Neurochemical Evidence that Pristanic Acid Impairs Energy Production and Inhibits Synaptic Na+, K+-ATPase Activity in Brain of Young Rats

Abstract Acetylcholinesterase (AChE), Na+, K+-ATPase and Mg2+-ATPase activities were estimated in homogenised rat pituitary and hypothalamus of 4-and 22-month-old rats. AChE activity was not altered in the pituitary of aged com pared to adult rats, while it was found decreased by about 40% in the hypothalamus. Na+,K+-ATPase activity remained stable in the hypothalamus, while it was decreased by about 38% in the pituitary. Mg2+-ATPase activity remained unchanged in the hypothalamus, but was increased by about 83% in the pituitary. This pituitary Na+, K+-ATPase inactivation may result in pathological mood and decreased neural excitability and metabolic energy production in aged animals.The age-related alterations of AChE , Na+, K+-ATPase and Mg2+-ATPase activities may reflect changes in secretion and responses of some hormones of pituitary and hypothalamus.

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Pristanic Acid Provokes Lipid, Protein, and DNA Oxidative Damage and Reduces the Antioxidant Defenses in Cerebellum of Young Rats

The Cerebellum ◽

10.1007/s12311-014-0593-0 ◽

2014 ◽

Vol 13 (6) ◽

pp. 751-759 ◽

Cited By ~ 5

Author(s):

Estela Natacha Brandt Busanello ◽

Vannessa Gonçalves Araujo Lobato ◽

Ângela Zanatta ◽

Clarissa Günther Borges ◽

Anelise Miotti Tonin ◽

...

Keyword(s):

Oxidative Damage ◽

Antioxidant Defenses ◽

Pristanic Acid ◽

Dna Oxidative Damage ◽

Young Rats

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In vivo and in vitro effects of homocysteine on Na + ,K + ‐ATPase activity in parietal, prefrontal and cingulate cortex of young rats

International Journal of Developmental Neuroscience ◽

10.1016/j.ijdevneu.2004.05.007 ◽

2004 ◽

Vol 22 (4) ◽

pp. 185-190 ◽

Cited By ~ 33

Author(s):

Cristiane Matté ◽

Siomara C. Monteiro ◽

Thiago Calcagnotto ◽

Caren S. Bavaresco ◽

Carlos Alexandre Netto ◽

...

Keyword(s):

Atpase Activity ◽

Cingulate Cortex ◽

Young Rats ◽

In Vitro Effects

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In vitro evidence that phytanic acid compromises Na+,K+-ATPase activity and the electron flow through the respiratory chain in brain cortex from young rats

Brain Research ◽

10.1016/j.brainres.2010.07.012 ◽

2010 ◽

Vol 1352 ◽

pp. 231-238 ◽

Cited By ~ 17

Author(s):

Estela Natacha Brandt Busanello ◽

Carolina Maso Viegas ◽

Alana Pimentel Moura ◽

Anelise Miotti Tonin ◽

Mateus Grings ◽

...

Keyword(s):

Atpase Activity ◽

Respiratory Chain ◽

Phytanic Acid ◽

Brain Cortex ◽

Electron Flow ◽

Young Rats ◽

Flow Through

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Neurochemical Evidence that Lysine Inhibits Synaptic Na+,K+-ATPase Activity and Provokes Oxidative Damage in Striatum of Young Rats In vivo

Neurochemical Research ◽

10.1007/s11064-010-0302-4 ◽

2010 ◽

Vol 36 (2) ◽

pp. 205-214 ◽

Cited By ~ 9

Author(s):

Bianca Seminotti ◽

Carolina Gonçalves Fernandes ◽

Guilhian Leipnitz ◽

Alexandre Umpierrez Amaral ◽

Ângela Zanatta ◽

...

Keyword(s):

Oxidative Damage ◽

Atpase Activity ◽

Young Rats

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Peripheral proteins and smooth membrane from erythrocyte ghosts. Segregation of ATP-utilizing enzymes into smooth membrane.

The Journal of Cell Biology ◽

10.1083/jcb.76.1.105 ◽

1978 ◽

Vol 76 (1) ◽

pp. 105-115 ◽

Cited By ~ 11

Author(s):

H Hayashi ◽

H W Jarrett ◽

J T Penniston

Keyword(s):

Atpase Activity ◽

Actin Filaments ◽

Energy Production ◽

Cooperative Interaction ◽

Erythrocyte Membranes ◽

Erythrocyte Ghosts ◽

Peripheral Proteins ◽

Smooth Membrane ◽

Integral Proteins ◽

Membranous Material

Erythrocytes and their isolated membranes display ATP-dependent endocytosis. To localize the enzymes responsible for this phenomenon, the erythrocyte membranes (ghosts) were fractionated under conditions which retained ATPase activity. Fractionation of the ghosts resulted in three fractions: spectrin-actin, the peripheral proteins soluble in high salt, and the smooth membrane containing integral proteins. On the average, 87% of the protein and 88% of the phosphorus of the original ghosts were recovered in these fractions, and all of the kinds of ATP-splitting activities of the membrane were recovered in the smooth membrane. A tiny ATPase activity, detectable by special methodology in spectrinactin, could have been due to contamination with membranous material. Although the purified spectrin-actin did not have a significant ATPase of its own, it stimulated the Ca2+, Mg2+-ATPase of the smooth membrane significantly, suggesting a cooperative interaction between these two fractions. This segregation of the ATPase activities into the smooth membrane, combined with the energy dependence of endocytosis, showed that the smooth membrane must be involved in the energy production for endocytosis. The possibility that the spectrin-actin filaments cooperate with a myosinlike ATPase in the membrane to generate membrane movements is discussed.

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