Ask about this productRelated genes to: HMGB4 antibody
- Gene:
- HMGB4 NIH gene
- Name:
- high mobility group box 4
- Previous symbol:
- -
- Synonyms:
- FLJ40388
- Chromosome:
- 1p35.1
- Locus Type:
- gene with protein product
- Date approved:
- 2005-09-30
- Date modifiied:
- 2014-11-19
Related products to: HMGB4 antibody
Related articles to: HMGB4 antibody
- High-mobility group (HMG) protein families are critical regulators of chromatin structure and gene expression in breast cancer. This study systematically evaluates their expression patterns, genetic interactions, and clinical relevance. - Source: PubMed
Shariff Ehtesham AhmedAzharuddin AhmedAbu-Zaid RatebAl-Wathinani AhmedAlenazy Eid BasheerSharieff Raiyan Ehtesham Ahmed - We have established a method for chromatin immunoprecipitation coupled to mass spectrometry (ChIP-MS) in Arabidopsis thaliana. We demonstrate its utility by investigating proteins associated with histone H3 lysine 27 acetylation (H3K27ac), a key epigenetic mark regulating photosynthesis-associated nuclear genes (PhANGs) during chloroplast development and establishment of photosynthesis. Purification of chromatin-associated proteins from light-grown Arabidopsis cell cultures identified 66 proteins associated with H3K27ac that met the selection criteria in the two replicate experiments: (i) 2-fold change in relation to IgG, (ii) at least two unique peptides, and (iii) relevant biological annotations. The identified proteins included chromatin remodelers, chromatin regulators and transcription factors with potential roles in H3K27ac deposition. To evaluate the physiological role of the candidates associated with the H3K27ac mark, we developed a rapid and reproducible phenotyping method based on controlled light scanning to determine chlorophyll accumulation in mutant seedlings. We complemented with pigment quantification and analysis of photosynthesis-associated nuclear genes (PhANGs) expression. Several mutants displayed altered greening, pigment accumulation, or affected photosynthetic gene expression consistent with a role during chloroplast development. Notably, chr11, chr17, and atpds5a mutants showed impaired pigment accumulation and reduced expression of PhANGs, whereas hmgb4 and mbd10 mutants exhibited increased greening and induction of PhANGs. Together, these findings establish ChIP-MS as a robust approach to identify histone mark-associated proteins in plants and provide a first set of candidate regulators of H3K27ac during chloroplast biogenesis. This technical advance opens new possibilities to discover chromatin-based regulation of plant development and environmental responses. - Source: PubMed
Brun AlexisQuevedo MartiSterling Luis ADekkers Dick H WDemmers JeroenHudson Elton PaulStrand Åsa - Advancing age in men significantly contributes to declining sperm fertility. Information on age-related proteomic changes in spermatozoa is limited. This study involved normal fertile Arab men in three age groups: young adult (21-30 years; = 6), late adult (31-40 years; = 7), and advanced age (40-51 years; = 5). Gradient-purified spermatozoa were analyzed using LC-MS/MS and proteomic data were processed using Progenesis QI (QIfp) v3.0 and UniProt/SwissProt. Significantly enriched annotations and clustering of proteins in the proteomic datasets were identified (2-fold change; < 0.05). A total of 588 proteins were identified, with 93% shared across the three groups. Unique proteins were MYLK4 for the young adult group, PRSS57 for the late adult group, and HMGB4, KRT4, LPGAT1, OXCT2, and MGRN1 for the advanced age group. Furthermore, 261 (44%) proteins were differentially expressed ( < 0.05) across the three groups. Functional enrichment analysis suggested an aging-related significant increase in pathways associated with neurodegenerative diseases and protein folding, alongside decreases in glycolysis/gluconeogenesis, flagellated sperm motility, acetylation, phosphoprotein modifications, oxidation processes, and Ubl conjugation. Cluster analysis highlighted significantly upregulated proteins in young adults (e.g., H2BC1, LAP3, SQLE, LTF, PDIA4, DYNLT2) and late adults (e.g., ATP5F1B, ODF2, TUBA3C, ENO1, SPO11, TEX45, TEKT3), whereas most proteins in the advanced age group exhibited downregulation (e.g., SPESP1, RAB10, SEPTIN4, RAB15, PTPN7, USP5, ANXA1, PRDX1). In conclusion, this study revealed aging-associated proteomic changes in spermatozoa that impact critical processes, including spermatogenesis, motility, metabolism, and fertilization, potentially contributing to fertility decline. These changes provide a molecular framework for developing therapies to preserve sperm proteostasis and enhance fertility in older men. - Source: PubMed
Publication date: 2025/06/25
