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Lipoperoxidation of rod outer segments of bovine retina is inhibited by soluble binding proteins for fatty acids

Authors
  • Terrasa, A.1
  • Guajardo, M.1
  • Catalá, A.1
  • 1 Universidad Nacional de La Plata, Cátedra de Bioquímica, Facultad de Ciencias Veterinarias, La Plata, 1900, Argentina , La Plata
Type
Published Article
Journal
Molecular and Cellular Biochemistry
Publisher
Springer-Verlag
Publication Date
Jan 01, 1998
Volume
178
Issue
1-2
Pages
181–186
Identifiers
DOI: 10.1023/A:1006839413757
Source
Springer Nature
Keywords
License
Yellow

Abstract

In the present study it was investigated if soluble-binding proteins for fatty acids (FABPs) present in neural retina show protection from in vitro lipoperoxidation of rod outer segment membranes (ROS). After incubation of ROS in an ascorbate-Fe++ system, at 37°C during 90-120 min, the total cpm originated from light emission (chemiluminescence) was found to be lower in those membranes incubated in the presence of soluble binding proteins for fatty acids. The fatty acid composition of rod outer segment membranes was substantially modified when subjected to non-enzymatic lipoperoxidation with a considerable decrease of docosahexaenoic acid (22:6 n-3) and arachidonic acid (20:4 n-6). As a result of this, the unsaturation index, a parameter based on the maximal rate of oxidation of specific fatty acids was higher in the native and control membranes when compared with peroxidized ones. A similar decrease of chemiluminescence was observed with the addition of increasing concentrations of native or delipidated FABP retinal containing fractions to rod outer segment membranes. These results indicate that soluble proteins with fatty acid binding properties may act as antioxidant protecting rod outer segment membranes from deleterious effect.

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