PON1 protein, human
It plays a crucial role in the hydrolysis and metabolism of various substrates, including organophosphate insecticides, nerve agents, and lipid peroxides.
PON1 is believed to have antioxidant properties and may contribute to the prevention of cardiovascular disease.
Research on the structure, function, and regulation of PON1 is important for understanding its physiological and pharmacological relevance.
Studiing PON1 may provide insights into its potentail therapeutic applications and its role in heatlh and disease.
Most cited protocols related to «PON1 protein, human»
Plasma total cholesterol (TC) and triglycerides levels were measured by enzymatic colorimetric assays (Prodia diagnostics, Boetzingen, Germany). HDL-cholesterol (HDL-C) was determined after precipitation of the apolipoprotein B-containing lipoproteins, and LDL-cholesterol (LDL-C) was calculated using Friedewald formula (Sekisui, Tokyo, JP). Lipoprotein (a), apolipoprotein AI (apoAI), and apolipoprotein B100 (apoB100) were detected by immunoturbidimetric assays (Prodia diagnostics, Boetzingen, Germany). All the assays were performed blindly. Serum tumor necrosis factor alpha (TNF-α) and interleukin-6 (IL-6) levels of mice were determined using an enzyme-linked immunosorbent assay (ELISA) kit according to the manufacturer's instructions (eBioscience, San Diego, USA). Each sample was assayed in triplicate, and the intra-assay coefficient of variation was less than 10%. The concentration of high-sensitivity C-reactive protein (hs-CRP) in human plasma was determined on an Olympus analyzer by a high sensitivity latex-enhanced immunoturbidimetry assay using Nanopia CRP kit (Sekisui, Tokyo, JP) with standards and controls supplied by the manufacturer.
Most recents protocols related to «PON1 protein, human»
Example 39
Generally, pharmacophores for FAAH inhibitors, urea and non-urea based, interact by either carbamoylating or forming transition-state mimics with the catalytic serine residue. However, since a large number of hydrolases utilize a similar catalytic serine residue, many FAAH inhibitors have suffered from poor selectivity. Therefore, the potency of t-TUCB, A-14 and A-21 on several other serine hydrolases was tested. Included in this panel were carboxylesterases, hydrolases involved in xenobiotic detoxification, and paraoxonases and esterases involved in the regulation of arterosclerosis. As is shown in Table 5 below, none of these serine hydrolases were inhibited by t-TUCB, A-14, or A-21.
Total protein was extracted by using Takara kit. The Protein concentration was detected by BCA assay. The primary antibodies used in this study were anti-CYP2C9 (1:1000, Abcam), anti-PON1(1:1000, Abcam) anti-beta-Actin (1:1000, Cell Signaling Technology).
Parameters related to oxidation, malondialdehyde (MDA) levels and antioxidant capacity, were measured by the MDA/thiobarbituric test and by the 2,2-diphenyl-1-picrylhydrazyl (DPPH) test, respectively. Nitrite levels in serum were measured by the Griess method.
PAF-AH activity was quantified using 2-thio-PAF (Cayman Chemicals, Denver, CO, USA) as a substrate [34 (link)] and PON-1 activity by using phenylacetate (Sigma/Merck, Darmstadt, Germany), as described [35 (link)]. Total PAF-AH activity was measured in serum. In addition, both PAF-AH and PON-1 activities, as well as ChE, detailed hereafter, were also determined in apoB-depleted serum (HDL fraction) obtained by serum precipitation with dextran sulfate [36 (link)].
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More about "PON1 protein, human"
This versatile protein, primarily expressed in the liver, exhibits esterase and lactonase activities, allowing it to hydrolyze and metabolize a diverse range of substrates, including organophosphate insecticides, nerve agents, and lipid peroxides.
Reseach on the structure, function, and regulation of PON1 has garnered significant interest due to its potential therapeutic applications and its role in health and disease.
PON1 is believed to possess antioxidant properties, and its involvement in the prevention of cardiovascular disease has been a focus of numerous studies.
Exploring the PON1 enzyme encompasses various related terms and subtopics.
Paraoxon, a potent organophosphate compound, is a well-known substrate for PON1's esterase activity.
Phenylacetate, another substrate, is commonly used to assess PON1's lactonase function.
The Cobas 8000 analyzer and Amplifluor assay are among the analytical tools employed to measure PON1 activity.
To study PON1, researchers often utilize techniques such as the QIAamp DNA Blood Mini Kit for DNA extraction, and the DCFH-DA assay to evaluate the enzyme's antioxidant properties.
Protease inhibitor cocktails are frequently employed to preserve the integrity of PON1 during experimentation.
Advancing our understanding of PON1 is crucial for unraveling its physiological relevance and exploring its potential therapeutic applications.
By leveraging the latest research methodologies and tools, scientists can continue to expand our knowledge of this versatile and fascinating protein.