|
Journal of Lipid Research, Vol. 42, 1187-1196, August 2001
Copyright © 2001 by Lipid Research, Inc.
Immunochemical detection of a lipofuscin-like fluorophore derived from malondialdehyde and lysine
Satoshi Yamadaa,
Shigenori Kumazawab,
Takeshi Ishiib,
Tsutomu Nakayamab,
Koichi Itakurac,
Noriyuki Shibatad,
Makio Kobayashid,
Kensuke Sakaie,
Toshihiko Osawae, and
Koji Uchidae
a Tsukuba Research Laboratory, NOF Company, Tsukuba 300-2635, Japan
b Department of Food and Nutritional Sciences, University of Shizuoka, Shizuoka 422-8529, Japan
c Faculty of Education, Aichi University of Education, Kariya 448, Japan
d Department of Pathology, Tokyo Women's Medical University, Tokyo 162-8666, Japan
e Laboratory of Food and Biodynamics, Graduate School of Bioagricultural Sciences, Nagoya University, Nagoya 464-8601, Japan
Correspondence to:
Koji Uchida, To whom correspondence should be addressed., uchidak{at}agr.nagoya-u.ac.jp (E-mail)
The accumulation of fluorescent age pigment or lipofuscin is a frequently observed age-associated cellular alteration in a variety of postmitotic cells of many species. These pigments are observed within granules composed, in part, of damaged protein and lipid. Modification of various biomolecules by aldehyde products of lipid peroxidation is believed to contribute to lipofuscin and ceroid formation. In the present study, we raised a monoclonal antibody (MAb 1F83) directed to the malondialdehyde-modified protein and identified a lipofuscin-like dihydropyridine fluorophore as the major epitope. This antibody was used to conclusively demonstrate that the fluorophore forms on oxidatively modified low density lipoproteins. In addition, we demonstrated that the materials immunoreactive to MAb 1F83 indeed constituted the atherosclerotic lesions, in which intense positivity was associated primarily with macrophage-derived foam cells.
The results of this study suggest that the reaction between the lipid peroxidation-derived aldehyde and primary amino groups of protein might represent a process common to the formation of the lipofuscin-like fluorophore during aging and its related diseases. Yamada, S., S. Kumazawa, T. Ishii, T. Nakayama, K. Itakura, N. Shibata, M. Kobayashi, K. Sakai, T. Osawa, and K. Uchida. Immunochemical detection of a lipofuscin-like fluorophore derived from malondialdehyde and lysine. J. Lipid Res. 2001. 42: 1187;1196.
Supplementary key words:
lipid peroxidation, protein modification, dihydropyridine, monoclonal antibody

CiteULike Complore Connotea Del.icio.us Digg Reddit Technorati What's this?
This article has been cited by other articles:

|
 |

|
 |
 
J. N. Baumgardner, K. Shankar, L. Hennings, E. Albano, T. M. Badger, and M. J. J. Ronis
N-Acetylcysteine Attenuates Progression of Liver Pathology in a Rat Model of Nonalcoholic Steatohepatitis
J. Nutr.,
October 1, 2008;
138(10):
1872 - 1879.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
N. Shanmugam, J. L. Figarola, Y. Li, P. M. Swiderski, S. Rahbar, and R. Natarajan
Proinflammatory Effects of Advanced Lipoxidation End Products in Monocytes
Diabetes,
April 1, 2008;
57(4):
879 - 888.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
E Albano, E Mottaran, M Vidali, E Reale, S Saksena, G Occhino, A D Burt, and C P Day
Immune response towards lipid peroxidation products as a predictor of progression of non-alcoholic fatty liver disease to advanced fibrosis
Gut,
July 1, 2005;
54(7):
987 - 993.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
N. Traverso, S. Menini, E. P. Maineri, S. Patriarca, P. Odetti, D. Cottalasso, U. M. Marinari, and M. A. Pronzato
Malondialdehyde, a Lipoperoxidation-Derived Aldehyde, Can Bring About Secondary Oxidative Damage To Proteins
J. Gerontol. A Biol. Sci. Med. Sci.,
September 1, 2004;
59(9):
B890 - B895.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
D. A. Slatter, N. C. Avery, and A. J. Bailey
Identification of a New Cross-link and Unique Histidine Adduct from Bovine Serum Albumin Incubated with Malondialdehyde
J. Biol. Chem.,
January 2, 2004;
279(1):
61 - 69.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
Y. Kawai, A. Saito, N. Shibata, M. Kobayashi, S. Yamada, T. Osawa, and K. Uchida
Covalent Binding of Oxidized Cholesteryl Esters to Protein: IMPLICATIONS FOR OXIDATIVE MODIFICATION OF LOW DENSITY LIPOPROTEIN AND ATHEROSCLEROSIS
J. Biol. Chem.,
May 30, 2003;
278(23):
21040 - 21049.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
M. Kondo, T. Shibata, T. Kumagai, T. Osawa, N. Shibata, M. Kobayashi, S. Sasaki, M. Iwata, N. Noguchi, and K. Uchida
15-Deoxy-Delta 12,14-prostaglandin J2: The endogenous electrophile that induces neuronal apoptosis
PNAS,
May 28, 2002;
99(11):
7367 - 7372.
[Abstract]
[Full Text]
[PDF]
|
 |
|
Copyright © 2001 by the American Society for Biochemistry and Molecular Biology.
|
Advertisement
Advertisement
|