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Biomedical subjects

Hasan Parvez

Publications and source records attributed to Hasan Parvez.

5 recordsLinked to original sources
PubMed2004

The effect of diabetes mellitus on the morphology and physiology of monoamine oxidase in the pancreas.

Monoamine oxidase (MAO) is an ubiquitous, non-soluble, membrane-bound enzyme, located in the outer membrane of mitochondria. MAO consists of two subtypes, MAO-A and MAO-B, depending on their substrates and sensitivity to inhibitors. MAO consists of two units joined together by a disulphide bond. The two units of MAO and flavin adenine dinucleotide (FAD) form a polymer in the outer membrane of mitochondria. The function of MAO-A is highly dependent on the lipid constituent of mitochondrial membrane, whereas the function of MAO-B does not depend on the lipid status of mitochondrial membrane. Hydrogen peroxide and ammonia are generated during MAO-induced metabolism of its substrates. MAO and its substrates are present in both the exocrine as well as the endocrine parts of the pancreas. In the islet of Langerhans, MAO-A is observed in about 50% of the cells, whereas MAO-B is less abundant and located mainly in the periphery of pancreatic islets. MAO-B is also demonstrated in centroacinar cells and in pancreatic ducts. Electron microscopy studies suggest that MAO is co-localised with insulin in secretory granules of pancreatic beta cells. Pharmacologically, beta-2-adrenoreceptors agonists such as terbutaline can stimulate MAO activity. In contrast, cholinergic muscarinic stimulation does not affect islet MAO activity. MAO activity in pancreatic tissue is significantly reduced in diabetes. This decrease in MAO activity is associated with an increase in pancreatic tissue levels of adrenaline (ADR) and noradrenaline (NA). Studies on the level of 5-hydroxyindoleacetic acid of pancreatic tissues suggest that serotonin level is also increased in diabetics. Many studies show that MAO inhibits insulin secretion. However, some of its substrates including, serotonin, adrenaline and noradrenaline have been shown to stimulate insulin secretion. In conclusion, the activity and subcellular localisation of MAO suggests that MAO may play an important role in pancreatic beta cell function and hence in the pathogenesis of diabetes mellitus.

Animals↗
PubMed2004

Monoamine oxidase expression during development and aging.

Monoamine oxidase (MAO) isoenzymes play a major role in regulating the concentration of several bioactive amines, including serotonin and catecholamines. Both in the nervous system and in peripheral organs, MAOs can potentially modulate all the processes involving these bioactive amines. In the present article, we review some of the most significant articles published so far on changes in MAOs during development and aging. The data available on development refer mainly to the mammal brain at fetal and post-fetal stages. Very little work has been done on studying MAO ontogenesis during early development, that is, at stages prior to organogenesis, and what has been done refers to non-mammal vertebrates such as fish, amphibians and birds. MAO A and MAO B changes have been measured as values of enzymatic activity, as amount of protein or, more rarely, as amount of mRNAs. A knowledge of MAO developmental changes not only provides a basis for the investigation of factors regulating MAO expression, but can also contribute to a better understanding of the possible trophic and/or morphogenetic role of monoaminergic neurotransmitters in the developing brain. Transgenic mice lacking MAO A and rodents treated with MAO inhibitors during gestation have been very useful in this second case. The investigations of changes in MAO A and MAO B during aging in the literature refer mostly to humans, mice and rats. Interest in studies on aging is stimulated, among other things, by the observation that age-related diseases leading to neurodegenerative phenomena could be accompanied by changes in MAO activity.

Aging↗
PubMed2004

A screening system of prodrugs selective for MAO-A or MAO-B.

We synthesized several prodrugs of glycine and gamma-aminobutyric acid. In order to establish a screening system from the prodrugs of selective activity to MAO-A or MAO-B, we examined purification conditions such as solubilization with Triton X-100, precipitation with ammonium sulfate, gel filtration and anion exchange chromatography. MAO-B was purified from various tissues such as guinea pig brain, kidney and spleen. MAO-A from human placenta without MAO-B was unstable in above purifications and used as crude. At each purification step, we checked sensitivity of the enzyme to specific inhibitors by developing a convenient fluorescence assay, in which hydrogen peroxide produced by the enzyme was reacted with p-hydroxyphenylpropionic acid. A fluorescence microplate reader measured a fluorescence of the fluorescent product from p-hydroxyphenylpropionic acid with horseradish peroxidase. In comparison with milacemide, N,N-bis(carbamoylmethyl)-N-pentylamine was the best and exclusive substrate for MAO-B. 2-N-(phenylethylamino)-acetoamide was the good substrate for MAO-A and MAO-B same as milacemide. 4-N-(n-pentylamino)-butyric acid and 4-(N-phenylethylamino)-butyric acid were the moderate substrates for both enzymes, which should release gamma-aminobutyric acid. These drugs will be new leading compounds.

Animals↗
PubMedDate not supplied

Mechanism of ghrelin-evoked glucagon secretion from the pancreas of diabetic rats.

OBJECTIVE: Ghrelin is a newly discovered peptide, which was first demonstrated in the epithelium of rat stomach. The purpose of the study was to examine the effect of ghrelin on glucagon secretion from pancreatic tissue fragments of normal and diabetic rats. METHODS: Diabetes was induced by streptozotocin (60 mg Kg body weight 1) given intraperitoneally. Four weeks after the onset of diabetes, pancreatic fragments of normal and diabetic rats were incubated with different concentrations (10 12 10 6 M) of ghrelin. Glucagon release was measured using radioimmunoassay technique. RESULTS: Ghrelin failed to stimulate or inhibit glucagon secretion from normal rat pancreas. However, it induced significant increases in glucagon secretion from pancreatic tissue fragments of diabetic rats. Either atropine (muscarinic cholinergic receptor antagonist) or propranolol (beta-adrenergic receptor antagonist) or yohimbine (alpha2-adrenergic receptor antagonist) or diltiazem (calcium channel antagonist) did not affect ghrelin-glucagon interaction. Moreover, a combination of atropine, propranolol and yohimbine had no significant effect on the interaction of ghrelin with glucagon. CONCLUSION: The ghrelin-induced glucagon secretion in diabetic rats is not controlled via cholinergic or adrenergic pathways. In conclusion, it appears that the main target of ghrelin in the rat endocrine pancreas is not glucagon-producing cells but rather insulin secreting cells which are more involve in weight gain and body growth.

Adrenergic alpha-2 Receptor Antagonists↗