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Reactive oxygen species (ROS) induce DNA damage with the ensuing activation of the chromosomal repair enzyme poly(ADP-ribose) polymerase (PARP). ROS also interact with the function of carotid body chemoreceptor cells. The possibility arises that PARP is part of the carotid chemosensing process. This study seeks to determine the presence of PARP and its changes in response to contrasting chemical stimuli, hypoxia and hyperoxia, both capable of generating ROS, in cat carotid bodies. The organs were dissected from anesthetized cats exposed in vivo to acute normoxic (PaO290 mmHg), hypoxic (PaO225 mmHg), and hyperoxic (PaO2> 400 mmHg) conditions. Carotid body homogenate was the source of PARP and [adenine 14C] NAD was the substrate in the assay. Specimens of the superior cervical ganglion and brainstem were used as reference tissues. We found that PARP activity amounted to 27 pmol/mg protein/min in the normoxic carotid body. The activity level more than doubled in both hypoxic and hyperoxic carotid bodies. Changes of PARP in the reference tissues were qualitatively similar. We conclude that PARP is present in the carotid body but the augmentation of the enzyme activity in both hypoxia and hyperoxia reflects DNA damage, induced likely by ROS and being universal for neural tissues, rather than a specific involvement of PARP in the chemosensing process.
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Stability of ascorbyl palmitate molecule in the rat brain

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Recent investigations have shown the ability of ascorbyl palmitate (AP), a bioactive, lipid-soluble ester of ascorbic acid (AA), to penetrate neural tissues. This study seeks to determine the occurrence of hydrolysis of AP molecule in brain tissue, which could rather point to the action of AA alone carried over the biological barrier and then released from the AP compound. The integrity of AP molecule was examined qualitatively in the rat brain by thin-layer-chromatography. AP was injected into an internal carotid artery in a dose of 75 mg per rat after tying off the common and external carotid arteries at the same side. The rats were sacrificed 15 min later, the brain tissue was extracted with chloroform/methanol and chromatographed. The AP bands plated from the samples ispilateral to the injection side strictly corresponded to the AP standard's location and were clearly separated from the AA standard with no overlap. The experiment showed that AP resists hydrolysis in the brain and thus the short-term biological effects of AP may be ascribed to the action of an intact ester molecule. The results may help elucidate the biological action of AP, a compound that increasingly attracts attention for biomedical use due to its antioxidant potential and ability to penetrate into the membrane signaling target sites.
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