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Journal articles on the topic 'AmyTan'

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Published: 4 June 2021

Last updated: 6 February 2022

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1

Rodriguez Sanoja, R., J. Morlon-Guyot, J. Jore, J. Pintado, N. Juge та J. P. Guyot. "Comparative Characterization of Complete and Truncated Forms of Lactobacillus amylovorus α-Amylase and Role of the C-Terminal Direct Repeats in Raw-Starch Binding". Applied and Environmental Microbiology 66, № 8 (2000): 3350–56. http://dx.doi.org/10.1128/aem.66.8.3350-3356.2000.

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ABSTRACT Two constructs derived from the α-amylase gene (amyA) of Lactobacillus amylovorus were expressed inLactobacillus plantarum, and their expression products were purified, characterized, and compared. These products correspond to the complete (AmyA) and truncated (AmyAΔ) forms of α-amylase; AmyAΔ lacks the 66-kDa carboxyl-terminal direct-repeating-unit region. AmyA and AmyAΔ exhibit similar amylase activities towards a range of soluble substrates (amylose, amylopectin and α-cyclodextrin, and soluble starch). The specific activities of the enzymes towards soluble starch are similar, but t

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2

Christopoulos, George, Patrick M. Sexton, George Paxinos, Xu-Feng Huang, Kevin Beaumont, and Arthur W. Toga. "Comparative distribution off receptors for amylin and the related peptides calcitonin gene related peptide and calcitonin in rat and monkey brain." Canadian Journal of Physiology and Pharmacology 73, no. 7 (1995): 1037–41. http://dx.doi.org/10.1139/y95-146.

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The distribution of amylin receptors (125I-labelled rat amylin) in brains of rat and monkey were mapped and compared with the distribution of receptors for calcitonin (CT) (125I-labelled salmon CT) and calcitonin gene related peptide (CGRP) (rat, 125I-labelled rat CGRPα; monkey, 125-labelled human CGRPα). In rat, amylin receptors were discretely distributed with the highest receptor densities found in mid-caudal accumbens nucleus, parts of the bed nucleus of the stria terminalis, amygdala, and hypothalamus. Moderate to high densities of binding also occurred in the area postrema, subfornical o

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3

Narita, Junya, Kenji Okano, Tomoe Kitao та ін. "Display of α-Amylase on the Surface of Lactobacillus casei Cells by Use of the PgsA Anchor Protein, and Production of Lactic Acid from Starch". Applied and Environmental Microbiology 72, № 1 (2006): 269–75. http://dx.doi.org/10.1128/aem.72.1.269-275.2006.

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ABSTRACT We developed a new cell surface engineering system based on the PgsA anchor protein from Bacillus subtilis. In this system, the N terminus of the target protein was fused to the PgsA protein and the resulting fusion protein was expressed on the cell surface. Using this new system, we constructed a novel starch-degrading strain of Lactobacillus casei by genetically displaying α-amylase from the Streptococcus bovis strain 148 with a FLAG peptide tag (AmyAF). Localization of the PgsA-AmyA-FLAG fusion protein on the cell surface was confirmed by immunofluorescence microscopy and flow cyto

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4

Niimi, Y., F. Sala, V. Deletis, and A. Berenstein. "Provocative Testing for Embolization of Spinal Cord AVMs." Interventional Neuroradiology 6, no. 1_suppl (2000): 191–94. http://dx.doi.org/10.1177/15910199000060s130.

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The purpose of this study is to evaluate efficacy and reliability of chemical provocative testing using neurophysiological monitoring prior to embolization of spinal cord AVMs (SCAVMs). We performed retrospective analysis of provocative testing using sodium amytal and lidocaine injected superselectively in 41 angiography and / or embolization procedures in 26 patients with a SCAVM, including 23 amytal and 26 lidocaine injections. All procedures were performed under general anesthesia using neuroleptic drugs, and with monitoring of cortical somatosensory evoked potentials (SEPs) and trans-crani

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5

Piper, August. "“Truth Serum” and “Recovered Memories” of Sexual Abuse: A Review of the Evidence." Journal of Psychiatry & Law 21, no. 4 (1993): 447–71. http://dx.doi.org/10.1177/009318539302100403.

