Ask about this productRelated genes to: Klhl12 antibody
- Gene:
- KLHL12 NIH gene
- Name:
- kelch like family member 12
- Previous symbol:
- -
- Synonyms:
- C3IP1
- Chromosome:
- 1q32.1
- Locus Type:
- gene with protein product
- Date approved:
- 2004-02-13
- Date modifiied:
- 2015-11-18
Related products to: Klhl12 antibody
Related articles to: Klhl12 antibody
- Pericyte to myofibroblast transformation is a key driver of renal fibrosis following acute kidney injury (AKI). Exosomes, miRNAs, and bone mesenchymal stem cells (BMSCs) are important in alleviating AKI renal fibrosis. We proposed to explore the role of engineering exosomes rich in miR-145-5p and correlated with KLHL12/KHSRP in AKI-induced pericytes-mediated fibrosis in the present study. Rat perirenal cells were isolated and cultured. Engineering exosomes rich in miR-145-5p derived from BMSCs were obtained through cell transfection technology. AKI rat model and Hypoxia/Reoxygenation (HR) induced perirenal cells injury model were established. Dual luciferase reporter gene, MeRIP, and Co-immunoprecipitation were performed to validate miR-145-5p targeting KLHL12 and its downstream molecules including KHSRP and FLI-1. Renal function, apoptosis and pyroptosis, fibrosis-related proteins were detected through biochemistry, immunohistochemistry, immunofluorescence, and transmission electron microscopy to explore the functional role of the miR-145-5p/ KLHL12/KHSRP/FLI-1 axis in cellular and animal models. According to our findings, pericyte-myoblast transformation contributed to AKI-induced fibrosis in vivo and HR-induced fibrosis along with apoptosis and pyroptosis in vitro. MiR-145-5p down-regulated KLHL12 expression by targeting its 3'UTR to improve perirenal cells-mediated fibrosis. KLHL12 might downregulate KHSRP to increase FLI-1 expression by promoting FLI-1 mRNA stability in AKI-induced fibrosis mediated by perirenal cells. These findings indicate that miR-145-5p enriched in BMSC derived engineered exosomes may suppress KLHL12 expression to up-regulate KHSRP and then down-regulate FLI-1 by m6A to attenuate perirenal cells-mediated fibrosis. - Source: PubMed
Publication date: 2026/04/20
Zeng FanzhouGou WeiFu XueziDing LinglingShao QingZhu ChanghaoLiu YutingCheng JinYang BoLiu Nanmei - Primary biliary cholangitis (PBC), is a chronic autoimmune liver disease, characterized by cholangiopathy, cholestasis and in the long-term fibrosis, biliary cirrhosis and ultimately end-stage liver disease unless liver transplantation is applied. The diagnostics of PBC is based on biochemical tests, autoantibody measurements and liver histopathology. Abdominal ultrasound, later magnetic resonance cholangiopancreatography (MRCP) or endoscopic ultrasound can be effective methods for imaging the intra- and extrahepatic bile ducts. Concerning autoantibodies, anti-mitochondrial (AMA) and PBC-specific antinuclear antibodies (ANA) are the front-line tests that can be identified by indirect immunofluorescence tests or solid-phase immunoassays. AMA and especially the AMA-M2 variant have a high sensitivity and specificity for PBC, while anti-gp210 and anti-sp100 (PBC-specific ANAs) have a lower sensitivity but very high specificity for the disease. Anti-centromere antibodies (ACA) can help in the diagnostics of PBC and some overlap syndromes. Novel emerging markers - anti-hexokinase 1 and anti-Kelch-like 12 protein (anti-KLHL12) - can help the identification of rare AMA- and ANA-negative PBC cases. There is cumulating evidence that beside diagnostics certain autoantibodies can provide information about the prognostics of PBC, can predict therapy response, furthermore, can act as activity marker in follow-up of the patients during therapy. We summarize here the most important data about the accepted and potential clinical applications of traditional and emerging new autoantibodies in PBC. - Source: PubMed
Publication date: 2026/03/19
