Pancreatic lipase-colipase binds strongly to the thylakoid membrane surface.
(2013) In Journal of the Science of Food and Agriculture 93(9). p.2254-2258- Abstract
- BACKGROUND: Isolated thylakoid membranes, i.e. the photosynthetic membranes of green leaves, inhibit the activity of pancreatic lipase and colipase during hydrolysis of fat in vitro. This inhibition has been demonstrated to cause reduced food intake and improved hormonal and lipid profile in vivo. One of the reasons suggested for the inhibiting effect is binding of lipase-colipase to the thylakoid membrane surface. This prompted a study of the binding of lipase and colipase to thylakoids. RESULTS: The results showed that lipase and colipase strongly bind to the thylakoid membrane surface. The dissociation constant was determined at 1.2 × 10(-8) mol L(-1) ; binding decreased after treatment of thylakoids with pepsin/trypsin to 1.0 × 10(-7)... (More)
- BACKGROUND: Isolated thylakoid membranes, i.e. the photosynthetic membranes of green leaves, inhibit the activity of pancreatic lipase and colipase during hydrolysis of fat in vitro. This inhibition has been demonstrated to cause reduced food intake and improved hormonal and lipid profile in vivo. One of the reasons suggested for the inhibiting effect is binding of lipase-colipase to the thylakoid membrane surface. This prompted a study of the binding of lipase and colipase to thylakoids. RESULTS: The results showed that lipase and colipase strongly bind to the thylakoid membrane surface. The dissociation constant was determined at 1.2 × 10(-8) mol L(-1) ; binding decreased after treatment of thylakoids with pepsin/trypsin to 1.0 × 10(-7) and to 0.6 × 10(-7) mol L(-1) after treatment with pancreatic juice. Similarly, delipidation of thylakoids caused a decrease in binding, the dissociation constant being 2.0 × 10(-7) mol L(-1) . CONCLUSION: The binding of pancreatic lipase-colipase to the thylakoid membrane is strong and may explain the inhibition of lipase-colipase activity by thylakoids. After treatment with proteases to mimic intestinal digestion binding is decreased, but is still high enough to explain the observed metabolic effects of thylakoids in vivo. © 2013 Society of Chemical Industry. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/3438221
- author
- Emek, Sinan Cem LU ; Åkerlund, Hans-Erik LU ; Erlanson-Albertsson, Charlotte LU and Albertsson, Per-Åke LU
- organization
- publishing date
- 2013
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Journal of the Science of Food and Agriculture
- volume
- 93
- issue
- 9
- pages
- 2254 - 2258
- publisher
- Wiley-Blackwell
- external identifiers
-
- wos:000319875500024
- pmid:23355304
- scopus:84878734504
- pmid:23355304
- ISSN
- 1097-0010
- DOI
- 10.1002/jsfa.6034
- language
- English
- LU publication?
- yes
- id
- b9aa3252-b348-43a5-96cd-87ebdc809c6d (old id 3438221)
- alternative location
- http://www.ncbi.nlm.nih.gov/pubmed/23355304?dopt=Abstract
- date added to LUP
- 2016-04-01 10:33:50
- date last changed
- 2022-04-04 19:20:41
@article{b9aa3252-b348-43a5-96cd-87ebdc809c6d,
abstract = {{BACKGROUND: Isolated thylakoid membranes, i.e. the photosynthetic membranes of green leaves, inhibit the activity of pancreatic lipase and colipase during hydrolysis of fat in vitro. This inhibition has been demonstrated to cause reduced food intake and improved hormonal and lipid profile in vivo. One of the reasons suggested for the inhibiting effect is binding of lipase-colipase to the thylakoid membrane surface. This prompted a study of the binding of lipase and colipase to thylakoids. RESULTS: The results showed that lipase and colipase strongly bind to the thylakoid membrane surface. The dissociation constant was determined at 1.2 × 10(-8) mol L(-1) ; binding decreased after treatment of thylakoids with pepsin/trypsin to 1.0 × 10(-7) and to 0.6 × 10(-7) mol L(-1) after treatment with pancreatic juice. Similarly, delipidation of thylakoids caused a decrease in binding, the dissociation constant being 2.0 × 10(-7) mol L(-1) . CONCLUSION: The binding of pancreatic lipase-colipase to the thylakoid membrane is strong and may explain the inhibition of lipase-colipase activity by thylakoids. After treatment with proteases to mimic intestinal digestion binding is decreased, but is still high enough to explain the observed metabolic effects of thylakoids in vivo. © 2013 Society of Chemical Industry.}},
author = {{Emek, Sinan Cem and Åkerlund, Hans-Erik and Erlanson-Albertsson, Charlotte and Albertsson, Per-Åke}},
issn = {{1097-0010}},
language = {{eng}},
number = {{9}},
pages = {{2254--2258}},
publisher = {{Wiley-Blackwell}},
series = {{Journal of the Science of Food and Agriculture}},
title = {{Pancreatic lipase-colipase binds strongly to the thylakoid membrane surface.}},
url = {{http://dx.doi.org/10.1002/jsfa.6034}},
doi = {{10.1002/jsfa.6034}},
volume = {{93}},
year = {{2013}},
}