Quantitative histochemical study of cytochrome oxidase in the dLGN of aging rats. 1996

F Díaz, and A Villena, and V Requena, and P González, and A Peláez, and I Pérez de Vargas
Department of Normal and Pathological Morphology, Faculty of Medicine, University of Málaga, Spain.

We carried out a quantitative histochemical study of the enzyme cytochrome oxidase (CO) in neurons of the dorsal lateral geniculate nucleus (dLGN) of male Wistar rats aged 3, 18, 24 and 28 months. The results show that the activity of cytochrome oxidase decreases significantly between 24 and 28 months. We also checked whether a correlation existed between neuronal size and enzymatic activity. Low correlation coefficients were obtained which were between 0.4139 at 3 months 0.2092 at 28 months. Nevertheless, we observed a certain relationship between both parameters, and therefore we classified the neurons as light, moderate and dark according to their optical density, which correlates with enzyme cytochrome oxidase activity, and as small, medium and large depending on their size. We found that light neurons were scarcely represented in the dLGN. At the age of 3 months, the most frequent neurons were moderate, medium-size ones, and dark, small ones. The population of moderate neurons increased with age, reaching 74.5% at the 28th month, 52.2% of which corresponded to medium-size neurons. In the same group dark neurons decreased, falling to a total of 15.3% made up of medium and large-size ones. These results could be interpreted as reflecting a decrease in the bioenergetic competence of the neurons of this nucleus in old age.

UI MeSH Term Description Entries
D008297 Male Males
D003576 Electron Transport Complex IV A multisubunit enzyme complex containing CYTOCHROME A GROUP; CYTOCHROME A3; two copper atoms; and 13 different protein subunits. It is the terminal oxidase complex of the RESPIRATORY CHAIN and collects electrons that are transferred from the reduced CYTOCHROME C GROUP and donates them to molecular OXYGEN, which is then reduced to water. The redox reaction is simultaneously coupled to the transport of PROTONS across the inner mitochondrial membrane. Cytochrome Oxidase,Cytochrome aa3,Cytochrome-c Oxidase,Cytochrome Oxidase Subunit III,Cytochrome a,a3,Cytochrome c Oxidase Subunit VIa,Cytochrome-c Oxidase (Complex IV),Cytochrome-c Oxidase Subunit III,Cytochrome-c Oxidase Subunit IV,Ferrocytochrome c Oxygen Oxidoreductase,Heme aa3 Cytochrome Oxidase,Pre-CTOX p25,Signal Peptide p25-Subunit IV Cytochrome Oxidase,Subunit III, Cytochrome Oxidase,p25 Presequence Peptide-Cytochrome Oxidase,Cytochrome c Oxidase,Cytochrome c Oxidase Subunit III,Cytochrome c Oxidase Subunit IV,Oxidase, Cytochrome,Oxidase, Cytochrome-c,Signal Peptide p25 Subunit IV Cytochrome Oxidase,p25 Presequence Peptide Cytochrome Oxidase
D006651 Histocytochemistry Study of intracellular distribution of chemicals, reaction sites, enzymes, etc., by means of staining reactions, radioactive isotope uptake, selective metal distribution in electron microscopy, or other methods. Cytochemistry
D000375 Aging The gradual irreversible changes in structure and function of an organism that occur as a result of the passage of time. Senescence,Aging, Biological,Biological Aging
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D017208 Rats, Wistar A strain of albino rat developed at the Wistar Institute that has spread widely at other institutions. This has markedly diluted the original strain. Wistar Rat,Rat, Wistar,Wistar Rats
D051381 Rats The common name for the genus Rattus. Rattus,Rats, Laboratory,Rats, Norway,Rattus norvegicus,Laboratory Rat,Laboratory Rats,Norway Rat,Norway Rats,Rat,Rat, Laboratory,Rat, Norway,norvegicus, Rattus

Related Publications

F Díaz, and A Villena, and V Requena, and P González, and A Peláez, and I Pérez de Vargas
January 1968, Arkhiv patologii,
F Díaz, and A Villena, and V Requena, and P González, and A Peláez, and I Pérez de Vargas
December 1989, Acta ophthalmologica,
F Díaz, and A Villena, and V Requena, and P González, and A Peláez, and I Pérez de Vargas
September 1993, Brain research,
F Díaz, and A Villena, and V Requena, and P González, and A Peláez, and I Pérez de Vargas
November 1994, Neuroscience,
F Díaz, and A Villena, and V Requena, and P González, and A Peláez, and I Pérez de Vargas
December 1995, Metabolic brain disease,
F Díaz, and A Villena, and V Requena, and P González, and A Peláez, and I Pérez de Vargas
December 1960, Oral surgery, oral medicine, and oral pathology,
F Díaz, and A Villena, and V Requena, and P González, and A Peláez, and I Pérez de Vargas
May 2001, Histochemistry and cell biology,
F Díaz, and A Villena, and V Requena, and P González, and A Peláez, and I Pérez de Vargas
January 1977, Neirofiziologiia = Neurophysiology,
F Díaz, and A Villena, and V Requena, and P González, and A Peláez, and I Pérez de Vargas
January 1966, Acta ophthalmologica,
F Díaz, and A Villena, and V Requena, and P González, and A Peláez, and I Pérez de Vargas
January 1967, Arkhiv patologii,
Copied contents to your clipboard!