Drugs online research references
Biol Res. 1994;27(2):135-43.
Stress-induced hyperglycemia and hypoinsulinemia are suppressed by sulfonylurea. Predominant role of insulin.
Vargas L, Paredes O, Kawada ME.
Departamento de Biologia Celular y Molecular, Facultad de Ciencias Biologicas, Pontificia Universidad Catolica de Chile, Santiago, Chile.
Based on the in vitro blockade of adrenal catecholamines release by sulfonylurea, we searched for an anti-stress activity of this drug. Stress-induced hyperglycemia and insulin inhibition were employed as adrenergic stress indicators. A standard dose of the oral sulfonylurea glipizide (200 micrograms/100 g), administered 15 min before a 1-h restraint stress to intact or 80% pancreatectomized rats, produced total suppression of the stress-induced hyperglycemia-hypoinsulinemia, an effect followed by a significant post-stress hypoglycemia of 1 h duration. The latter effect was elicited by all the sulfonylureas assayed. In the 80% pancreatectomized rats, glipizide nearly halved the increases in plasma catecholamines at 30 min of stress, but did not modify those attained at 60 min, when glycemia was decreasing and insulinemia was still increasing. Moreover, behavioral experiments in intact stressed rats showed that the adrenergic overt behavior inhibition caused by propranolol was not produced either by glipizide or insulin, reinforcing that glipizide affect was not mediated by catecholamine inhibition. These findings suggest a blockade of catecholamines hepatic receptors by the anticipated insulin release induced by sulfonylurea. Thus, insulin fully dominated when insulin and catecholamines were administered in a stress-like sequence. A confirmation of these findings in diabetic patients subjected to surgical stress would allow a new therapeutic application of sulfonylurea. It is concluded that an anticipated insulin release plus an insulin dominant role over catecholamines activity might explain the anti-stress effect of sulfonylurea.
online pharmacy ref source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=8640242&dopt=Abstract
J Pharmacol Exp Ther. 1996 Jun;277(3):1751-8.
Adrenergic regulation of the heat shock response in brown adipose tissue.
Matz JM, LaVoi KP, Blake MJ.
Department of Pharmacology and Toxicology, University of North Dakota School of Medicine, Grand Forks, USA.
One of several ways that cells respond to damage or stress is by the expression of a set of highly conserved proteins termed, heat shock proteins (HSP). Induction of the heat shock response has been positively correlated with adaptation or protection of cells and tissues from the destructive effects of various types of stressors. Although heat can induce a generalized HSP response in most cells, the selective induction of HSP in specific cell populations by pharmacological agents may prove therapeutically useful for the protection of organs or tissues at risk for damage. Results from our studies suggest that the HSP response is integrated with fundamental physiological stress responses and demonstrate that distinct regulatory events couple neurotransmitter/hormone-receptor interactions with HSP expression in mammalian tissues. We demonstrate that the adrenergic receptor agonist, phenylephrine, induces HSP expression in brown adipose tissue (BAT). Apparently, this response is mediated by alpha-adrenergic receptors in BAT because prazosin, but not propranolol, blocks HSP induction and hexamethonium is without effect. Based on the transcripts induced and the magnitude of heat shock element-binding activity, phenylephrine appears to induce HSP expression through unique transcriptional regulatory mechanisms. The phenylephrine-induced HSP response is not unique to BAT as we have found that HSP are induced in other tissues as well. In BAT, HSP may facilitate the thermogenic function of this tissue, however, their function in other tissues remains unclear. The results of this study characterize a model system where the heat shock response is differentially evoked by a specific pharmacological agent and may aide in the development of treatment strategies to selectively target HSP expression in vivo.
online pharmacy ref source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=8667247&dopt=Abstract
Anal Chem. 1996 Jul 15;68(14):2370-8.
Experimental and theoretical study of the adsorption behavior and mass transfer kinetics of propranolol enantiomers on cellulase protein as the selector.
Fornstedt T, Zhong G, Bensetiti Z, Guiochon G.
Department of Chemistry, University of Tennessee, Knoxville 37996-1600, USA.
The thermodynamics and mass transfer kinetics of the retention of the R and S enantiomers of propranolol were investigated on a system comprising an acetic acid buffer solution as the mobile phase and the protein cellobiohydrolase I immobilized on silica as the stationary phase. The bi-Langmuir isotherm model fitted best to each set of single-component isotherm data. The monolayer capacity of the nonchiral type of adsorption sites was 22.9 mM. For the chiral type of sites, it was 0.24 mM for the R enantiomer and 0.64 mM for the S enantiomer. Peak tailing was observed, even at very low concentrations allowing operation of the low-capacity chiral sites under linear conditions. This tailing can be explained on the basis of heterogeneous mass transfer kinetics. At higher concentrations, which are often used in analytical applications, the isotherms on the chiral sites no longer have a linear behavior, and peak tailing is consequently more pronounced. Under those conditions, peak tailing originates from the combined effect of heterogeneous thermodynamics and heterogeneous mass transfer kinetics. These complex phenomena are explained and modeled using the transport-dispersive model with a solid film linear driving force model modified to account for heterogeneous mass transfer kinetics. The rate coefficient of the mass transfer kinetics was found to be concentration dependent.
online pharmacy ref source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=8686929&dopt=Abstract
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