Antal-Szalmás PéterBencze DóraDemeter SaroltaPénzes-Daku KrisztinaSzabó LillaTóth BeátaFöldesi RózaPapp MáriaNagy Gábor - Targeted protein degradation can be induced by recruiting a protein of interest to an E3 ligase, resulting in its ubiquitination and subsequent proteasome-mediated degradation. However, only a small number of E3 ligases have been utilized for degradation. Expansion of the repertoire of useful E3 ligases via the identification of ligands to those ligases could broaden the scope and applicability of the degradation paradigm. We have identified KLHL12 as an E3 ligase with higher expression in cancer over normal tissues. We report here the use of NMR-based screening to identify fragments that bind to KLHL12, and X-ray structures of a fragment hit bound to KLHL12. Using this structural information, we optimized the hits, leading to the first reported small molecules that bind to KLHL12 with submicromolar affinity. Derivatives of these compounds may be useful for the construction of PROTACs to selectively degrade protein targets in tumors while sparing normal cells. - Source: PubMed
Publication date: 2026/03/29
Waterson Alex GVadukoot AnishJana SomnathCui JianwenLuong KelvinRietz Tyson AMadrigal-Carrillo Ezequiel AlejandroLehmann Brian DSensintaffar John LZhao BinAmporndanai KangsaPetros Zoe AScaggs William RushChacon Simon SelenaVekariya Rakesh HKim KwanghoThangaraj ManikandanChristov Plamen PSouth Taylor MSai JiqingThiruvaipati AnushaSchmidt Charles REells RebeccaMoore William JOlejniczak Edward TPhan JasonFesik Stephen W - Interactions between peptides based on a region in the zinc finger translocation associated (ZFTA) protein and the Kelch domain of Kelch-like protein 20 (KLHL20) have been characterised by biosensor analysis, supported by AlphaFold2-based structure predictions of peptides bound to the protein. Residues critical for the interaction were identified. The analysis showed that all peptides exhibited relatively weak and complex interactions with KLHL20. The original ZFTA peptide had a much higher affinity for KLHL20 than for the Kelch domain of KLHL12 (KLHL12), indicating a specificity for KLHL20. The estimated K of 35 µM was like that for a 21-mer peptide derived from death-associated protein kinase 1, a known KLHL20 substrate. Removal of flexible C-terminal residues generated a 12-mer, predicted to form a stable helix. This reduced the affinity 100-fold. Removal of N-terminal residues resulted in a 10-mer predicted to be flexible, which had a similar affinity as the original 16-mer. The similar affinities for peptides representing different regions of ZFTA suggest that the recognition is feature specific rather than sequence specific. The interaction mechanism reflects "fuzzy binding", consistent with the role of KLHL20 as an adaptor protein in the ubiquitination of disordered protein substrates by Cullin-3 E3 ubiquitin ligase. - Source: PubMed
Myers Nadine E MWhittaker JoannaCadot Marie Elodie HélèneVarga Julia KDiallo MarcelNilsson JakobBach AndersSandström AnjaSchueler-Furman OraDanielson U Helena - Lymphoid cancers of different types and subtypes are known to cluster in families. We hypothesize that there are shared susceptibility factors in families with these heterogenous lymphoid malignancies. Exome sequencing was performed on 100 individuals from 43 lymphoid cancer pedigrees. Variants from 37 families were ranked using the eights-based vriant anking in edigrees (WARP) pipeline. Six affected unrelated probands were used for interpretation only. We detected recurrent variants in the germline lymphoid cancer gene in 4 (9%) of the 43 families, and variants in other genes involved in lymphoid cancers: and . Variants in genes including and involved in the WNT/β-catenin pathway were identified, representing a novel observation. Some variants appeared to segregate with specific types of lymphoid cancers; others were shared across different subtypes. Identifying factors predisposing to different types of lymphoid cancers will help understand the etiology of these neoplasms. - Source: PubMed
Publication date: 2026/02/07
Ralli SnehaJones Samantha JeanLeach StephenLynch Henry JBrooks-Wilson Angela R