PHKB Antibody (OASA09376)
- Known as:
- PHKB Antibody (OASA09376)
- Catalog number:
- oasa09376
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Aviva Systems Biology
- Gene target:
- PHKB Antibody (OASA09376)
Related genes to: PHKB Antibody (OASA09376)
- Gene:
- PHKB NIH gene
- Name:
- phosphorylase kinase regulatory subunit beta
- Previous symbol:
- -
- Synonyms:
- -
- Chromosome:
- 16q12.1
- Locus Type:
- gene with protein product
- Date approved:
- 1989-02-23
- Date modifiied:
- 2016-10-05
Related products to: PHKB Antibody (OASA09376)
Related articles to: PHKB Antibody (OASA09376)
- Muscle fibers exhibit high plasticity: both the fast-twitch fiber type and slow-twitch fiber type can mutually transform under the regulation of phosphorylation. In this study, we characterized the muscle fiber profiles and phosphoproteomes of the (EDL) and (SOL) in slow-growing Xueshan chickens and fast-growing Ross 308 broilers. Fiber-type distribution was quantified by immunohistochemistry and RT-qPCR of , and . TMT-based phosphoproteomics, combined with bioinformatic analysis, was used to identify differentially expressed phosphopeptides (DEPs) in two comparisons: Ross 308 SOL vs. Ross 308 EDL, and Xueshan EDL vs. Ross 308 EDL. The proportion of type I (slow-twitch) fibers in EDL was significantly higher in Xueshan chickens than in Ross 308 broilers (15.53% vs. 6.14%, < 0.05), with no significant differences in fiber distribution or diameter between the SOL and EDL in Xueshan chickens ( > 0.05). A total of 3226 phosphopeptides corresponding to 1762 phosphoproteins were identified, with serine as the most abundant phosphorylated amino acid (73.92%). PDHA1, PHKB and PGAM1 were identified as the key DEPs common to both comparison groups. Bioinformatic analyses revealed that reversible site-specific phosphorylation regulates avian muscle fiber-type transformation mainly via the glycolysis/gluconeogenesis pathway. - Source: PubMed
Publication date: 2026/04/24
Li YiHuo WeiranWeng KaiqiLiu JinluGu YingjieCai YuchunZhang YangZhang YuHu XumingChen GuohongXu Qi - Glycogen storage disease type IX (GSD IX) arises from hepatic phosphorylase b kinase (PhK) deficiency attributable to pathogenic variants in the PHKA2, PHKB, and PHKG2 genes. This multicenter retrospective study evaluated clinical and biochemical data from 52 patients diagnosed across three European countries, with a median follow-up of 9.3 years (range: 1-49). In the cohort, 86.5% were classified as GSD IXa, whereas GSD IXb and IXc accounted for 7.7% and 3.8%, respectively; one diagnosis was based solely on enzymatic testing. Null variants in PHKA2 consistently resulted in severe PhK deficiency, whereas missense variants and in-frame deletions were associated with variable enzymatic impairment (8/19 tested cases). The median age at symptom onset was 1.6 years, and the mean age at diagnosis was 2.0 years. Predominant manifestations included hepatomegaly (82%), elevated aminotransferases (81%), hypertriglyceridemia (71%), hypercholesterolemia (67%), hypoglycemia (46%), hyperlactatemia (38%), and short stature (30%). Aberrant apolipoprotein C-III glycosylation was detected in 80% of analyzed samples. Nutritional intervention was associated with improved growth (height SD score - 0.8 ± 1.3 vs -0.2 ± 1.65; = 0.031) and fewer documented fasting hypoglycemia episodes (20/44 vs 9/44; = 0.012), although hepatomegaly frequently persisted. Liver biopsies showed steatosis, fibrosis, and/or chronic hepatitis in 52% of examined cases. A single hepatic adenoma was identified in a 14-year-old male. Overall, the clinical course of GSD IX was favorable, with hepatomegaly, elevated liver enzymes, and dyslipidemia as the most prevalent features. Severe hypoglycemic episodes were uncommon, and no clear genotype-phenotype correlation emerged. - Source: PubMed
Publication date: 2026/02/14