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This article discusses the Amytal interview, which is sometimes believed to be useful to indicate deception, to reveal concealed contents of the mind, or to compel disclosure of those contents. The medical literature is reviewed to determine if the procedure reliably yields information valuable in legal evaluations of adults claiming recovered memories of childhood sexual abuse. The review finds that no investigator who had performed Amytal interviews endorsed them as a method of recovering accurate memories; rather, the literature repeatedly comments on several characteristics of these examin

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6

Lavallée, J. C., and Et M. Tremblay. "La narcose sous barbiturique: mutisme*." Canadian Journal of Psychiatry 37, no. 9 (1992): 646–50. http://dx.doi.org/10.1177/070674379203700909.

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The authors review the history and current uses of the amytal interview. This technique was quite popular over 50 years ago when it began, but has been ignored for the past ten years. A clinical case of mutism is described in this research to illustrate the usefulness of the amytal interview. In this particular case, the narcosis has permitted the uncovering of delusions and consequently the administration of the appropriate treatment.

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7

Gershon, Ariel, and Edward Shorter. "How amytal changed psychopharmacy: off-label uses of sodium amytal (1920–40)." History of Psychiatry 30, no. 3 (2019): 352–58. http://dx.doi.org/10.1177/0957154x19847605.

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In the early 1930s, American neurologist and psychiatrist William Bleckwenn used sodium amytal to render catatonic patients responsive, so that he could engage in talk therapy. Bleckwenn found a new, ‘off-label’ use for this anaesthetic and anxiolytic medication in psychiatry and, in doing so, allowed for important discoveries in the diagnosis and treatment of catatonia. Pharmacological textbooks reveal a ‘label’, while the Index-Catalogue of the Library of the Surgeon-General’s Office reveals explorations ‘off label’ of barbiturates. The ‘off-label’ use of barbiturates facilitated talk therap

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8

Cornish, J., K. E. Callon, C. Q. X. Lin, et al. "Dissociation of the effects of amylin on osteoblast proliferation and bone resorption." American Journal of Physiology-Endocrinology and Metabolism 274, no. 5 (1998): E827—E833. http://dx.doi.org/10.1152/ajpendo.1998.274.5.e827.

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This study assesses the structure-activity relationships of the actions of amylin on bone. In fetal rat osteoblasts, only intact amylin and amylin-(1—8) stimulated cell proliferation (half-maximal concentrations 2.0 × 10−11 and 2.4 × 10−10 M, respectively). Amylin-(8—37), COOH terminally deamidated amylin, reduced amylin, and reduced amylin-(1—8) (reduction results in cleavage of the disulfide bond) were without agonist effect but acted as antagonists to the effects of both amylin and amylin-(1—8). Calcitonin gene-related peptide-(8—37) also antagonized the effects of amylin and amylin-(1—8) o

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9

Kiriyama, Yoshimitsu, та Hiromi Nochi. "Role and Cytotoxicity of Amylin and Protection of Pancreatic Islet β-Cells from Amylin Cytotoxicity". Cells 7, № 8 (2018): 95. http://dx.doi.org/10.3390/cells7080095.

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Amylin, (or islet amyloid polypeptide; IAPP), a 37-amino acid peptide hormone, is released in response to nutrients, including glucose, lipids or amino acids. Amylin is co-stored and co-secreted with insulin by pancreatic islet β-cells. Amylin inhibits food intake, delays gastric emptying, and decreases blood glucose levels, leading to the reduction of body weight. Therefore, amylin as well as insulin play important roles in controlling the level of blood glucose. However, human amylin aggregates and human amylin oligomers cause membrane disruption, endoplasmic reticulum (ER) stress and mitoch

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10

Qi, Dongfei, Kun Cai, Oumei Wang та ін. "Fatty acids induce amylin expression and secretion by pancreatic β-cells". American Journal of Physiology-Endocrinology and Metabolism 298, № 1 (2010): E99—E107. http://dx.doi.org/10.1152/ajpendo.00242.2009.

