Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P61278 (somatostatin)
 22,083 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Previous studies have shown that nerve cells containing NADPH-diaphorase (NADPH-d) are relatively resistant to various damaging processes. NADPH-d has been found to be colocalized with somatostatin (SOM) and neuropeptide Y (NPY) in neuronal populations of several forebrain regions. We have investigated the anatomical distribution, morphology and cell sizes of NADPH-d neurons in amygdala and temporal cortex in Alzheimer's disease (AD) compared to controls of different age. NADPH-d cells and fibers were present in layers II-VI of the cortex and in the white matter below the cortical mantle. In the amygdaloid complex, NADPH-d cells and processes were observed in almost all subnuclei. In the amygdala of aged controls, only insignificant atrophic alterations of NADPH-d neurons and fibers were seen. In AD, a moderate, but significant shift towards an increased number of medium-to small-sized neurons was measured in amygdala and cortex, indicating cell shrinkage during the course of the disease. However, there were no differences when comparing NADPH-d staining in amygdaloid subregions in AD cases that contained numerous neuritic plaques (i.e., accessory basal nucleus) with areas that were relatively free of lesions (i.e., lateral nucleus). Analysis of cell size of SOM- and NPY-immunoreactive cells revealed only slight atrophic changes during aging. In AD, however, a significant atrophy of somatostatin neurons in temporal cortex was found, whereas no further cell shrinkage was noted for NPY as compared to aged controls. Colocalization tests demonstrated a large overlap between NPY, SOM and NADPH-d in the amygdala, whereas a subpopulation of cortical SOM neurons, predominantly localized in upper layers, showed a lack of NADPH-d. Our findings of a relative stability of a selective subclass of neurons during aging and AD support the hypothesis that cellular pathology may affect only specific neuronal populations while others might be spared.
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PMID:NADPH-diaphorase-positive cell populations in the human amygdala and temporal cortex: neuroanatomy, peptidergic characteristics and aspects of aging and Alzheimer's disease. 137 87

The Bacillus subtilis dihydrofolate reductase (DHFR) gene was expressed in Escherichia coli. The gene product was purified to homogeneity by Butyl-Toyopearl, Toyopearl HW55, and DEAE-Toyopearl column chromatographies, and its molecular properties were compared to those of E. coli DHFR. The specific enzyme activity of the B. subtilis DHFR was 240 units/mg under the standard assay conditions, being about four times higher than that of the E. coli DHFR. Km for coenzyme NADPH was 20.7 microM, a value about three times larger than that of E. coli, whereas Km (1.5 microM) for the substrate, dihydrofolate, was similar to that of E. coli DHFR. This seems to reflect the low homology of the amino acid sequence in residues 61-88 of the two DHFRs where one of the NADPH binding sites is located [Bystrof, C. & Kraut, J. (1991) Biochemistry 30, 2227-2239]. Similar to the E. coli DHFR [Iwakura, M. et al. (1992) J. Biochem. 111, 37-45], the extension of amino acid sequences at the C-terminal end of the B. subtilis DHFR could be attained without loss of the enzyme function or decrease of the protein yield. Thus, the DHFR is useful as a carrier protein for expressing small polypeptides, such as leucine enkephalin, bradykinin, and somatostatin.
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PMID:Dihydrofolate reductase from Bacillus subtilis and its artificial derivatives: expression, purification, and characterization. 163 61

Striatal atrophy in Huntington's disease (HD) is characterized by selective preservation of a subclass of neurons colocalizing NADPH-diaphorase (NADPH-d), somatostatin (SS), and neuropeptide Y (NPY), which have been reported to show three- to fivefold increases in SS-like immunoreactivity (SSLI) and NPY content. Since HD brain is capable of producing excessive quantities of the excitotoxin quinolinic acid (Quin), an N-methyl-D-aspartate (NMDA) receptor agonist, and since experimental Quin lesions show neuronal loss with sparing of NADPH-d/SS/NPY neurons, it has been suggested that Quin may be important in the pathogenesis of HD. In the present study we determined whether Quin stimulates SS gene function in cultured cortical cells known to be rich in NADPH-d/SS/NPY neurons. Cultures of dispersed fetal rat cortical cells were exposed to Quin (1 and 10 mM) with or without (-)-2-amino-5-phosphonovaleric acid (APV; 0.5 mM), an NMDA receptor antagonist, NMDA (0.2 and 0.5 mM), and glutamate (Glu; 0.5 mM). Medium and cellular SSLI was determined by radioimmunoassay and SS mRNA by Northern analysis with a cRNA probe. Quin induced significant (p less than 0.01) 1.6- and 2.5-4 fold increases in SSLI and SS mRNA accumulation, respectively, which were abolished by APV. Release of SSLI into the culture medium was stimulated two- to fivefold by Quin over a 2- to 20-h period. The increase in SS mRNA produced by Quin was time and dose dependent. A similar dose-dependent increase in SS mRNA comparable with that observed with Quin was induced by NMDA.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Quinolinic acid stimulates somatostatin gene expression in cultured rat cortical neurons. 167 45

