| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
|
|
|
|||||||
|
|||||||||
Volume 272, Number 50, Issue of December 12, 1997
pp. 31362-31368
(Received for publication, July 25, 1997, and in revised form, September 25, 1997)
From the Several proteins found in retinal
photoreceptor cells (guanylate cyclase activating protein, protein
kinase A, recoverin, and transducin) are N-terminally modified with the
fatty acids 12:0, 14:0, 14:1n-9, and 14:2n-6,
whereas similar proteins in other tissues contain only 14:0. It has
been hypothesized that the acyl-CoA pool of the retina contains amounts
of 12:0, 14:1n-9, and 14:2n-6 elevated over
14:0, in comparison to other tissues, and this accounts for the
specificity of N-terminal fatty acylation. To test this hypothesis, we
performed fatty acid analysis on total acyl-CoAs purified from bovine
retina (light-adapted), heart, and liver. We also examined the
N- and S-linked fatty acid composition of the total protein
pools from these tissues. Acyl-CoAs were prepared from heart, liver,
and retina and separated by high performance liquid chromatography
(HPLC). Identities of peaks were based on HPLC of standard 12:0, 14:0,
14:1n-9, and 14:2n-6 CoAs. Total protein was
subjected to base hydrolysis followed by acidic methanolysis to release
S- and N-linked fatty acids, respectively, and fatty acid
phenacyl esters were prepared for HPLC analysis. Retina had levels of
12:0 (2.7 ± 2.1%), 14:1n-9 (2.9 ± 2.2%), and
14:2n-6 (1.6 ± 0.7%) CoAs below that of 14:0 CoA
(7.0 ± 1.8%). Likewise, heart levels of 14:2n-6 CoA
(3.7 ± 0.1%) were near and 12:0 (2.6 ± 0.6%) and
14:1n-9 (0.7 ± 0.3%) CoAs were below that of 14:0 CoA (3.8 ± 1.0%). Liver had levels of 12:0 (16.1 ± 5.7%)
and 14:2n-6 (8.1 ± 1.2%) CoAs above and
14:1n-9 CoA (1.2 ± 0.6%) below that of 14:0 CoA
(5.9 ± 0.8%). Fatty acid analysis of total protein showed that
all tissues contained S-linked 16:0, 18:0, and 18:1n-9. Retina proteins contained N-linked 14:0,
14:1n-9, and 14:2n-6, whereas heart and liver
had only 14:0. Our findings do not support the hypothesis that the CoA
ester pool of the retina is enriched with 12:0, 14:1n-9,
and 14:2n-6 over 14:0, in comparison to other tissues. This
suggests that alternative models must be considered for the regulation
of N-terminal fatty acylation of proteins in photoreceptor cells.
Identification and Quantitation of the Fatty Acids Composing the
CoA Ester Pool of Bovine Retina, Heart, and Liver
and
Department of Biochemistry, Baylor College
of Medicine, Houston, Texas 77030, the § Oklahoma Center
for Neuroscience and Departments of Ophthalmology and Biochemistry & Molecular Biology, University of Oklahoma Health Sciences Center,
Oklahoma City, Oklahoma 73104, and the ¶ Dean A. McGee Eye
Institute, Oklahoma City, Oklahoma 73104
CiteULike 
Complore 
Connotea 
Del.icio.us 
Digg 
Reddit 
Technorati What's this?
This article has been cited by other articles:
|
|
 |
|
  M. Y. Golovko and E. J. Murphy An improved method for tissue long-chain acyl-CoA extraction and analysis J. Lipid Res., September 1, 2004; 45(9): 1777 - 1782. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 Y. Hashimoto, T. Matsuda, Y. Matsuura, T. Haga, and Y. Fukada Production of N-Lauroylated G Protein {alpha}-Subunit in Sf9 Insect Cells: The Type of N-Acyl Group of G{alpha} Influences G Protein-Mediated Signal Transduction J. Biochem., March 1, 2004; 135(3): 319 - 329. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 O. W. Lindwasser and M. D. Resh Myristoylation as a target for inhibiting HIV assembly: Unsaturated fatty acids block viral budding PNAS, October 1, 2002; 99(20): 13037 - 13042. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 J. P. Chapple, A. J. Hardcastle, C. Grayson, L.A. Spackman, K. R. Willison, and M. E. Cheetham Mutations in the N-terminus of the X-linked retinitis pigmentosa protein RP2 interfere with the normal targeting of the protein to the plasma membrane Hum. Mol. Genet., August 12, 2000; 9(13): 1919 - 1926. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 X. Liang, A. Nazarian, H. Erdjument-Bromage, W. Bornmann, P. Tempst, and M. D. Resh Heterogeneous Fatty Acylation of Src Family Kinases with Polyunsaturated Fatty Acids Regulates Raft Localization and Signal Transduction J. Biol. Chem., August 10, 2001; 276(33): 30987 - 30994. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
T. M. Stulnig, J. Huber, N. Leitinger, E.-M. Imre, P. Angelisova, P. Nowotny, and W. Waldhausl Polyunsaturated Eicosapentaenoic Acid Displaces Proteins from Membrane Rafts by Altering Raft Lipid Composition J. Biol. Chem., September 28, 2001; 276(40): 37335 - 37340. [Abstract] [Full Text] [PDF]
|
|
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
| All ASBMB Journals | Molecular and Cellular Proteomics |
| Journal of Lipid Research | ASBMB Today |
