KBTBD10 Blocking Peptide
- Known as:
- KBTBD10 Blocking Peptide
- Catalog number:
- 33r-5874
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Fitzgerald industries international
- Gene target:
- KBTBD10 Blocking Peptide
Related genes to: KBTBD10 Blocking Peptide
- Gene:
- KLHL41 NIH gene
- Name:
- kelch like family member 41
- Previous symbol:
- KBTBD10
- Synonyms:
- SARCOSIN, Krp1
- Chromosome:
- 2q31.1
- Locus Type:
- gene with protein product
- Date approved:
- 2004-01-15
- Date modifiied:
- 2015-11-18
Related products to: KBTBD10 Blocking Peptide
Related articles to: KBTBD10 Blocking Peptide
- Metabolic dysfunction-associated steatotic liver disease (MASLD) is increasing in both prevalence and severity, highlighting the need for non-invasive biomarkers to assess disease activity. Extracellular vesicles (EVs), which carry molecular cargo from their cells of origin, hold promise as accessible biomarkers. We performed proteomic profiling of plasma-derived EVs from 70 patients with MASLD to identify protein signatures associated with key histological features (steatosis, metabolic dysfunction-associated steatohepatitis (MASH), and fibrosis). These proteins were subsequently correlated with magnetic resonance (MR)-based liver imaging. Plasma EV protein profile differed between mild (S1) and advanced steatosis (S3). H4C1, OIT3, and ANPEP were elevated in S3, while CCDC25 and KLHL41 were decreased (|log fold change| > 1, < 0.05). KLHL41 had a weak-to-moderate correlation with proton density fat fraction (PDFF) (R = -0.34, = 0.016). GP1BA was upregulated in MASH (log fold change = 1.13, = 0.03) but showed weak correlation with cT1, an imaging parameter for steatohepatitis (R = 0.22, = 0.173). In fibrosis, complement component 7 (C7) was elevated in advanced (≥F3) vs. mild fibrosis (Publication date: 2025/11/14
Li YakunSon Koen C vanSerna-Salas SandraWolters Justina CWassenaar Nienke P MDriessen StanMak Anne LindeDijk Anne-Marieke vanHouttu Veera A TWitjes Julia JZwirs DionaDoukas MichailVerheij JoanneDullaart Robin P FBlokzijl HansHolleboom Adriaan GMoshage Han - Beta-adrenergic agonists are widely used for bronchial relief in respiratory conditions such as asthma and exercise-induced bronchoconstriction. However, this drug class has also been shown to have muscle anabolic properties. Kelch-Like Family Member 41 (KLHL41) is a sarcomeric protein implicated in muscle remodeling and hypertrophy. In this study, we examined the effects of oral clenbuterol, therapeutic inhaled formoterol, and resistance training on KLHL41 protein abundance in human skeletal muscle. KLHL41 levels were measured by immunoblotting in vastus lateralis muscle biopsies from healthy adults following 2 weeks of oral clenbuterol administration, 6 weeks of inhaled formoterol at therapeutic doses, or 8 weeks of resistance training. We also assessed sex differences and the effects of acute versus prolonged interventions. Prolonged oral clenbuterol administration significantly increased KLHL41 abundance compared to placebo (p < 0.001), with a magnitude similar to that observed after resistance training (p < 0.01), whereas therapeutic inhaled formoterol had no effect on KLHL41 levels. Neither acute clenbuterol administration nor a single resistance training session altered KLHL41 abundance, and no sex differences were observed in baseline KLHL41 levels. These findings indicate that beta-adrenergic stimulation via oral clenbuterol, but not therapeutic inhalation of formoterol, promotes sarcomeric remodeling through KLHL41-related pathways similar to those activated by resistance training. The distinct effects of these agents on KLHL41 support current anti-doping regulations prohibiting clenbuterol use and highlight KLHL41 as a potential molecular marker of skeletal muscle adaptation to hypertrophic stimuli. - Source: PubMed
