Sterol ester hydrolytic activity of lipoprotein lipase from Pseudomonas fluorescence.

Sugiura, Masahiro; Isobe, Masakazu; Oikawa, Tsutomu; Oono, Hiroyuki

doi:10.1248/cpb.24.1202

Cited by 10 publications

(5 citation statements)

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“…However, these conditions did not enable dissociation of TRL from LDL. Cholesterol esterase is known not only to hydrolyze cholesterol ester, but also to have lipoprotein lipase activity, degrading TGs (13). TG and esterified cholesterols are strongly hydrophobic and are present in the core of lipoprotein particles.…”

Section: Discussionmentioning

confidence: 99%

Development and Population Results of a Fully Automated Homogeneous Assay for LDL Triglyceride

Ito

Ohta

Ikezaki

et al. 2018

The Journal of Applied Laboratory Medicine

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Background: Low-density lipoprotein (LDL) is measured by its cholesterol content (LDL-C), but it has been suggested that LDL triglyceride (LDL-TG) may also be related to coronary artery disease risk. LDL-TG can be measured after ultracentrifugation or electrophoresis, but these are labor intensive methods, indicating the need for an automated homogeneous assay. Methods: TG-rich lipoproteins (TRLs), LDL, and HDL were isolated by ultracentrifugation and used to determine optimal characteristics of surfactants and various enzymes for assay development. We analyzed assay precision and linearity, and compared results with those obtained after ultracentrifugation. Serum samples from a large population study (n = 12 284 subjects) were used to generate reference intervals for LDL-TG and to determine levels in various types of hyperlipidemia. Results: An assay for LDL-TG has been developed by use of surfactants 1 and 2, and enzymes to measure LDL-TG directly on an automated analyzer. There was an excellent correlation between results obtained with this assay and after isolation of LDL by ultracentrifugation. When the assay was applied to serum samples from normal and hyperlipidemic subjects, median normal values were 0.09 mmol/L, with significant median elevations observed in subjects with increased LDL-C, hypertriglyceridemia, combined hyperlipidemia, and hyperchylomicronemia of 0.19, 0.18, 0.28, and 0.43 mmol/L, respectively, as compared with mean LDL-C values in these subjects of 2.25, 4.01, 2.66, 3.96, and 2.43 mmol/L, respectively. Conclusions: We have developed an automated homogeneous assay for LDL-TG for potential use in research and clinical laboratories, and documented that the TG molar content of LDL is about 5% of its cholesterol content. IMPACT STATEMENT LDL is assessed by measuring its cholesterol content. It has been suggested that LDL triglycerides are also related to cardiovascular disease risk. We have developed an automated homogeneous LDL-TG assay with use of an optimized combination of surfactants, lipoprotein lipase, and cholesterol esterase. We investigated LDL-TG distribution in a large population study. This assay readily distinguished LDL-TG from TG in other lipoprotein fractions, and the assay provided results that were highly correlated with LDL-TG measured after isolation of LDL by ultracentrifugation. Thus, our automated LDL-TG assay has potential value in clinical research and practice.

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Section: Discussionmentioning

confidence: 99%

Development and Population Results of a Fully Automated Homogeneous Assay for LDL Triglyceride

Ito

Ohta

Ikezaki

et al. 2018

The Journal of Applied Laboratory Medicine

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“…Assay of esterase activity: The activities of esterase and lipase were determined ac cording to our methods described previously, using 9-naphthyl derivatives, phenyl acetate, tributyrin and olive oil as substrates (7,8). The drug-hydrolyzing activity was also deter mined according to our method, using acethylsalicylic acid (aspirin), salicylic acid derivatives, ethylchlorophenoxy-isobutyrate (clofibrate, CPIB), indanyl carbenicillin (I-CBPC), procaine, atropine, acethylcholine, benzylcholine and procainamide as substrates (4,9).…”

Section: Methodsmentioning

confidence: 99%

Comparative study of human intestinal and hepatic esterases as related to enzymatic properties and hydrolizing activity for ester-type drugs.

et al. 1980

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Carboxylesterase capable of hydrolyzing carboxyl esters, thiol esters and armatic amides, is found in most animal tissues (1).Recently a variety of ester-type drugs are being used in various ways as prodrugs (2).Ester-type prodrugs are hydrolyzed by esterases in intestinal mucosa, liver and serum, and the degree of hydrolysis affects their pharmacological activities. There are, however, only a few reports on the purification and properties of human intestinal esterase and hepatic esterase (3). We have already reported the purification of esterase from human intestinal mucosa (4, 5). When esterase from intestinal mucosa has been examined for its action in the metabolism of ester-type drugs in the body, esterase from liver must also be considered.In this paper, we detailed the difference of two esterases in their enzymatic properties and substrate specificities. MATERIALS AND METHODSEnzyme purification:The small intestine (jejunum) and liver were obtained from humans at the time autopsy carried out 12 hr after death. Esterase from the intestinal

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“…The extracellular lipase required oleic acid as a stabilizer/activator, whereas the cell‐bound lipases did not, and differed in several properties from the extracellular enzyme. Sugiura et al [101]and Ota et al [102]solubilized two cell‐bound, monomeric lipases of 39 and 44 kDa, which differed in their pH optima. Gomi et al [103]showed that the lipase(s) exist in the cell wall as an activator‐bound complex, which is rapidly dissociated upon enzyme purification.…”

Section: Physiologymentioning

confidence: 99%

Physiology and genetics of the dimorphic fungusYarrowia lipolytica

Barth¹,

Gaillardin²

1997

FEMS Microbiol Rev

442

100

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The ascomycetous yeast Yarrowia lipolytica (formerly Candida, Endomycopsis, or Saccharomyces lipolytica) is one of the more intensively studied 'non-conventional' yeast species. This yeast is quite different from the well-studied yeasts Saccharomyces cerevisiae and Schizosaccharomyces pombe with respect to its phylogenetic evolution, physiology, genetics, and molecular biology. However, Y. lipolytica is not only of interest for fundamental research, but also for biotechnological applications. It secretes several metabolites in large amounts (i.e. organic acids, extracellular proteins) and the tools are available for overproduction and secretion of foreign proteins. This review presents a comprehensive overview on the available data on physiology, cell biology, molecular biology and genetics of Y. lipolytica.

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Sterol ester hydrolytic activity of lipoprotein lipase from Pseudomonas fluorescence.

Cited by 10 publications

References 0 publications

Development and Population Results of a Fully Automated Homogeneous Assay for LDL Triglyceride

Development and Population Results of a Fully Automated Homogeneous Assay for LDL Triglyceride

Comparative study of human intestinal and hepatic esterases as related to enzymatic properties and hydrolizing activity for ester-type drugs.

Physiology and genetics of the dimorphic fungusYarrowia lipolytica

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