Gipc3KO/KO cochleas. GIPC3 bound directly to MYO6, and the loss of MYO6 led to altered distribution of GIPC3. Immunoaffinity purification of GIPC3 from chicken inner ear extracts identified co-precipitating proteins associated with adherens junctions, intermediate filament networks and the cuticular plate. Several of immunoprecipitated proteins contained GIPC family consensus PDZ-binding motifs (PBMs), including MYO18A, which bound directly to the PDZ domain of GIPC3. We propose that GIPC3 and MYO6 couple to PBMs of cytoskeletal and cell junction proteins to shape the cuticular plate. - Source: PubMed
Publication date: 2023/05/25
Chatterjee ParomaMorgan Clive PKrey Jocelyn FBenson ConnorGoldsmith JenniferBateschell MichaelRicci Anthony JBarr-Gillespie Peter G - GIPC3 has been implicated in auditory function. Initially localized to the cytoplasm of inner and outer hair cells of the cochlea, GIPC3 increasingly concentrated in cuticular plates and at cell junctions during postnatal development. Early postnatal mice had mostly normal mechanotransduction currents, but had no auditory brainstem response at one month of age. Cuticular plates of hair cells did not flatten during development as did those of controls; moreover, hair bundles were squeezed along the cochlear axis in mutant hair cells. Junctions between inner hair cells and adjacent inner phalangeal cells were also severely disrupted in cochleas. GIPC3 bound directly to MYO6, and the loss of MYO6 led to altered distribution of GIPC3. Immunoaffinity purification of GIPC3 from chicken inner ear extracts identified co-precipitating proteins associated with adherens junctions, intermediate filament networks, and the cuticular plate. Several of immunoprecipitated proteins contained GIPC-family consensus PDZ binding motifs (PBMs), including MYO18A, which binds directly to the PDZ domain of GIPC3. We propose that GIPC3 and MYO6 couple to PBMs of cytoskeletal and cell-junction proteins to shape the cuticular plate. - Source: PubMed
Publication date: 2023/03/01
Chatterjee ParomaMorgan Clive PKrey Jocelyn FBenson ConnorGoldsmith JenniferBateschell MichaelRicci Anthony JBarr-Gillespie Peter G