Magner MartinŠáhó RobertSlavíková PetraBakaľár RadovanDvořáková LenkaPešková KarolínaRamadža Danijela PetkovićBarić IvoIlic NikolaČechová AnnaŘeboun MartinVlášková HanaKelifová SilvieJešina PavelProcházková DagmarHansíková HanaHonzík TomášZeman Jiří - This study aimed to identify lactylation-associated genes linked to immune infiltration and diagnostic potential in neuropathic pain using integrated bioinformatic and machine learning approaches. Two microarray datasets (GSE124272 and GSE150408) comprising peripheral blood transcriptomes from 25 NP patients and 25 healthy controls were obtained from the gene expression omnibus. After batch correction and merging, the combined dataset served as the training set. Differentially expressed genes overlapping with lactylation-related gene sets were identified. Functional enrichment analyses, including gene ontology and Kyoto encyclopedia of genes and genomes pathway analyses, were performed. A protein-protein interaction network was constructed. Three machine learning algorithms-least absolute shrinkage and selection operator, support vector machine recursive feature elimination, and random forest-were applied to identify robust diagnostic gene signatures. Subsequently, the candidate biomarkers were validated using an independent test set (GSE95849). A diagnostic nomogram was developed, and regulatory networks were analyzed. Immune infiltration analysis was conducted via cell-type identification by estimating relative subsets of RNA transcripts. Functional analyses indicated involvement of pathways such as glucagon signaling, thermogenesis, and mitochondrial inner membrane function. Machine learning-identified 5 diagnostic gene candidates: CYP27A1, ELAC2, TMEM126B, LYRM7, and PHKB. Among these, CYP27A1 and PHKB were further investigated in an independent test set. Immune infiltration analysis showed significant alterations in 19 immune cell types, with CYP27A1 and PHKB closely correlated with immune cell distribution. This study identified CYP27A1 and PHKB as potential lactylation-associated biomarkers for NP, offering new insights into its pathogenesis and a theoretical basis for improved diagnosis. - Source: PubMed
Wu WenhuiYang Denghao - BACKGROUND: Glycogen storage diseases (GSDs) are a group of hereditary metabolic disorders caused by defects in biosynthesis, and storage of glycogen that affect various organs, such as liver, muscles, and heart. Approximately 29 genes are implicated in GSDs. This study aimed to identify the genetic variants causing GSDs in Jordanian patients. METHODS: Twenty patients with clinically suspected GSD were studied. Clinical data were reviewed and whole exome sequencing (WES) was conducted. Variants were validated, and the carrier status of the parents was confirmed by Sanger sequencing. Following genetic counseling, seven families opted for prenatal diagnosis (PND), and one of them proceeded with preimplantation genetic diagnosis (PGD) after the previous unsuccessful PND. RESULTS: Thirteen putative disease-causing variants in nine genes (AGL, GAA, GBE1, G6PC, PHKA2, PHKB, PHKG2, SLC2A2, and SLC37A4) were identified. Three of these variants have never been published. GSDII was the most common type (25%), followed by GSDIa (20%), GSDIb (15%), GSDIII and GSDIXC (10% each), and GSDIV, GSDIXa, GSDIXb, and GSDXI (5% each). Out of eight PND cases, two fetuses were affected, whereas the rest were unaffected. PGD identified two normal embryos out of the 13 tested, resulting in the successful birth of a healthy son. CONCLUSIONS: This study expands the genetic spectrum of GSD-associated genes and highlights the role of consanguinity in disease prevalence. WES has proven effective for the diagnosis of GSDs, facilitating accurate disease identification, early treatment, and management. These findings are valuable for genetic counseling, PND, and PGD as effective tools for disease prevention and family planning. - Source: PubMed
Publication date: 2025/10/03
Shboul MohammadEl-Khateeb MohammedFathallah Rajaa - Glycogen storage disease type IX (GSD IX) is a group of inherited metabolic disorders caused by phosphorylase kinase deficiency affecting the liver or muscle. Despite being relatively common among GSDs, GSD IX remains underexplored. - Source: PubMed
Publication date: 2025/05/15
Candela EgidioMontanari GiuliaZanaroli AndreaBaronio FedericoOrtolano RitaBiasucci GiacomoLanari Marcello