Beg Mohd AminIsmail Abrar OsamaAlaiya AyodeleKhan Firdous AhmadHamoda Taha Abo-Almagd Abdel-MeguidSheikh Ishfaq AhmadSharma PriyankaBaothman Omar MohammedAlkhzaim Ali HasanShinwari ZakiaAbuzinadah Rinad FahadMohammed ArifAssiri Abdullah MohammedAbuzenadah Adel MohammadMemili ErdoganFeugang Jean Magloire - Lipopolysaccharide (LPS) endotoxin is a well-characterized microbe-associated molecular pattern (MAMP) that forms the outer membrane of both pathogenic and commensal Gram-negative bacteria. It plays a crucial role in triggering inflammatory disorders such as mastitis, acidosis, and septicemia. In heifers, an LPS challenge induces a dynamic stress response, marked by elevated cortisol levels, increased body temperature, and altered immune function. Research indicates that LPS administration leads to a significant rise in cortisol post-challenge. Building on this understanding, the present study aimed to estimate genetic parameters for serum cortisol response to LPS challenge in and its linear associations with production, health, reproduction, and conformation traits. Additionally, a genome-wide association study (GWAS) was conducted to identify genetic regions associated with cortisol response. A total of 252 animals were evaluated for cortisol response, with correlations estimated between cortisol levels and 55 genomic breeding values for key traits. Genetic parameters and heritability for cortisol response were estimated using Residual Maximum Likelihood (REML) in the Blupf90+ v 2.57 software. Single-Step GWAS (ssGWAS) employing a 10-SNP window approach and 42,123 SNP markers was performed to identify genomic regions that explained at least 0.5% of additive genetic variance. Finally, candidate genes and QTLs located 50 kb up and downstream of those windows were identified. The cortisol response showed significant but weak linear associations with cystic ovaries, body maintenance requirements, lactation persistency, milk yield, and protein yield (-value ≤ 0.05) and showed suggestive weak linear associations with udder texture, clinical ketosis, heel horn erosion, and milking speed (-value ≤ 0.15). Cortisol response showed significant additive genetic variance, along with moderate heritability of 0.26 (±0.19). A total of 34 windows explained at least 0.5% of additive genetic variance, and 75 QTLs and 11 candidate genes, comprising the genes , , , , , , , , , , and , were identified. The functional enrichment analysis allowed us to infer two instances where these gene products could interfere with cortisol production: the first instance is related to the complement system, and the second one is related to the EMT (Epithelium-Mesenchymal Transition) and pituitary gland formation. Among the QTLs, 13 were enriched in the dataset, corresponding to traits related to milk (potassium content), the exterior (udder traits, teat placement, foot angle, rear leg placement, and feet and leg conformation), production (length of productive life, net merit, and type), and reproduction (stillbirth and calving ease). In summary, the cortisol response to LPS challenge in seems to be moderately heritable and has weak but significant linear associations with important production and health traits. Several candidate genes identified could perform important roles, in at least two ways, for cortisol production, and QTLs were identified close to regions of the genome that explained a significant amount of additive genetic variance for cortisol response. Therefore, further investigations are warranted to validate these findings with a larger dataset. - Source: PubMed
Publication date: 2025/06/26
Galindo Bruno AShandilya Umesh KSharma AnkitaSchenkel Flavio SCanovas AngelaMallard Bonnie AKarrow Niel A - High motility spermatozoa are good for cryopreservation and artificial insemination (AI) of mammalian semen. In this study, normal motility (NM) and low motility (LM) Mediterranean buffalo spermatozoa were compared using quantitative proteomics and phosphoproteomics techniques to screen for important proteins and phosphorylated proteins related to the motility of spermatozoa and to identify candidate protein molecular markers related to the quality of Mediterranean buffalo semen. Proteomics results identified 2550 proteins, with 119 proteins upregulated and 146 proteins downregulated in the LM spermatozoa versus the NM spermatozoa. The differentially abundant proteins were mainly involved in carbohydrate metabolism, glycolysis/gluconeogenesis, and tricarboxylic acid cycles. The phosphoproteomics analysis revealed 412 proteins, 1228 phosphorylated peptides, and 1465 phosphorylation modification sites. Compared to the NM group, 119 peptides were downregulated in the LM group, corresponding to 98 proteins, and 84 phosphorylated peptides were upregulated in the white matter, corresponding to 61 proteins. Differentially phosphorylated proteins were primarily involved in spermatogenesis, flagellate sperm motility, and glycolysis/gluconeogenesis. The combined proteomics and phosphoproteomics results identified the common proteins HMGB4, POC1B, PKM, LDHA, TBC1D21, and CBY2, whose main roles were related to spermatogenesis, sperm flagellar structure, and energy metabolism, which can be used as potential markers of Mediterranean buffalo sperm quality. - Source: PubMed
Publication date: 2025/02/15
Xue QingsongRen XuanXu TairanYang TingSun LeLuo XiHuang ShihaiShi DeshunLi Xiangping