Disease relevance of ACP2

• Legionella micdadei cells contain an acid phosphatase (ACP2) which blocks superoxide anion production by human neutrophils stimulated with formyl-Met-Leu-Phe (fMLP) [A. K. Saha, et al. (1985) Arch. Biochem. Biophys. 243, 150-160] [1].

High impact information on ACP2

• Two other cysteine proteinase genes (ACP2, ACP3) are 85% identical to each other and are present in both pathogenic and nonpathogenic isolates [2].
• To determine whether it was possible to increase toxin sensitivity by increasing the rate of toxin internalization, we constructed diphtheria toxin cytoplasmic domain mutant cell lines containing rapid-internalization signals from either the low density lipoprotein receptor or from the lysosomal acid phosphatase precursor [3].
• The results indicate that the presence of ACP 2 is essential for the synthesis of decanoic acid in C. lanceolata seeds, and its expression in the phase of accumulation of high levels of this fatty acid provides an additional and highly efficient cofactor for stimulating the FAS reaction [4].
• Analysis of PCR amplifications, first from somatic cell hybrids and subsequently from radiation hybrids, localizes the human RAPSN gene locus to chromosome 11p11.2-p11.1 in close proximity to ACP2 [5].
• Three human genes known between 11p11 and 11p13 (FSHB, CAT, ACP2) were on murine chromosome 2 [6].

Biological context of ACP2

• Regional mapping of the gene for human lysosomal acid phosphatase (ACP2) using a hybrid clone panel containing segments of human chromosome 11 [7].
• Genetic polymorphism of rabbit (Oryctolagus cuniculus) tissue acid phosphatases (ACP2 and ACP3) [8].
• We explored the possibility that ACP2 acts by interfering with polyphosphoinositide hydrolysis and the production of the intracellular second messengers, inositol trisphosphate (IP3) and diacylglycerol, following neutrophil stimulation [1].
• The observed genetic diversity between the species at the ACP2 locus supports other studies which indicate that A. alosa is the less polymorphic species of the two [9].

Anatomical context of ACP2

• Subsequent chromatography of ACP2 on a Sephadex G-150 column revealed coincident elution of phosphatase activity and neutrophil blocking activity [10].
• Bone marrow (BM) cells from BALB/c mice were transduced in vitro with a retroviral construct containing green fluorescent protein (GFP) for detection and human LAP (hLAP) as a test molecule [11].

Associations of ACP2 with chemical compounds

• Chromatography of the extract on a hydroxylapatite column resolved two acids phosphatases (designated ACP1 and ACP2) [10].
• When human neutrophil phosphoinositides were prelabeled with 32Pi, subsequent incubation with ACP2 resulted in an 85% loss of the labeled PIP2 over 2 h [1].
• Phosphatidylinositol 4,5-bisphosphate (PIP2) was hydrolyzed rapidly by ACP2 in vitro [1].
• The phase evolution from CaHPO4, intermediate amorphous calcium phosphate (ACP) phases (including ACP1 and ACP2 with different structures) to final beta-TCP with increasing aging time was observed [12].
• Activity staining of ACP by native polyacrylamide gel electrophoresis revealed three isoforms: ACP-1, ACP-2, and ACP-3 [13].

Other interactions of ACP2

• Red cell acid phosphatase 1 (ACP1) is monomorphic while tissue acid phosphatase 2 (ACP2) is polymorphic in a wild rabbit population, with two alleles: ACP2*1 (0.96) and ACP2*2 (0.04) [8].

Analytical, diagnostic and therapeutic context of ACP2

• We identified hLAP sequences by polymerase chain reaction (PCR) of total DNA in recipient blood and UV-irradiated skin but not in unirradiated skin [11].

References