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Ratiometric Fluorescent Strategy for Localizing Alkaline Phosphatase Activity in Mitochondria Based on the ESIPT Process.

08:00 EDT 12th September 2019 | BioPortfolio

Summary of "Ratiometric Fluorescent Strategy for Localizing Alkaline Phosphatase Activity in Mitochondria Based on the ESIPT Process."

Fluorescent probes are powerful tools for detecting and mapping the species of interest in vitro and in vivo. Although the probes always show high selectivity and sensitivity, they are usually affected by some factors, such as detecting conditions and the probe concentrations. Ratiometric fluorescent strategies, possessing advantage of low background noise, would solve the problem effectively and lead to a higher sensing performance. Thus, an ESIPT-based ratiometric probe (HBTP-mito) was developed on the basis of a phosphorylated 2-(2'-hydroxyphenyl)-benzothiazole derivative for the determination of ALP activity. HBTP-mito is water soluble and emits green fluorescence in TBS buffer due to the blockage of ESIPT. Upon the introduction of ALP, the phosphate ester of HBTP-mito was hydrolyzed and the ESIPT process was restored. Accordingly, the fluorescence at 514 nm decreases, while emission at 650 nm shows a "turn-on" response. The ratio of intensity (/) decreases linearly with ALP activity increasing from 0 to 60 mU/mL, obtained an LOD of 0.072 mU/mL. The favorable performance of the probe enables its application not only in the detection of ALP activity in biological samples, but also in the localization of the ALP levels in living cells and in vivo.

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Name: Analytical chemistry
ISSN: 1520-6882
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Medical and Biotech [MESH] Definitions

An enzyme that catalyzes the hydrolysis of nitrophenyl phosphates to nitrophenols. At acid pH it is probably ACID PHOSPHATASE (EC 3.1.3.2); at alkaline pH it is probably ALKALINE PHOSPHATASE (EC 3.1.3.1). EC 3.1.3.41.

A physiologically active metabolite of VITAMIN D. The compound is involved in the regulation of calcium metabolism, alkaline phosphatase activity, and enhances the calcemic effect of CALCITRIOL.

One of four major classes of mammalian serine/threonine specific protein phosphatases. Protein phosphatase 2C is a monomeric enzyme about 42 kDa in size. It shows broad substrate specificity dependent on divalent cations (mainly manganese and magnesium). Three isozymes are known in mammals: PP2C -alpha, -beta and -gamma. In yeast, there are four PP2C homologues: phosphatase PTC1 that have weak tyrosine phosphatase activity, phosphatase PTC2, phosphatase PTC3, and PTC4. Isozymes of PP2C also occur in Arabidopsis thaliana where the kinase-associated protein phosphatase (KAPP) containing a C-terminal PP2C domain, dephosphorylates Ser/Thr receptor-like kinase RLK5.

A trace element with atomic symbol Mn, atomic number 25, and atomic weight 54.94. It is concentrated in cell mitochondria, mostly in the pituitary gland, liver, pancreas, kidney, and bone, influences the synthesis of mucopolysaccharides, stimulates hepatic synthesis of cholesterol and fatty acids, and is a cofactor in many enzymes, including arginase and alkaline phosphatase in the liver. (From AMA Drug Evaluations Annual 1992, p2035)

An enzyme that catalyzes the conversion of an orthophosphoric monoester and water to an alcohol and orthophosphate. EC 3.1.3.1.

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