Ask about this productRelated genes to: ACTA1 Blocking Peptide
- Gene:
- ACTA1 NIH gene
- Name:
- actin alpha 1, skeletal muscle
- Previous symbol:
- ACTA
- Synonyms:
- NEM3
- Chromosome:
- 1q42.13
- Locus Type:
- gene with protein product
- Date approved:
- 1986-01-01
- Date modifiied:
- 2019-04-23
Related products to: ACTA1 Blocking Peptide
Related articles to: ACTA1 Blocking Peptide
- Kampung Unggul Balitbangtan (KUB) chicken is a superior Indonesian native breed with high adaptability, good growth potential, and desirable meat quality. Nutritional strategies such as multienzyme supplementation are increasingly applied to improve productivity and meat quality without altering basal diet composition. This study investigated the effects of dietary multienzyme supplementation, consisting of phytase and protease, on growth performance, carcass characteristics, organ development, meat quality, and muscle-related gene expression in KUB chickens. Sixteen one-day-old male KUB chicks were randomly allocated to four dietary treatments: a control diet without multienzymes and three diets supplemented with phytase (200 mg/kg) combined with protease at 300, 500, or 700 mg/kg of feed. Growth performance parameters were measured up to 45 days of age, followed by carcass evaluation, organ weight analysis, meat quality assessment, and transcriptomic and quantitative real-time PCR analyses of breast muscle tissue. Multienzyme supplementation significantly improved final body weight and feed conversion ratio, particularly during the finisher phase, while reducing feed intake at higher enzyme inclusion levels. Carcass percentage and breast weight were enhanced in multienzyme-treated groups, accompanied by favorable changes in digestive and immune organ development. Meat quality analysis showed increased water-holding capacity, reduced cooking loss, and improved color characteristics, notably higher redness and lower yellowness values. Transcriptomic profiling and gene expression analysis revealed significant modulation of key muscle growth-related genes, including ACTA1, MYBPC1, TGFβ2, IGF2, and MYH9, indicating adaptive transcriptional responses associated with improved nutrient utilization rather than direct structural muscle alterations. In conclusion, dietary supplementation with a combination of phytase and protease effectively enhances growth performance, feed efficiency, carcass traits, and meat quality in KUB chickens while modulating growth-related gene expression. Multienzyme inclusion represents a promising and cost-effective nutritional strategy for improving productivity and meat quality in native chicken production systems. - Source: PubMed
Publication date: 2026/04/15
Ayuti Siti RaniLamid MirniWarsito Sunaryo HadiArif Mohammad Anam AlKim Eun JoongShin SangsuHamid Iwan SahrialMafruchati MaslichahAkmal MuslimKhairullah Aswin Rafif - Facioscapulohumeral muscular dystrophy (FSHD) is an autosomal dominant muscular disease in which genetic mutations activate DUX4 expression in skeletal muscle. Currently, there are no approved therapies for FSHD. We developed Delpacibart braxlosiran (del-brax, also known as AOC 1020), an antibody oligonucleotide conjugate (AOC), for the treatment of FSHD that is designed to specifically target and reduce DUX4 mRNA in skeletal muscle. AOC 1020 is composed of DUX4 mRNA-targeting small interfering RNA (siRNA), siDUX4.6, conjugated to a human transferrin receptor 1 (TfR1)-targeting monoclonal antibody to facilitate productive siRNA delivery to muscle. We demonstrate that siDUX4.6 reduces DUX4-regulated gene expression in FSHD patient-derived myotubes in vitro and in skeletal muscle of the ACTA1-MCM; FLExDUX4 FSHD mouse model in vivo. Single systemic intravenous treatment was sufficient to prevent DUX4-induced muscle weakness and fibrosis in this FSHD mouse model and reduce DUX4-regulated genes by ∼75% 8 weeks post-dose. The pharmacokinetic profiles of AOCs with siDUX4.6 were comparable in murine and non-human primate muscle. These data demonstrate the potential of AOC 1020 to treat the underlying cause of FSHD by suppressing DUX4 expression in muscles of patients with FSHD. The safety and efficacy of AOC 1020 is currently being investigated in clinical trials. - Source: PubMed
Malecova BarboraSala DavidMelikian Garineh MJohns RachelErdogan GulinHartmann MarcJordan MaryamArias Joel DannyBhattacharya ArvindMeng QingyingDansereau OliverBeppler Samuel WDoppalapudi Venkata RHuang HanhuaFlanagan William MichaelLevin Arthur A - AllergoOncology has emerged as an interdisciplinary field exploring the interaction between allergic diseases and cancer; however, the lack of stable in vivo models has limited mechanistic investigations. This study aimed to establish an experimental animal model to explore the impact of systemic allergic responses on tumor progression and to provide preliminary insights into the regulatory role of allergy in cancer development. - Source: PubMed
Publication date: 2026/04/08
Fan XiaoyuGuo ShushuZhang WenchaoXu ZeaoSun SimanLi YanHe JiumingJin Hongtao - Angiotensin II (AngII) induces cardiac hypertrophy but the exact mechanism is not known. The present study investigates the role of the interleukin-1 receptor-associated kinase (IRAK), in AngII-induced cardiac inflammation, fibrosis and hypertrophy. - Source: PubMed
Publication date: 2026/03/22
Jaiswal ShreyaSharma GauravBarthwal Manoj Kumar - Spinocerebellar ataxia type 1 is a neurodegenerative disease characterized by motor dysfunction and premature death usually from compromised swallowing and respiration. Using plethysmography, we characterized respiration in the conditional f-ATXN1 SCA1 model. We found a progressive elevation of baseline respiration that impairs ability of f-ATXN1 mice to increase breathing during challenge. To delineate regions contributing to respiratory dysfunction, f-ATXN1 mice were crossed with Nestin-Cre and Acta1-Cre mice, respectively. Respiration improved by removing mATXN1 from neural lineages, but not from skeletal muscle demonstrating mATXN1 in the central nervous system is a key driver of respiratory dysfunction in SCA1 mouse models. Moreover, respiratory dysfunction in SCA1 mice involves two aspects: behavioral dysregulation exhibited as increased movement during plethysmography, and functional dysregulation of respiratory circuitry. As both of these aspects are rescued by deleting mATXN1 from neural cells, we further investigated the role of cerebellar Purkinje cells and chemosensing neurons in the brain stem in SCA1 respiratory phenotype. Our results indicate complex multiregional etiology of respiratory dysfunction. Mechanistically we found that in contrast to most other SCA1 symptoms, nuclear localization of mATXN1 does not play a key role in respiratory dysfunction. - Source: PubMed
Publication date: 2026/03/17
Soles AlyssaGrittner JessicaDouglas KaiaYang PraseuthDuvick LisaO'Callaghan BrennonBarnett RyanChau ChristineCosiquien RojRainwater OrionSerres ShannahDougherty BrendanOrr Harry TCvetanovic Marija