ACPT
- Known as:
- ACPT
- Catalog number:
- 001036A
- Product Quantity:
- 250ul
- Category:
- -
- Supplier:
- ABM
- Gene target:
- ACPT
Related genes to: ACPT
- Gene:
- ACP4 NIH gene
- Name:
- acid phosphatase 4
- Previous symbol:
- ACPT
- Synonyms:
- -
- Chromosome:
- 19q13.33
- Locus Type:
- gene with protein product
- Date approved:
- 2001-07-13
- Date modifiied:
- 2017-06-23
Related products to: ACPT
Related articles to: ACPT
- Plastid ACPs are not limiting factors for seed oil accumulation and show functional redundancy, while their differentiation affects fatty acid composition. Plastid acyl carrier proteins (ACPs) act as acyl carriers in the fatty acid biosynthesis, yet the specific functions of different isoforms and their roles in seed oil accumulation remain unclear. To investigate the functions of the five ACPs in Arabidopsis seeds, this study analyzed their structure, expression pattern, and phenotypes of mutants and seed-specific overexpression lines. The results showed that ACP1, ACP2, ACP3, and ACP5 are expressed in developing seeds. Total fatty acid content of seeds is not affected by mutations of single, double, or triple ACPs, or their overexpression. Comprehensive analysis of changes in fatty acid composition in loss-of-function and overexpression seeds revealed that ACP1 and ACP5 may promote the accumulation of longer-chain and more unsaturated fatty acids. ACP2 has similar, but weaker effects on fatty acid composition compared with ACP1 and ACP5. ACP3 may uniquely enhance the accumulation of 20:1. ACP4 differs from the other four ACPs in both protein structure and a function of increasing 16:0 and 18:2. Our results indicate that ACPs exhibit functional redundancy and may not be limiting factors in oil accumulation, yet these ACPs differentially affect fatty acid composition. - Source: PubMed
Publication date: 2026/06/10
Guo NingxinChen YangyangZhao JialiangWen JiayinZhao CuizhuZhang Meng - Amelogenin (AMELX), the predominant extracellular matrix protein (EMP) in forming enamel, has a single phosphorylation site at Serine 16 (S16). Previously, we demonstrated that AMELX phosphorylation enhances its ability to stabilize amorphous calcium phosphate and inhibit mineralization. To study the role of AMELX phosphorylation in vivo, we substituted S16 with Ala to prevent phosphorylation in a generated AmelxS16A knock-in (KI) mice. These KI mice exhibited hypoplastic enamel with ectopic calcifications, a lack of enamel rods, an accelerated transformation of amorphous calcium phosphate (ACP) to apatitic enamel crystals, and progressive pathological changes in ameloblasts, the enamel forming cells responsible for enamel production. The goal of this study was to test the hypothesis that the phosphorylation status of AMELX affects its interactions with other proteins in the extracellular enamel space. To determine the effect of AMELX phosphorylation on the protein–protein interactions, we have conducted Proximity Ligation Assays (PLA) of wild type (WT) and KI mandibular incisors. Specifically, we conducted PLA of Amelx with a transmembrane acid phosphatase 4 (Acp4), basal lamina protein laminin β3 (Lamβ3) and the EMP ameloblastin (Ambn). Quantitative image analysis showed significantly higher PLA signal for Acp4 in the ameloblast cell bodies and distal ends of WT mice. PLA signal was also significantly higher for Ambn in the ameloblast distal ends and in the enamel matrix of WT mice. For Lam5, the signal was also higher in ameloblasts cell bodies, ameloblast distal ends and the enamel matrix of WT mice. Collectively, the significantly higher PLA signals between phosphorylated Amelx and Ambn, Acp4, and Lamβ3, compared with nonphosphorylated Amelx, suggest that AMELX phosphorylation promotes potentially important protein–protein interactions during amelogenesis. - Source: PubMed
Publication date: 2026/04/29
Vasquez BrentBui Ai ThuMargolis Henry CBeniash Elia - Amelogenesis imperfecta (AI) is a group of rare inherited conditions causing tooth enamel defects. Human acid phosphatase 4 (ACP4) is a transmembrane protein involved in maintaining appositional enamel growth. Variants in ACP4 cause recessive hypoplastic AI. Here we identify further families and review published ACP4 variants causing AI. In three Pakistani families, we identified a new ACP4 variant, c.254T > C, p.(Pro85Leu), which long-read sequencing revealed to be a founder variant. Two further families were homozygous for previously reported pathogenic ACP4 variants. Further details are also reported for two families previously listed in a technical/cohort study by this group. In total, seventeen ACP4 variants had been reported in the literature causing AI in seventeen families prior to this study. This report adds an eighteenth variant and brings the total to 22 families. Nine families derive from a cohort of over 400 AI probands curated in Leeds, UK, and account for 9/129 families solved for recessive AI, suggesting ACP4 variants are a significant cause of recessive AI. ACP4 variants implicated in AI include fifteen missense, one splice and two frame-breaking deletions. Most missense variants are within the acid phosphatase domain, with one in the transmembrane domain. The consistent hypoplastic phenotype suggests a single mutational mechanism, and the report of a family with a homozygous frameshift variant likely to be subject to nonsense mediated decay points to loss of function. Missense variants alter amino acids at the catalytic core or affect protein stability, homodimerisation or membrane localisation, all likely to result in functional insufficiency. - Source: PubMed
Publication date: 2026/04/11
Liu LuAu Cheuk WangHany UmmeyRigby Alice LChauhan AneshaBrown CatrionaSims JessieMurillo GinaAcosta de Carmargo Marìa GabrielaInglehearn Chris FWatson Christopher MMighell Alan JSmith Claire E L - In most vertebrates, teeth are continuously shed and replaced throughout life, while mammals and several lineages of reptiles have reduced replacement to only one or two generations. In contrast to the vast majority of their living relatives, members of the lizard families Chamaeleonidae and Agamidae have dispensed with lifelong tooth replacement, instead developing acrodont dentition that fuses to the jawbone to be used for the lifetime of the animal. Though, the loss of tooth replacement has not come without a cost. In order to mitigate the consequences that come with tooth replacement loss, mammals and acrodont lizards have evolved adaptations that strengthen enamel structure and minimize wear and tear experienced during the life of the animal. While these physical adaptations are well documented, the effect that loss of tooth replacement has had on the molecular components of teeth has not received significant attention. Here, we analyze the coding and amino acid sequences of six tooth proteins (AMBN, AMEL, AMTN, ACP4, ENAM, and MMP20) from acrodont lizards, pleurodont lizards that replace teeth, and mammals. We show that the reduction of tooth generations has disproportionately affected the evolutionary trajectory of proteins associated with enamel structure, with a particularly magnified effect on the evolution of AMEL. - Source: PubMed
Publication date: 2025/08/07
Abramyan JohnLi GengxinKhansa Hannah - Breast cancer is a very common disease affecting females on a global scale. It is responsible for approximately 10% of breast cancer-related fatalities. In 2022, approximately 2,308,897 new cases were reported globally. Recent studies focused on breast tumors have successfully recognized somatic mutations. This study aimed to identify previously unidentified somatic mutations in breast cancer patients belonging to Pakistan. - Source: PubMed
Publication date: 2025/07/31
Nawaz YasirMunir SabaTanvir FouziaRiaz Hafiza FizzahNawaz AqeelaRiaz Samreen