Ask about this productRelated genes to: ACP6 antibody
- Gene:
- ACP6 NIH gene
- Name:
- acid phosphatase 6, lysophosphatidic
- Previous symbol:
- -
- Synonyms:
- LPAP, ACPL1
- Chromosome:
- 1q21.2
- Locus Type:
- gene with protein product
- Date approved:
- 2004-07-09
- Date modifiied:
- 2016-10-05
Related products to: ACP6 antibody
Related articles to: ACP6 antibody
- The clinical phenotypes associated with 1q21.1 deletion or duplication syndromes vary considerably among individuals, and the underlying mechanisms remain poorly elucidated. Moreover, data on prenatal ultrasound findings in fetuses carrying these copy number variants are still limited. This study aimed to preliminarily evaluate the association between prenatal phenotypic features and 1q21.1 deletion/duplication syndromes. - Source: PubMed
Publication date: 2025/11/10
Luo XiaojinChen XiaohangTang YanliLiu LiXu JinmaoWu LipingPei YuanyuanLiu WeiqiangWei Fengxiang - Endometrial cancer (EC) is one of the most prevalent malignant tumors affecting women's health and well-being, with both morbidity and mortality rates increasing every year. Acid phosphatase type 6 (ACP6) is a mitochondrial lipid phosphatase that is involved in tumorigenesis and cancer progression. Although ACP6 is significantly contributing to these pathways, its specific function in EC remains poorly explored. - Source: PubMed
Publication date: 2025/06/27
Lin QinglingLiang XiaoleiMa LiangjianMa XingLi BinYang YongxiuYang Kehu - Golden pompano (Trachinotus ovatus), a marine farmed fish, is economically valuable in China. Lysophosphatidic acid phosphatase type 6 (ACP6) is a type of histidine acid phosphatase and plays an important role in regulating host inflammatory responses and anti-cancer effects in mammals. However, its function in teleost remains unknown. The present study aimed to investigate ACP6 function in golden pompano. ACP6 from golden pompano was identified, cloned, and named TroACP6. The open reading frame of TroACP6 was 1275 bp in length, encoding 424 amino acids. The TroACP6 protein shared high sequence identity (43.32%-90.57 %) with the ACP6 of other species. It contained a histidine phosphatase domain with the active site motif "RHGART" and the catalytic dipeptide HD (histidine and aspartate). Meanwhile, TroACP6 mRNA was widely distributed in the various tissues of healthy golden pompano, with the maximum expression in the head kidney. The function of TroACP6 was analyzed both in vitro and in vivo, and the results revealed that the purified recombinant TroACP6 protein exhibited optimum phosphatase activity at pH 6.0 and 50 °C in vitro. Meanwhile, upon Edwardsiella tarda challenge, TroACP6 expression in tissues increased significantly in vivo. In addition, TroACP6 overexpression enhanced the respiratory burst activity and superoxide dismutase activity of head kidney macrophages in vivo. Furthermore, the overexpression and knockdown of TroACP6 in vivo had a significant effect on bacterial infection. In summary, the study findings indicate that TroACP6 in golden pompano is involved in host defense against bacterial infection. - Source: PubMed
Publication date: 2024/09/12
Qiu RengLei YangYang QiaoliZeng JianZhou YongcanSun BinSun Yun - A series of arylsulfones and heteroarylsulfones have previously been demonstrated to dysregulate the conserved bacterial ClpP protease, causing the unspecific degradation of essential cellular housekeeping proteins and ultimately resulting in cell death. A cocrystal structure of a 2-β-sulfonylamide analog, ACP1-06, with ClpP showed that its 2-pyridyl sulfonyl substituent adopts two orientations in the binding site related through a sulfone bond rotation. From this, a new -aryl phosphine oxide scaffold, designated as ACP6, was designed based on a "conformation merging" approach of the dual orientation of the ACP1-06 sulfone. One analog, ACP6-12, exhibited over a 10-fold increase in activity over the parent ACP1-06 compound, and a cocrystal X-ray structure with ClpP confirmed its predicted binding conformation. This allowed for a comparative analysis of how different ligand classes bind to the hydrophobic binding site. The study highlights the successful application of structure-based rational design of novel phosphine oxide-based antibiotics. - Source: PubMed
Publication date: 2024/09/02
Lin FuningMabanglo Mark FZhou Jin LinBinepal GursonikaBarghash Marim MWong Keith SGray-Owen Scott DBatey Robert AHoury Walid A - Ventricular septal defects (VSDs) are recognized as one of the commonest congenital heart diseases (CHD), accounting for up to 40% of all cardiac malformations, and occur as isolated CHDs as well as together with other cardiac and extracardiac congenital malformations in individual patients and families. The genetic etiology of VSD is complex and extraordinarily heterogeneous. Chromosomal abnormalities such as aneuploidy and structural variations as well as rare point mutations in various genes have been reported to be associated with this cardiac defect. This includes both well-defined syndromes with known genetic cause (e.g., DiGeorge syndrome and Holt-Oram syndrome) and so far undefined syndromic forms characterized by unspecific symptoms. Mutations in genes encoding cardiac transcription factors (e.g., NKX2-5 and GATA4) and signaling molecules (e.g., CFC1) have been most frequently found in VSD cases. Moreover, new high-resolution methods such as comparative genomic hybridization enabled the discovery of a high number of different copy number variations, leading to gain or loss of chromosomal regions often containing multiple genes, in patients with VSD. In this chapter, we will describe the broad genetic heterogeneity observed in VSD patients considering recent advances in this field. - Source: PubMed
Perrot AndreasRickert-Sperling Silke