Chicken Hyaluronan Binding Protein 1 ELISA , HABP1
- Known as:
- Chicken Hyaluronan Binding Protein 1 Enzyme-linked immunosorbent assay test , HABP1
- Catalog number:
- E12H0035
- Category:
- -
- Supplier:
- Blue Gene Biotech
- Gene target:
- Chicken Hyaluronan Binding Protein 1 ELISA HABP1
Related genes to: Chicken Hyaluronan Binding Protein 1 ELISA , HABP1
- Gene:
- C1QBP NIH gene
- Name:
- complement C1q binding protein
- Previous symbol:
- HABP1
- Synonyms:
- gC1Q-R, gC1qR, p32, SF2p32
- Chromosome:
- 17p13.2
- Locus Type:
- gene with protein product
- Date approved:
- 1995-12-11
- Date modifiied:
- 2016-10-05
Related products to: Chicken Hyaluronan Binding Protein 1 ELISA , HABP1
Related articles to: Chicken Hyaluronan Binding Protein 1 ELISA , HABP1
- The protein p32 (C1QBP) is a multifunctional and multicompartmental homotrimer that is overexpressed in many cancer types, including colon cancer. High expression levels of C1QBP are negatively correlated with the survival of patients. Previously, we demonstrated that C1QBP is an essential promoter of migration, chemoresistance, clonogenic, and tumorigenic capacity in colon cancer cells. However, the mechanisms underlying these functions and the effects of specific C1QBP protein inhibitors remain unexplored. Here, we show that the specific pharmacological inhibition of C1QBP with the small molecule M36 significantly decreased the viability rate, clonogenic capacity, and proliferation rate of different colon cancer cell lines in a dose-dependent manner. The effects of the inhibitor of C1QBP were cytostatic and non-cytotoxic, inducing a decreased activation rate of critical pro-malignant and mitogenic cellular pathways such as Akt-mTOR and MAPK in RKO colon cancer cells. Additionally, treatment with M36 significantly affected the mitochondrial integrity and dynamics of malignant cells, indicating that p32/C1QBP plays an essential role in maintaining mitochondrial homeostasis. Altogether, our results reinforce that C1QBP is an important oncogene target and that M36 may be a promising therapeutic drug for the treatment of colon cancer. - Source: PubMed
Publication date: 2024/02/27
Egusquiza-Alvarez Carlos AlejandroMoreno-Londoño Angela PatriciaAlvarado-Ortiz EduardoRamos-Godínez María Del PilarSarabia-Sánchez Miguel AngelCastañeda-Patlán María CristinaRobles-Flores Martha - Novel CHCHD2 mutations causing C-terminal truncation and interrupted CHCHD2 protein stability in Parkinson's disease (PD) patients were previously found. However, there is limited understanding of the underlying mechanism and impact of subsequent CHCHD2 loss-of-function on PD pathogenesis. The current study further identified the crucial motif (aa125-133) responsible for diminished CHCHD2 expression and the molecular interplay within the C1QBP/CHCHD2/CHCHD10 complex to regulate mitochondrial functions. Specifically, CHCHD2 deficiency led to decreased neural cell viability and mitochondrial structural and functional impairments, paralleling the upregulation of autophagy under cellular stresses. Meanwhile, as a binding partner of CHCHD2, C1QBP was found to regulate the stability of CHCHD2 and CHCHD10 proteins to maintain the integrity of the C1QBP/CHCHD2/CHCHD10 complex. Moreover, C1QBP-silenced neural cells displayed severe cell death phenotype along with mitochondrial damage that initiated a significant mitophagy process. Taken together, the evidence obtained from our in vitro and in vivo studies emphasized the critical role of CHCHD2 in regulating mitochondria functions via coordination among CHCHD2, CHCHD10, and C1QBP, suggesting the potential mechanism by which CHCHD2 function loss takes part in the progression of neurodegenerative diseases. - Source: PubMed
Publication date: 2024/03/07
Ren Yan-LinJiang ZhengWang Jia-YiHe QinLi Si-XuGu Xiao-JingQi Yang-RanZhang MinYang Wen-JieCao BeiLi Jing-YuWang YiChen Yong-Ping - Mutations in CHCHD2 have been linked to Parkinson's disease, however, their exact pathophysiologic roles are unclear. The p32 protein has been suggested to interact with CHCHD2, however, the physiological functions of such interaction in the context of PD have not been clarified. - Source: PubMed
Publication date: 2024/02/23
Tio MurniWen RujingChoo Cai NingTan Jian BinChua AaronXiao BinSundaram Jeyapriya RajameenakshiChan Christine Hui ShanTan Eng-King - Missense mutations in the DNA binding domain of p53 are observed frequently in esophageal squamous cell carcinoma (ESCC). Recent studies have revealed the potentially oncogenic transcriptional networks regulated by mutant p53 proteins. However, majority of these studies have focused on common "hotspot" p53 mutations while rarer mutations are poorly characterized. In this study, we report the characterization of rare, "non-hotspot" p53 mutations from ESCC. In vitro tumorigenic assays performed following ectopic-expression of certain "non-hotspot" mutant p53 proteins caused enhancement of oncogenic properties in squamous carcinoma cell lines. Genome-wide transcript profiling of ESCC tumor samples stratified for p53 status, revealed several genes exhibiting elevated transcript levels in tumors harboring mutant p53. Of these, ARF6, C1QBP, and TRIM23 were studied further. Reverse transcription-quantitative PCR (RT-qPCR) performed on RNA isolated from ESCC tumors revealed significant correlation of TP53 transcript levels with those of the three target genes. Ectopic expression of wild-type and several mutant p53 forms followed by RT-qPCR, chromatin affinity-purification (ChAP), and promoter-luciferase assays indicated the exclusive recruitment of p53 mutants-P190T and P278L, to the target genes leading to the activation of expression. Several functional assays following knockdown of the target genes revealed a significant suppression of tumorigenicity in squamous carcinoma cell lines. Rescue experiments confirmed the specificity of the knockdown. The tumorigenic effects of the genes were confirmed in nude mice xenograft assays. This study has therefore identified novel oncogenic targets of "non-hotspot" mutant p53 proteins relevant for ESCC besides validating the functional heterogeneity of the spectrum of tumor-specific p53 mutations. - Source: PubMed
Publication date: 2024/02/15
George Sara AKotapalli ViswakalyanRamaswamy PandillaKumar RajuGowrishankar SwarnalataUppin Shantveer GBashyam Murali D - Four undescribed compounds including one aromatic glucoside derivative, cordyceglycoside A (1), one new isoleucine derivative inner salt, cordycepisosalt A (2), a rare four-membered lactam, cinerealactam B (3), and one sesquiterpene derivative, cordycepsetp A (4), together with six known compounds were isolated from Cordyceps militaris. The structures including absolute configurations of these new compounds, were unambiguously elucidated by spectroscopic data analysis and single crystal X-ray diffraction. Biological evaluation of compounds 1-4 showed that 3 displays anti-renal fibrotic activities in TGF-β1 induced NRK-52e cells. Furthermore, DARTS coupled with LC-MS/MS analysis was used to identify candidate target proteins for 3. Subsequently, C1qbp knockdown using siRNA allowed us to validate the target protein of 3. - Source: PubMed
Publication date: 2024/02/03
Yang WeiZhu Kun-FangTao Cheng-TianYan Yong-MingCheng Yong-Xian