Rainbow trout, Oncorhynchus mykiss, were used to evaluate the effects of carbohydrate loading on plasma levels of pancreatic hormones and associated changes in metabolic indexes in a carnivorous fish. Glucose (3,000 mg/dl, 10 microliters/g body wt) was injected intraperitoneally into fish (mean wt 54 +/- 5 g) that were killed 0.5-24 h after administration. Glucose injection resulted in hyperglycemia with maximum glucose levels of 306 +/- 13 mg/dl observed 60 min after injection. Glucose administration also resulted in hyperlipidemia. Plasma fatty acids increased twofold in glucose-injected animals. Alterations in plasma metabolites reflected changes in energy stores. Although total lipid concentration was unaffected by glucose injection, lipolytic enzyme activity in the liver was enhanced. Biosynthetic capacity, as indicated by NADPH production from glucose-6-phosphate dehydrogenase, was decreased by glucose injection. Liver glycogen content was reduced in glucose-injected animals 1 h after injection. Glucose injection was attended by increases in the plasma levels of gene II somatostatin-25 (predominant form of pancreatic somatostatin in salmonids) and of glucagon. Insulin levels were initially suppressed after glucose injection. These results indicate that metabolic adjustments caused by glucose administration can be related to the regulatory action of pancreatic hormones. Furthermore, these results suggest that the somatostatin-secreting cells of the trout are sensitive to glucose and that somatostatin-suppressed insulin secretion contributes to the glucose intolerance of trout.
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PMID:Insulin suppression is associated with hypersomatostatinemia and hyperglucagonemia in glucose-injected rainbow trout. 167 8

Transversal sections through the basal forebrain of 11 adult male rats were immunostained for glutamic acid decarboxylase (GAD), choline acetyltransferase (ChAT), somatostatin (SOM) and parvalbumin (PARV). Immunohistochemistry of ChAT, PARV, and SOM was combined with histochemistry of NADPH-diaphorase (NADPH-d) to obtain information on the colocalization of various neuroactive substances and this enzyme and to facilitate the recognition of morphological details of double-stained neurons. The distribution patterns of GAD- and PARV-immunoreactive cells were only in part congruent in basal forebrain nuclei in the rat. In the medial septal nucleus (MS) and the vertical limb of the diagonal band (vDB) PARV-immunopositive neurons were homogeneously scattered inside the nucleus, whereas the GAD-immunoreactive cells were much more numerous in the lateral part of this nuclear complex. In the horizontal limb of the diagonal band (hDB) and the nucleus preopticus magnocellularis (NPM), where GAD-immunoreactive cells occurred in high number, only very few cells contained PARV-immunoreaction product. In the substantia innominata-nucleus basalis Meynert complex (SI-NB) and in the ventral pallidum (VP) the neuropil was heavily stained with the GAD-immunoreaction product. The number of GAD-positive cells appeared low in the SI-NB, but much higher in the VP. In this nucleus GAD- and PARV-immunoreactive cells seem to be identical. PARV-positive neurons are very sparse in the SI-NB. Double-staining of PARV-immunoreactivity and NADPH-d was not registered. These nuclei were the only ones in which some cells with SOM-like immunoreactivity were observed. Among ChAT-positive neurons those double-stained with NADPH-d occurred in moderate number, but with obvious regional differences. In MS-vDB and the marginal zone of hDB the two neuron groups were intermingled, but only in the innermost part of the hDB ChAT-single-immunostained cells form aggregates, which were also typical of the zone in the SI-NB that surrounds and infiltrates the globus pallidus (GP). Double-labelled cells were more frequent in the lateral aspect of the NPM and SI-NB. Cells single-stained for NADPH-d were frequent in the MS-vDB along the border toward the lateral septal nuclei, but low in number in the NPM, VP and SI-NB. The functional aspects of the occurrence of GAD-immunoreactive cell aggregates in the lateral preoptic area (LP) and the lateral hypothalamic area (LH) were discussed with special regards to extrinsic GABAergic input in the dorsal SI-NB.(ABSTRACT TRUNCATED AT 400 WORDS)
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PMID:Morphology of neurons in the rat basal forebrain nuclei: comparison between NADPH-diaphorase histochemistry and immunohistochemistry of glutamic acid decarboxylase, choline acetyltransferase, somatostatin and parvalbumin. 168 12

NADPH diaphorase staining neurons, uniquely resistant to toxic insults and neurodegenerative disorders, have been colocalized with neurons in the brain and peripheral tissue containing nitric oxide synthase (EC 1.14.23.-), which generates nitric oxide (NO), a recently identified neuronal messenger molecule. In the corpus striatum and cerebral cortex, NO synthase immunoreactivity and NADPH diaphorase staining are colocalized in medium to large aspiny neurons. These same neurons colocalize with somatostatin and neuropeptide Y immunoreactivity. NO synthase immunoreactivity and NADPH diaphorase staining are colocalized in the pedunculopontine nucleus with choline acetyltransferase-containing cells and are also colocalized in amacrine cells of the inner nuclear layer and ganglion cells of the retina, myenteric plexus neurons of the intestine, and ganglion cells of the adrenal medulla. Transfection of human kidney cells with NO synthase cDNA elicits NADPH diaphorase staining. The ratio of NO synthase to NADPH diaphorase staining in the transfected cells is the same as in neurons, indicating that NO synthase fully accounts for observed NADPH staining. The identity of neuronal NO synthase and NADPH diaphorase suggests a role for NO in modulating neurotoxicity.
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PMID:Nitric oxide synthase and neuronal NADPH diaphorase are identical in brain and peripheral tissues. 171 81