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Amylin is the major component of pancreatic amyloid, which is implicated in the development of type 2 diabetes. It is costored with insulin in the secretory granules of pancreatic β-cells and cosecreted with insulin following stimulation with glucose. Here, we investigate the effect of fatty acids (FAs) on amylin expression and secretion by β-cells and explore the underlying mechanisms. Palmitate and oleate dose-dependently induced amylin mRNA accumulation in murine pancreatic β-cell line MIN6 and primary pancreatic islets. the inductive effect of FAs on amylin expression is independent of glu

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11

Hazar, Erkan. "Amyand Herni: Olgu sunumu." Cumhuriyet Medical Journal 35, no. 4 (2013): 597–99. http://dx.doi.org/10.7197/1305-0028.2262.

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12

Dacquin, Romain, Rachel A. Davey, Catherine Laplace, et al. "Amylin inhibits bone resorption while the calcitonin receptor controls bone formation in vivo." Journal of Cell Biology 164, no. 4 (2004): 509–14. http://dx.doi.org/10.1083/jcb.200312135.

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Amylin is a member of the calcitonin family of hormones cosecreted with insulin by pancreatic β cells. Cell culture assays suggest that amylin could affect bone formation and bone resorption, this latter function after its binding to the calcitonin receptor (CALCR). Here we show that Amylin inactivation leads to a low bone mass due to an increase in bone resorption, whereas bone formation is unaffected. In vitro, amylin inhibits fusion of mononucleated osteoclast precursors into multinucleated osteoclasts in an ERK1/2-dependent manner. Although Amylin +/− mice like Amylin-deficient mice displa

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13

Fernandes-Santos, Caroline, Zhongming Zhang, Donald A. Morgan, Deng-Fu Guo, Andrew F. Russo, and Kamal Rahmouni. "Amylin Acts in the Central Nervous System to Increase Sympathetic Nerve Activity." Endocrinology 154, no. 7 (2013): 2481–88. http://dx.doi.org/10.1210/en.2012-2172.

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Abstract The pancreatic hormone amylin acts in the central nervous system (CNS) to decrease food intake and body weight. We hypothesized that amylin action in the CNS promotes energy expenditure by increasing the activity of the sympathetic nervous system. In mice, ip administration of amylin significantly increased c-Fos immunoreactivity in hypothalamic and brainstem nuclei. In addition, mice treated with intracerebroventricular (icv) amylin (0.1 and 0.2 nmol) exhibited a dose-related decrease in food intake and body weight, measured 4 and 24 hours after treatment. The icv injection of amylin

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14

Fürnsinn, Clemens, Peter Nowotny, Michael Roden, et al. "Insulin resistance caused by amylin in conscious rats is independent of induced hypocalcemia and fades during long-term exposure." Acta Endocrinologica 129, no. 4 (1993): 360–65. http://dx.doi.org/10.1530/acta.0.1290360.

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To compare the effect of short- vs long-term amylin infusion on insulin sensitivity, glucose tolerance and serum calcemia, euglycemic-hyperinsulinemic clamp (26 pmol·kg−1·min−1) and glucose tolerance tests (2.4 mmol/kg over 30 min) were performed in lean Zucker rats. Three infusion protocols were employed: control group: 24 h of iv saline; short-term amylin exposure: 22 h of iv saline followed by 2 h of iv amylin (20 μg/h); long-term amylin exposure: 24 h of iv amylin (20 μg/h). Insulin resistance was induced by short-term amylin infusion during euglycemic clamping, as shown by a 41% decrease

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15

Trikha, Saurabh, and Aleksandar M. Jeremic. "Clustering and Internalization of Toxic Amylin Oligomers in Pancreatic Cells Require Plasma Membrane Cholesterol." Journal of Biological Chemistry 286, no. 41 (2011): 36086–97. http://dx.doi.org/10.1074/jbc.m111.240762.

