Substantial species differences in relation to formation and degradation of N-acyl-ethanolamine phospholipids in heart tissue: An enzyme activity study

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Substantial species differences in relation to formation and degradation of N-acyl-ethanolamine phospholipids in heart tissue : An enzyme activity study. / Moesgaard, B.; Petersen, G.; Hansen, Harald S.; Mortensen, S.A.

In: Comparative Biochemistry and Physiology - Part B: Biochemistry & Molecular Biology, Vol. 131, No. 3, 01.01.2002, p. 475-482.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Moesgaard, B, Petersen, G, Hansen, HS & Mortensen, SA 2002, 'Substantial species differences in relation to formation and degradation of N-acyl-ethanolamine phospholipids in heart tissue: An enzyme activity study', Comparative Biochemistry and Physiology - Part B: Biochemistry & Molecular Biology, vol. 131, no. 3, pp. 475-482. https://doi.org/10.1016/S1096-4959(02)00003-9

APA

Moesgaard, B., Petersen, G., Hansen, H. S., & Mortensen, S. A. (2002). Substantial species differences in relation to formation and degradation of N-acyl-ethanolamine phospholipids in heart tissue: An enzyme activity study. Comparative Biochemistry and Physiology - Part B: Biochemistry & Molecular Biology, 131(3), 475-482. https://doi.org/10.1016/S1096-4959(02)00003-9

Vancouver

Moesgaard B, Petersen G, Hansen HS, Mortensen SA. Substantial species differences in relation to formation and degradation of N-acyl-ethanolamine phospholipids in heart tissue: An enzyme activity study. Comparative Biochemistry and Physiology - Part B: Biochemistry & Molecular Biology. 2002 Jan 1;131(3):475-482. https://doi.org/10.1016/S1096-4959(02)00003-9

Author

Moesgaard, B. ; Petersen, G. ; Hansen, Harald S. ; Mortensen, S.A. / Substantial species differences in relation to formation and degradation of N-acyl-ethanolamine phospholipids in heart tissue : An enzyme activity study. In: Comparative Biochemistry and Physiology - Part B: Biochemistry & Molecular Biology. 2002 ; Vol. 131, No. 3. pp. 475-482.

Bibtex

@article{aaa174801883418b86df4a613637f92f,
title = "Substantial species differences in relation to formation and degradation of N-acyl-ethanolamine phospholipids in heart tissue: An enzyme activity study",
abstract = "The formation of N-acyl-ethanolamines (NAEs), including the cannabinoid receptor ligand anandamide, and their precursors N-acyl-ethanolamine phospholipids (NAPEs) are catalyzed by NAPE-hydrolyzing phospholipase D (NAPE-PLD) and N-acyl-transferase, respectively. NAPE and NAE are suggested to have beneficial effects on the heart, but in the literature there are indications of species differences in the activity of these enzymes. We have examined heart microsomes from rats, mice, guinea pigs, rabbits, frogs, cows, dogs, cats, mini pigs and human beings for activities of these two enzymes. N-Acyl-transferase activity was very high in dogs and cats (>13 pmol/min/mg protein) whereas it was very low to barely detectable in the other species (45 pmol/min/mg protein) whereas it was 9 pmol/min/mg protein in frogs and below that in the other species. The ratio of activity between the two enzymes varied from 0.002 to 15 in the investigated species. The activity of the two enzymes in rat hearts as opposed to rat brain did not change during development. These results indicate that there may be substantial species differences in the generation of anandamide and other NAEs as well as NAPEs in heart tissues.",
author = "B. Moesgaard and G. Petersen and Hansen, {Harald S.} and S.A. Mortensen",
year = "2002",
month = jan,
day = "1",
doi = "10.1016/S1096-4959(02)00003-9",
language = "English",
volume = "131",
pages = "475--482",
journal = "Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology",
issn = "1096-4959",
publisher = "Elsevier",
number = "3",

}

RIS

TY - JOUR

T1 - Substantial species differences in relation to formation and degradation of N-acyl-ethanolamine phospholipids in heart tissue

T2 - An enzyme activity study

AU - Moesgaard, B.

AU - Petersen, G.

AU - Hansen, Harald S.

AU - Mortensen, S.A.

PY - 2002/1/1

Y1 - 2002/1/1

N2 - The formation of N-acyl-ethanolamines (NAEs), including the cannabinoid receptor ligand anandamide, and their precursors N-acyl-ethanolamine phospholipids (NAPEs) are catalyzed by NAPE-hydrolyzing phospholipase D (NAPE-PLD) and N-acyl-transferase, respectively. NAPE and NAE are suggested to have beneficial effects on the heart, but in the literature there are indications of species differences in the activity of these enzymes. We have examined heart microsomes from rats, mice, guinea pigs, rabbits, frogs, cows, dogs, cats, mini pigs and human beings for activities of these two enzymes. N-Acyl-transferase activity was very high in dogs and cats (>13 pmol/min/mg protein) whereas it was very low to barely detectable in the other species (45 pmol/min/mg protein) whereas it was 9 pmol/min/mg protein in frogs and below that in the other species. The ratio of activity between the two enzymes varied from 0.002 to 15 in the investigated species. The activity of the two enzymes in rat hearts as opposed to rat brain did not change during development. These results indicate that there may be substantial species differences in the generation of anandamide and other NAEs as well as NAPEs in heart tissues.

AB - The formation of N-acyl-ethanolamines (NAEs), including the cannabinoid receptor ligand anandamide, and their precursors N-acyl-ethanolamine phospholipids (NAPEs) are catalyzed by NAPE-hydrolyzing phospholipase D (NAPE-PLD) and N-acyl-transferase, respectively. NAPE and NAE are suggested to have beneficial effects on the heart, but in the literature there are indications of species differences in the activity of these enzymes. We have examined heart microsomes from rats, mice, guinea pigs, rabbits, frogs, cows, dogs, cats, mini pigs and human beings for activities of these two enzymes. N-Acyl-transferase activity was very high in dogs and cats (>13 pmol/min/mg protein) whereas it was very low to barely detectable in the other species (45 pmol/min/mg protein) whereas it was 9 pmol/min/mg protein in frogs and below that in the other species. The ratio of activity between the two enzymes varied from 0.002 to 15 in the investigated species. The activity of the two enzymes in rat hearts as opposed to rat brain did not change during development. These results indicate that there may be substantial species differences in the generation of anandamide and other NAEs as well as NAPEs in heart tissues.

UR - http://www.scopus.com/inward/record.url?scp=0036186465&partnerID=8YFLogxK

U2 - 10.1016/S1096-4959(02)00003-9

DO - 10.1016/S1096-4959(02)00003-9

M3 - Journal article

AN - SCOPUS:0036186465

VL - 131

SP - 475

EP - 482

JO - Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology

JF - Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology

SN - 1096-4959

IS - 3

ER -

ID: 45562203