Publication date: 2025/11/04
Hostrup MortenMoesgaard LukasThomassen MartinDeshmukh AtulJessen Søren - Amyotrophic lateral sclerosis (ALS) is a fatal neurodegenerative disorder with a largely unknown duration and pathophysiology of the pre-diagnostic phase, especially for the common non-monogenic form. - Source: PubMed
Publication date: 2025/09/01
Homann JanKorologou-Linden RoxannaViallon VivianMorgan SarahDobricic ValerijaDeecke LauraSchessner Julia PSmith-Byrne KarlBirtles DanielZhao YujiaWuu JoanneArtaud FannyHajizadah FatemaHuerta Jose MariaOhlei OlenaLebedev MikhailKolijn P MartijnGuevara MarcelaJimenez-Zabala AnaSánchez María JoséTrobajo-Sanmartín CaminoColorado-Yohar Sandra MAlonso-Martín SoniaPetrova DafinaSieri SabinaBerger KlausPeters SusanWareham NickKaaks RudolphTravis Ruth CVermeulen Roel C H Tzoulaki IoannaElbaz AlexisMann MatthiasSacerdote CarlottaMasala GiovannaKatzke VerenaBenatar MichaelBertram LarsMiddleton LefkosRiboli ElioGunter Marc JFerrari PietroRobinson OliverLill Christina M - Amyotrophic lateral sclerosis (ALS) is a fatal neurodegenerative disorder with a largely unknown duration and pathophysiology of the pre-diagnostic phase, especially for the common non-monogenic form. - Source: PubMed
Publication date: 2025/08/28
Homann JanKorologou-Linden RoxannaViallon VivianMorgan SarahDobricic ValerijaDeecke LauraSchessner Julia PSmith-Byrne KarlBirtles DanielZhao YujiaWuu JoanneArtaud FannyHajizadah FatemaHuerta Jose MariaOhlei OlenaLebedev MikhailKolijn P MartijnGuevara MarcelaJimenez-Zabala AnaSánchez María JoséTrobajo-Sanmartín CaminoColorado-Yohar Sandra MAlonso-Martín SoniaPetrova DafinaSieri SabinaBerger KlausPeters SusanWareham NickKaaks RudolphTravis Ruth CVermeulen Roel C H Tzoulaki IoannaElbaz AlexisMann MatthiasSacerdote CarlottaMasala GiovannaKatzke VerenaBenatar MichaelBertram LarsMiddleton LefkosRiboli ElioGunter Marc JFerrari PietroRobinson OliverLill Christina M - Sarcomere assembly and growth are fundamental processes essential for the development, function, and repair of skeletal muscle. However, the mechanisms underlying sarcomere formation and assembly , which are critical for the formation of functional myofibers in vertebrates, remain poorly understood. Defects in sarcomeres contribute to muscle dysfunction in numerous genetic and acquired myopathies, yet the lack of a clear understanding of specific sarcomeric defects has hindered the development of effective therapies. Nemaline myopathy (NM) is caused by mutations in genes that primarily affect sarcomere structure and function. The disease is clinically heterogeneous, with the congenital form being the most severe. Using zebrafish models of congenital forms of NM, we investigated sarcomere assembly in during skeletal muscle development to identify key steps contributing to myofibril formation and muscle growth under both normal and disease conditions. Our findings demonstrate that the gene encoding the sarcomeric protein KLHL41 plays a critical role in the formation and directional organization of new sarcomeres within developing myofibrils, facilitating both radial and longitudinal muscle growth. Dysregulation of sarcomeric proteins and impaired protein turnover in the KLHL41-NM zebrafish model resulted in the development of sarcomeric defects. Moreover, we show that the interaction between the KLHL41-troponin complex is essential for muscle growth and cross-bridge regulation in developing muscle. These studies address a significant gap in the understanding of sarcomeric defects in myopathies and will help guide the development of targeted therapies aimed at rescuing these processes. - Source: PubMed
Publication date: 2025/06/01
Han HyewonShi JanetBongiorno Alfredo HMansur ArianWidrick JeffreyTate GraceGill SehajpreetKarimi EsmatGranzier HenkMoore Jeffrey RGupta Vandana A