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Self-assembly of the human pancreatic hormone amylin into toxic oligomers and aggregates is linked to dysfunction of islet β-cells and pathogenesis of type 2 diabetes mellitus. Recent evidence suggests that cholesterol, an essential component of eukaryotic cells membranes, controls amylin aggregation on model membranes. However, the pathophysiological consequence of cholesterol-regulated amylin polymerization on membranes and biochemical mechanisms that protect β-cells from amylin toxicity are poorly understood. Here, we report that plasma membrane (PM) cholesterol plays a key role in molecula

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16

Young, A. A., B. Gedulin, D. Wolfe-Lopez, H. E. Greene, T. J. Rink, and G. J. Cooper. "Amylin and insulin in rat soleus muscle: dose responses for cosecreted noncompetitive antagonists." American Journal of Physiology-Endocrinology and Metabolism 263, no. 2 (1992): E274—E281. http://dx.doi.org/10.1152/ajpendo.1992.263.2.e274.

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Increasing concentrations of amylin progressively depressed the maximal insulin-stimulated radioglucose incorporation into soleus muscle glycogen, but did not substantively change the EC50 (range 0.78 to 1.52 nM); these findings show noncompetitive, insurmountable antagonism of insulin action by amylin. The results from 36 combinations of different insulin and amylin concentrations were used to construct a response surface that can be used to predict the response for any combination of insulin and amylin concentration. The predicted response to a constant ratio of insulin and amylin concentrat

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17

Baqué, S., J. J. Guinovart, and A. M. Gómez-Foix. "Amylin impairment of insulin effects on glycogen synthesis and phosphoenolpyruvate carboxykinase gene expression in rat primary cultured hepatocytes." Biochemical Journal 304, no. 2 (1994): 449–53. http://dx.doi.org/10.1042/bj3040449.

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The ability of amylin to impair hepatic insulin action is controversial. We have found that the effect of amylin in primary cultured hepatocytes is strongly dependent on the culture conditions. Only in hepatocytes preincubated in the presence of fetal serum did amylin, at concentrations ranging from 1 to 100 nM, reduce insulin-stimulated glycogen synthesis rate and glycogen accumulation without showing direct effects. Neither basal glycogen synthase nor glycogen phosphorylase activity was modified by amylin treatment. Nevertheless, amylin (100 nM) blocked the activation of glycogen synthase by

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18

Bruner, John Clay. "Comments on the genus Amyzon (family Catostomidae)." Journal of Paleontology 65, no. 4 (1991): 678–86. http://dx.doi.org/10.1017/s0022336000030766.

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At least four of the seven described species of Amyzon are valid species with doubtful status given to Amyzon pandatum Cope, 1874, and Amyzon fusiforme Cope, 1875. Amyzon gosiutensis Grande, Eastman, and Cavender, 1982, is a junior synonym of Amyzon aggregatum Wilson, 1977b. The Klondike Mountain Formation specimens examined from Republic, Washington, are identified as Amyzon aggregatum Wilson, 1977b. The known range of A. aggregatum is extended south to Republic, Washington, and southeast to the Laney Shale Member of the Green River Formation, Wyoming.

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19

Zimmermann, U., B. Fluehmann, W. Born, JA Fischer, and R. Muff. "Coexistence of novel amylin-binding sites with calcitonin receptors in human breast carcinoma MCF-7 cells." Journal of Endocrinology 155, no. 3 (1997): 423–31. http://dx.doi.org/10.1677/joe.0.1550423.

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Amylin, calcitonin (CT) and calcitonin gene-related peptide (CGRP) share limited structural homology including amino-terminal ring structures linked by a disulfide bridge and amidated carboxy-termini. Here, we have compared [125I]Bolton-Hunter-[Lys1] rat amylin ([125I]amylin) binding and the stimulation of cyclic AMP accumulation by human (h) amylin, hCT and hCGRP-I in the human breast carcinoma cell lines MCF-7 and T47D, which predominantly express hCT1a and hCT1b receptor isoforms (hCTR1a, hCTR1b) at a similar total number of hCT-binding sites. In MCF-7 cells, half-maximal inhibition (IC50)

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20

Turek, Victoria F., James L. Trevaskis, Barry E. Levin, et al. "Mechanisms of Amylin/Leptin Synergy in Rodent Models." Endocrinology 151, no. 1 (2010): 143–52. http://dx.doi.org/10.1210/en.2009-0546.