Cysteamine (100 micrograms) markedly reduces the number (by about 60%) and intensity of staining of NADPH diaphorase-reactive neurons 6 h after local injection into the striatum. This effect was reversible (after 24 h) and was only observed when the indirect staining procedure was applied in which NADPH formed by endogenous malate dehydrogenase is used. However, no direct effect of cysteamine on the malate dehydrogenase reaction was found. The decrease in NADPH diaphorase activity parallels the previously reported cysteamine induced decrease in somatostatin contained in the same neurons and may point to a biochemical interrelation of somatostatin and NADPH diaphorase in these neurons.
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PMID:Local injection of cysteamine into the rat striatum decreases number and intensity of staining of neurons by indirect NADPH diaphorase reaction. 245 Mar 8

Salmon (Oncorhynchus kisutch) somatostatin (sSS; 4 or 8 ng/g body wt) or synthetic Gillichthys urotensin II (UII; 2 or 4 ng/g body wt) were injected intraperitoneally into juvenile freshwater coho salmon. Both sSS and UII caused a dose-dependent increase in plasma free fatty acids (FFA) which diminished with time. sSS induced an initial (1 hr) transient hyperglycemia. By contrast, UII tended to induce hypoglycemia, this effect being significant 5 hr after injection of the higher dose. Both sSS and UII depressed plasma insulin titers 1 hr after injection. By 3 hr, the sSS-associated insulin depression was no longer observed. UII treatment induced a hyperinsulinemia which was present 3 and 5 hr after peptide administration. Although no decreases in liver total lipid concentration or in mesenteric fat total tissue mass were observed, lipolytic enzyme activity within each depot was significantly enhanced by both peptides. Neither sSS nor UII altered 3H2O incorporation into fatty acids or neutral lipids. However, enhanced lipogenesis, particularly by UII, was indicated by increased NADPH production resulting from glucose-6-phosphate dehydrogenase activity. Both sSS and UII enhanced glucose mobilization, as indicated by decreased liver glycogen content and increased liver glucose-6-phosphatase activity. UII, but not sSS, stimulated glycogen synthetase activity. These results suggest that both sSS and UII stimulate hyperlipidemia by enhancing depot lipase activity and that although both factors are potentially gluconeogenetic, sSS seems to be glycogenolytic and hyperglycemic, whereas UII may channel glucose to FFA synthesis.
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PMID:Effects of somatostatin-25 and urotensin II on lipid and carbohydrate metabolism of coho salmon, Oncorhynchus kisutch. 288 97

Fetal frontal cortex transplants that survived 2-9 months in cavities in adult rat motor/sensory cortex were processed for vasoactive intestinal polypeptide (VIP), somatostatin 14 (SS), and neuropeptide Y (NPY) immunocytochemistry, and NADPH-diaphorase (NADPH-d) histochemistry. All transplants had surviving VIP, SS, NPY, and NADPH-d neuronal perikarya and fibers with normal adult morphology. The number of peptidergic neurons within transplants, however, often appeared to be less than that in equivalent areas of host cortex. Most transplanted SS and VIP neuronal perikarya did not migrate to form the laminae characteristic of normal cortex. A few transplants had SS and VIP cells arranged in laminae in which the VIP processes were parallel to one another and perpendicular to one transplant surface, approximating normal host neocortex. VIP, NPY, and SS fibers crossed between host brains and transplants, suggesting that peptide host-transplant interactions are possible. All adult host cortical and most transplanted NPY neurons colocalized with NADPH-d. The failure of some transplanted NPY neurons to express NADPH-d suggests these transplanted cells may be functionally impaired, but that they can survive without the NADPH-d enzyme.
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PMID:Fetal frontal cortex transplanted to injured motor/sensory cortex of adult rats. II. VIP-, somatostatin-, and NPY-immunoreactive neurons. 288 9

The tryptophan metabolite quinolinic acid (QUIN) was injected unilaterally into rat cerebral cortex or striatum in order to determine whether the neurotoxin would destroy neuropeptide Y (NPY)- and somatostatin (SS)-immunoreactive, and NADPH-diaphorase (NADPH-D)-containing neurons. Following intrastriatal injections of QUIN, NPY and SS immunoreactivity and NADPH-D-activity was absent in the injection core area. In contrast, cortical NPY- and SS-immunoreactive cells and NADPH-D-containing neurons were resistant to QUIN's neurotoxicity. These results suggest that in contrast to striatal neurons, cortical SS- and NPY-containing neurons do not express N-methyl-D-aspartate receptors.
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PMID:Differential sensitivity of neuropeptide Y, somatostatin and NADPH-diaphorase containing neurons in rat cortex and striatum to quinolinic acid. 289 26


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