| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH |
|
|
|
|||||||
|
|||||||||
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
1 Lab Genetics & Molec Cardiology/Medicine-LIM13, Heart Institute (InCor)/University of Sao Paulo Medical School, Sao Paulo, SP, Brazil
2 Thomson Mass Spectrometry Laboratory, Institute of Chemistry/State University of Campinas, Campinas, SP, Brazil
3 Department of Histology and Embryology, Institute of Biomedical Sciences/University of Sao Paulo, Sao Paulo, SP, Brazil
4 Department of Pathology, The University of North Carolina, Chapel Hill, NC, USA
* To whom correspondence should be addressed. E-mail: krieger{at}incor.usp.br.
Mice harboring 1, 2, or 3 copies of the ACE gene were used to evaluate the quantitative role of the ACE locus on obesity. Three-copy mice fed with a high-fat diet had lower body weight and periepididymal adipose tissue than did 1- and 2-copy mice (P<0.05). On regular chow, 3-copy mice had to eat more to maintain the same body weight; on a high-fat diet, they ate the same but weighed less than 1- and 2-copy mice (P<0.05), indicating a higher metabolic rate in 3-copy mice that was not affected by Ang II AT1 blocker treatment. A catalytically inactive form of EP24.15 was used to isolate ACE substrates from adipose tissue. LC-ESI-MS/MS identified 162 peptide peaks; 16 peptides were present in both groups (1- and 3-copy mice fed with a high-fat diet), while 58 of the 72 unique peptides were found only in the 3-copy mice. Peptide size distribution was shifted to lower molecular weight in 3-copy mice. Two of the identified peptides, LVVYPWTQRY and VVYPWTQRY, which are ACE substrates, inhibited in vitro protein kinase C phosphorylation in a concentration-dependent manner. In addition, neurolysin (EP24.16) activity was lower in fat tissue from 3- vs. 1-copy mice (P<0.05). Taken together, these results provide evidence that ACE is associated with body weight and periepididymal fat accumulation. This response may involve the generation of oligopeptides that inhibit the activity of EP24.16 and other oligopeptidases within the adipose tissue.
This article has been cited by other articles:
|
|
 |
|
  F. M. Cunha, D. A. Berti, Z. S. Ferreira, C. F. Klitzke, R. P. Markus, and E. S. Ferro Intracellular Peptides as Natural Regulators of Cell Signaling J. Biol. Chem., September 5, 2008; 283(36): 24448 - 24459. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 A. S. Heimann, I. Gomes, C. S. Dale, R. L. Pagano, A. Gupta, L. L. de Souza, A. D. Luchessi, L. M. Castro, R. Giorgi, V. Rioli, et al. Hemopressin is an inverse agonist of CB1 cannabinoid receptors PNAS, December 18, 2007; 104(51): 20588 - 20593. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 A. Muthumala, H. Montgomery, J. Palmen, J. A. Cooper, and S. E. Humphries Angiotensin-Converting Enzyme Genotype Interacts With Systolic Blood Pressure to Determine Coronary Heart Disease Risk in Healthy Middle-Aged Men Hypertension, August 1, 2007; 50(2): 348 - 353. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 M. Liang and B. Ventura Physiological genomics in PG and beyond: July to September 2005 Physiol Genomics, October 17, 2005; 23(2): 119 - 124. [Full Text] [PDF]
|
|
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH |
| Visit Other APS Journals Online |