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Abstract The present studies aimed to identify mechanisms contributing to amylin/leptin synergy in reducing body weight and adiposity. We reasoned that if amylin/leptin harnessed complementary neuronal pathways, then in the leptin-sensitive state, amylin should augment leptin signaling/binding and that in the absence of endogenous amylin, leptin signaling should be diminished. Amylin (50 μg/kg, ip) amplified low-dose leptin-stimulated (15 μg/kg, ip) phosphorylated signal transducer and activator of transcription-3 signaling within the arcuate nucleus (ARC) in lean rats. Amylin (50 μg/kg · d) o

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21

Rumsey, W. L., D. F. Wilson, and M. Erecinska. "Relationship of myocardial metabolism and coronary flow: dependence on extracellular calcium." American Journal of Physiology-Heart and Circulatory Physiology 253, no. 5 (1987): H1098—H1105. http://dx.doi.org/10.1152/ajpheart.1987.253.5.h1098.

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The hypothesis that extracellular [Ca2+] ([Ca2+]e) influences the transmission of vasoregulatory information from the heart to coronary smooth muscle was examined. The isolated, retrogradely perfused rat heart was used to evaluate vascular reactivity to transient infusion of either 0.88 mM Amytal (amobarbital), hypoxia (95% N2-5% CO2), or 12 microM adenosine in the presence and absence of 2.5 microM verapamil. Amytal alone enhanced coronary flow by 78% and lactate efflux by 10-fold, whereas it decreased O2 consumption by 40% and the ratio of the free cytosolic concentrations of ATP-to-ADP time

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22

Rocha, Samanta F. Blattes da, Murilo S. Meneses, Pedro A. Kowacs, Cristiane Simão, Heraldo Larocca, and Sonival C. Hunhevicz. "O methohexital sódico (Brevital®) no teste de Wada: relato de dois casos." Journal of Epilepsy and Clinical Neurophysiology 11, no. 2 (2005): 87–90. http://dx.doi.org/10.1590/s1676-26492005000200004.

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RESUMO INTRODUÇÃO: O teste de Wada® continua sendo um exame freqüentemente utilizado, para a avaliação qualitativa e quantitativa da lateralidade das funções de linguagem e das funções de memória verbal, e do possível déficit residual, uma vez que simula o efeito da cirurgia na investigação pré-operatória de candidatos a lobectomia temporal. No Brasil, há consideráveis dificuldades impostas pelas autoridades sanitárias para obtenção do Amytal® (amobarbital sódico). OBJETIVOS: Descrever o protocolo do teste de Wada realizado com Brevital® (methoexital sódico) em dois candidatos a lobectomia tem

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23

Kumar, Ammu Prasanna, Sungmun Lee, and Suryani Lukman. "Computational and Experimental Approaches to Design Inhibitors of Amylin Aggregation." Current Drug Targets 20, no. 16 (2019): 1680–94. http://dx.doi.org/10.2174/1389450120666190719164316.

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Amylin is a neuroendocrine peptide hormone secreted by pancreatic &#223;-cells; however, amylin is toxic to &#223;-cells when it is aggregated in type 2 diabetes mellitus (T2DM). It is important to understand amylin’s structures and aggregation mechanism for the discovery and design of effective drugs to inhibit amylin aggregation. In this review, we investigated experimental and computational studies on amylin structures and inhibitors. Our review provides some novel insights into amylin, particularly for the design of its aggregation inhibitors to treat T2DM. We detailed the potentia

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Schultz, Nina, Elin Byman, Malin Fex, and Malin Wennström. "Amylin alters human brain pericyte viability and NG2 expression." Journal of Cerebral Blood Flow & Metabolism 37, no. 4 (2016): 1470–82. http://dx.doi.org/10.1177/0271678x16657093.

