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Pancreatic lipase-colipase binds strongly to the thylakoid membrane surface.

Emek, Sinan Cem LU ; Åkerlund, Hans-Erik LU ; Erlanson-Albertsson, Charlotte LU and Albertsson, Per-Åke LU (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)
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author
; ; and
organization
publishing date
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
2020-06-24 01:34:46
@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},
}