Bovine Apolipoprotein E in Plasma: Increase of ApoE Concentration Induced by Fasting and Distribution in Lipoprotein Fractions.

Takahashi, Yûji; Sato, Kei; Itoh, Fumiaki; Miyamoto, Toru; Oohashi, Tsutai; Katoh, Norio

doi:10.1292/jvms.65.199

Cited by 11 publications

(11 citation statements)

References 30 publications

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“…This suggests that fasting is able to up-regulate these adipocyte-derived factors in a specific manner. Adipose apoE mRNA levels have been shown to gradually increase in both subcutaneous and visceral WAT during various fasting durations [25,231,232]. This could be related to the TAG content and/or free cholesterol stores within the adipocyte in vivo.…”

Section: Other Adipose-derived Signalsmentioning

confidence: 99%

Adipose-Derived Factors During Nutritional Transitions

Bertile¹,

Raclot²

2006

CNF

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It is now commonly accepted that white adipocytes actively secrete a wide range of bioactive molecules including leptin, adiponectin, resistin and many other signals. These adipose-derived factors are mainly influenced by nutritional transitions. This review addresses essentially the differential regulation and role of animal adipose-secreted products in regulating metabolic, endocrine and behavioral responses during prolonged fasting. When reaching a low adiposity threshold, animals enter late fasting characterized by elevated rates of protein degradation while lipid utilization decreases. Low NEFA levels in late fasting could affect PPAR activation and the management of body reserves, thus promoting food seeking behavior. Low leptin levels are also likely involved in the efficient mobilization of energy stores and in the induction of strong rises in hypothalamic orexigenic neuropeptides in late fasting. This effect is prevented by leptin perfusion. During fasting, adiponectin reduced levels could be related to its ability to signal nutritional and/or metabolic changes, to promote energy preservation or to prepare the body to efficiently restore body weight in case of refeeding while resistin low levels could constitute an adipose status sensor and/or improve glucose homeostasis. The fasting-induced changes of other signals during the fed/fasted/refed transitions are also briefly discussed.

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Section: Other Adipose-derived Signalsmentioning

confidence: 99%

Adipose-Derived Factors During Nutritional Transitions

Bertile¹,

Raclot²

2006

CNF

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“…The N-terminal peptide sequencing of the 43-kDa proteins found in HDL was performed as described previously [22], using a Model 491 protein sequencer (Applied Biosystems Japan Ltd., Tokyo, Japan).…”

Section: Determination Of N-terminal Amino Acid Sequencementioning

confidence: 99%

“…After being separated by ultracentrifugation, the HDL fraction was delipidated with acetone/ethanol (1:1, v/v) [22]. Apolipoproteins were resolved in 6 M urea solution, subjected to preparative SDS-PAGE, and stained with Coomassie brilliant blue.…”

Section: Determination Of N-terminal Amino Acid Sequencementioning

confidence: 99%

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Bovine Paraoxonase 1 Activities in Serum and Distribution in Lipoproteins

et al. 2005

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ABSTRACT. Paraoxonase 1 (PON1) is an enzyme associated with high-density lipoprotein (HDL) and has a protective effect against oxidation of lipoproteins in mammals. We investigated PON1 enzyme activities in bovine serum and its distribution among bovine serum lipoproteins. Paraoxonase activity and arylesterase activity in serum (152 Holstein cows and 42 Japanese Blacks) were 275 ± 55 U/ml and 130 ± 27 U/ml (mean ± SD), respectively. There was a high correlation (r=0.962) between the two enzyme activities, and the activity ratio of paraoxonase/arylesterase did not exhibit individual variation. More than 85% of both paraoxonase and arylesterase activities were detected in the HDL fraction separated by ultracentrifugation. The 43-kDa protein in the HDL fraction was identified as bovine PON1 by N-terminal amino acid sequence analysis. Bovine PON1 was purified by ultracentrifugation and preparative sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and an anti-bovine PON1 antiserum was developed. The concentration of PON1 protein determined by immunoblotting was closely correlated (r=0.976) with paraoxonase activity in serum. Bovine HDL was further fractionated into subpopulations, and the distribution of PON1 was examined. Paraoxonase activity and PON1 protein increased with decreasing HDL size and approximately 60% of total paraoxonase activity was distributed in the heavy HDL fraction. The different distributions of PON1 among HDL subpopulations might be concerned to the function and metabolism of bovine HDL. KEY WORDS: arylesterase, cattle, high-density lipoprotein, paraoxonase.

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“…ELISA: The ELISA was essentially performed as described for apoE, with modifications [23]. Samples were diluted with PBS or 1 M urea solution.…”

Section: Animalsmentioning

confidence: 99%

Enzyme-Linked Immunosorbent Assay for Bovine Apolipoprotein A-IV

Takahashi

Konishi

Sato

et al. 2004

The Journal of Veterinary Medical Science

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ABSTRACT. The present report describes an enzyme-linked immunosorbent assay for bovine apolipoprotein (apo) A-IV. This assay was applied to the determination of its concentration and distribution in sera from cattle. The distribution of apoA-IV in lipoprot ein fractions separated by ultracentrifugation was mostly recovered in the non-lipoprotein fractions (d>1.21 g/ml, 90%), but, in the case of gel filtration chromatography, apoA-IV was mainly eluted in HDL and non-lipoprotein fractions. The apoA-IV concentrations during early, mid-a nd late lactating stages in cows were significantly higher than during the nonlactating stage (p<0.05). From early to late lactating stages, the concentration of apoA-IV was unaltered. After 4 days of fasting, the concentration of plasma apoA-IV had decreased significantly (p<0.05) at days 3 and 4, and was returned to the basal level by 3 days of refeeding. These results suggested that the concentration of apoA-IV is modified by nutritional conditions. KEY WORDS: apolipoprotein A-IV, bovine, ELISA, lipoprotein.

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Bovine Apolipoprotein E in Plasma: Increase of ApoE Concentration Induced by Fasting and Distribution in Lipoprotein Fractions.

Cited by 11 publications

References 30 publications

Adipose-Derived Factors During Nutritional Transitions

Adipose-Derived Factors During Nutritional Transitions

Bovine Paraoxonase 1 Activities in Serum and Distribution in Lipoproteins

Enzyme-Linked Immunosorbent Assay for Bovine Apolipoprotein A-IV

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