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Amylin, a pancreatic β-cell-derived peptide hormone, forms inclusions in brain microvessels of patients with dementia who have been diagnosed with type 2 diabetes and Alzheimer’s disease. The cellular localization of these inclusions and the consequences thereof are not yet known. Using immunohistochemical staining of hippocampus and parahippocampal cortex from patients with Alzheimer’s disease and non-demented controls, we show that amylin cell inclusions are found in pericytes. The number of amylin cell inclusions did not differ between patients with Alzheimer’s disease and controls, but amy

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Reidelberger, Roger D., Urban Arnelo, Lars Granqvist, and Johan Permert. "Comparative effects of amylin and cholecystokinin on food intake and gastric emptying in rats." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 280, no. 3 (2001): R605—R611. http://dx.doi.org/10.1152/ajpregu.2001.280.3.r605.

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CCK is a physiological inhibitor of gastric emptying and food intake. The pancreatic peptide amylin exerts similar actions, yet its physiological importance is uncertain. Objectives were to compare the dose-dependent effects of intravenous infusion of amylin and CCK-8 on gastric emptying and food intake in rats, and to assess whether physiological doses of amylin are effective. Amylin and CCK-8 inhibited gastric emptying with mean effective doses (ED50s) of 3 and 35 pmol · kg−1 · min−1 and maximal inhibitions of 60 and 65%, respectively. Amylin and CCK-8 inhibited food intake with ED50s of 8 a

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Mulyadi, Sri Mulyani, Tri Yuliati, Maulana Tegar, and Imam Ardhila. "Cytotoxic Activity of Pentacyclic Triterpene-3-Heptadecanoate Ester against Hela Cell Line and Its Docking Study." Media Pharmaceutica Indonesiana (MPI) 1, no. 1 (2017): 12. http://dx.doi.org/10.24123/mpi.v1i1.35.

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Pentacyclic triterpene-3-heptadecanoate (12,13-dihydro-α-amyrin-20,30-en-3-heptadecanoate)ester refers to the compound as a result of reaction between pentacyclic triterpene-3-ol(12,13-dihydro-α-amyrin-20,30-en-3-ol) and heptadecanoic acid. This research was aimed to conductcytotoxicity test of pentacyclic triterpene-3-heptadecanoate; 12,13-dihydro-α-amyrin-20,30-en-3-oland 12,13-dihydro-α-amyrin-20,30-en-3-acetate esters against Hela cell line. The activity assay wascarried out using MTT method. The results indicated that IC50 value of 12,13-dihydro-α-amyrin-3-heptadecanoate; 12,13-dihydro-α-

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Duffy, Sonya, Thomas A. Lutz, and Christina N. Boyle. "Rodent models of leptin receptor deficiency are less sensitive to amylin." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 315, no. 4 (2018): R856—R865. http://dx.doi.org/10.1152/ajpregu.00179.2018.

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The pancreatic hormone amylin is released from beta cells following nutrient ingestion and contributes to the control of body weight and glucose homeostasis. Amylin reduces food intake by activating neurons in the area postrema (AP). Amylin was also shown to synergize with the adipokine leptin, with combination therapy producing greater weight loss and food intake reduction than either hormone alone. Although amylin and leptin were initially thought to interact downstream of the AP in the hypothalamus, recent findings show that the two hormones can act on the same AP neurons, suggesting a more

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Hettiarachchi, M., S. Chalkley, S. M. Furler, et al. "Rat amylin-(8—37) enhances insulin action and alters lipid metabolism in normal and insulin-resistant rats." American Journal of Physiology-Endocrinology and Metabolism 273, no. 5 (1997): E859—E867. http://dx.doi.org/10.1152/ajpendo.1997.273.5.e859.

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To clarify roles of amylin, we investigated metabolic responses to rat amylin-(8—37), a specific amylin antagonist, in normal and insulin-resistant, human growth hormone (hGH)-infused rats. Fasting conscious rats were infused with saline or hGH, each with and without amylin-(8—37) (0.125 μmol/h), over 5.75 h. At 3.75 h, a hyperinsulinemic (100 mU/l) clamp with bolus 2-deoxy-d-[3H]glucose and [14C]glucose was started. hGH infusion led to prompt (2- to 3-fold) basal hyperamylinemia ( P < 0.02) and hyperinsulinemia. Amylin-(8—37) reduced plasma insulin ( P < 0.001) and enhanced several meas

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Frost, L. H. "Methylphenidate in Amytal-resistant mutism." Acta Psychiatrica Scandinavica 79, no. 4 (1989): 408–10. http://dx.doi.org/10.1111/j.1600-0447.1989.tb10278.x.

