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L-amino acid sensing by CaSR and Physiological Impact on Mice.

Larsson, Anna LU (2014) KBK820 20142
Pure and Applied Biochemistry
Abstract
After localizing of the extracellular calcium sensing receptor (CaSR) throughout the gastrointestinal tract, free aromatic L-amino acids have been found to act as positive allosteric modulators suggesting the CaSR is a potential mediator in protein digestion. The binding site for L-amino acids in the CaSR is located in the venus flytrap domain (VFD). Point mutations on residue Thr-145 and Ser-170 in the venus flytrap domain (VFD), holding binding site(s) for L-amino acids, together, stereo selectively impairs and disables L-amino acid sensing while leaving Ca2+-sensing intact. In this study, we investigated if knock-in mice (KI) with double mutation T145A/S170T in the CaSR leads to increased food intake and weight gain due to probable... (More)
After localizing of the extracellular calcium sensing receptor (CaSR) throughout the gastrointestinal tract, free aromatic L-amino acids have been found to act as positive allosteric modulators suggesting the CaSR is a potential mediator in protein digestion. The binding site for L-amino acids in the CaSR is located in the venus flytrap domain (VFD). Point mutations on residue Thr-145 and Ser-170 in the venus flytrap domain (VFD), holding binding site(s) for L-amino acids, together, stereo selectively impairs and disables L-amino acid sensing while leaving Ca2+-sensing intact. In this study, we investigated if knock-in mice (KI) with double mutation T145A/S170T in the CaSR leads to increased food intake and weight gain due to probable decreased secretions of anorectic hormones and hence decreased sensation of fullness. Comparison with wild-type (WT) mice showed KI-mice weighed significantly more after nine weeks of age (p < 0.001) and consumed more feed when given a diet with casein-based protein content (p < 0.01). The present data suggest that the CaSR may serve as a potential regulator and mediator in dietary protein and food intake regulation, making it a potential therapeutic target in treating obesity. (Less)
Please use this url to cite or link to this publication:
author
Larsson, Anna LU
supervisor
organization
course
KBK820 20142
year
type
H2 - Master's Degree (Two Years)
subject
keywords
Calcium Sensing Receptor, L-Amino Acids, Protein-Leverage Hypothesis
language
English
id
4732901
date added to LUP
2014-12-19 12:39:38
date last changed
2015-01-22 18:03:59
@misc{4732901,
  abstract     = {{After localizing of the extracellular calcium sensing receptor (CaSR) throughout the gastrointestinal tract, free aromatic L-amino acids have been found to act as positive allosteric modulators suggesting the CaSR is a potential mediator in protein digestion. The binding site for L-amino acids in the CaSR is located in the venus flytrap domain (VFD). Point mutations on residue Thr-145 and Ser-170 in the venus flytrap domain (VFD), holding binding site(s) for L-amino acids, together, stereo selectively impairs and disables L-amino acid sensing while leaving Ca2+-sensing intact. In this study, we investigated if knock-in mice (KI) with double mutation T145A/S170T in the CaSR leads to increased food intake and weight gain due to probable decreased secretions of anorectic hormones and hence decreased sensation of fullness. Comparison with wild-type (WT) mice showed KI-mice weighed significantly more after nine weeks of age (p < 0.001) and consumed more feed when given a diet with casein-based protein content (p < 0.01). The present data suggest that the CaSR may serve as a potential regulator and mediator in dietary protein and food intake regulation, making it a potential therapeutic target in treating obesity.}},
  author       = {{Larsson, Anna}},
  language     = {{eng}},
  note         = {{Student Paper}},
  title        = {{L-amino acid sensing by CaSR and Physiological Impact on Mice.}},
  year         = {{2014}},
}