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30

Rees, Tayla A., Debbie L. Hay, and Christopher S. Walker. "Amylin antibodies frequently display cross-reactivity with CGRP: characterization of eight amylin antibodies." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 320, no. 5 (2021): R697—R703. http://dx.doi.org/10.1152/ajpregu.00338.2020.

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Amylin is a 37-amino acid endocrine hormone secreted from the pancreas in response to nutrient intake, acting centrally to promote meal-ending satiation. With many studies linking amylin action to the nervous system, determining the distribution or expression of amylin in the nervous system is critical. However, amylin shares sequence identity and structural homology to the related neuropeptide calcitonin gene-related peptide (CGRP). This creates challenges in identifying selective amylin antibodies that do not cross-react with CGRP, especially in neural tissues, where CGRP is densely packed i

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Na, Hana, Hua Tian, Zhengrong Zhang, et al. "Oral Amylin Treatment Reduces the Pathological Cascade of Alzheimer’s Disease in a Mouse Model." American Journal of Alzheimer's Disease & Other Dementiasr 36 (January 1, 2021): 153331752110128. http://dx.doi.org/10.1177/15333175211012867.

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Intraperitoneal injection of amylin or its analog reduces Alzheimer’s disease (AD) pathology in the brains. However, self-injecting amylin analogs is difficult for patients due to cognitive deficits. This work aims to study the effects of amylin on the brain could be achieved by oral delivery as some study reported that amylin receptor may be present in the gastrointestinal tract. A 6-week course of oral amylin treatment reduced components of AD pathology, including the levels of amyloid-β, phosphorylated tau, and ionized calcium binding adaptor molecule 1. The treatment reduced active forms o

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Lutz, Thomas A. "The role of amylin in the control of energy homeostasis." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 298, no. 6 (2010): R1475—R1484. http://dx.doi.org/10.1152/ajpregu.00703.2009.

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Amylin is an important player in the control of nutrient fluxes. Amylin reduces eating via a meal size effect by promoting meal-ending satiation. This effect seems to depend on a direct action in the area postrema (AP), which is an area rich in amylin receptors. Subsequent to the activation of AP neurons, the neural signal is conveyed to the forebrain via relays involving the nucleus of the solitary tract (NTS) and the lateral parabrachial nucleus (lPBN) to the lateral hypothalamic area (LHA) and other hypothalamic nuclei. While the NTS and lPBN seem to be necessary for amylin's eating inhibit

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Castle, Arthur L., Chia-Hua Kuo, and John L. Ivy. "Amylin influences insulin-stimulated glucose metabolism by two independent mechanisms." American Journal of Physiology-Endocrinology and Metabolism 274, no. 1 (1998): E6—E12. http://dx.doi.org/10.1152/ajpendo.1998.274.1.e6.

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The effects of amylin on fiber type-specific muscle glucose metabolism under hyperglycemic (10 mmol/l) and hyperinsulinemic (2.1 nmol/l) conditions were investigated using a rat hindlimb perfusion system. Amylin concentration ranged from 1 to 100 nM. Efficacy for inhibition of glucose uptake traced with 2-deoxyglucose by amylin was demonstrated in all three fiber types. The incorporation of 2-deoxy-[3H]glucose tracer decreased from control values by 41% in fast oxidative (FO), 36% in fast glycolytic (FG), and 37% in slow oxidative (SO) muscle with 100 nM amylin. Amylin increased intracellular

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Ye, Ji-Ming, Megan Lim-Fraser, Gregory J. Cooney, et al. "Evidence that amylin stimulates lipolysis in vivo: a possible mediator of induced insulin resistance." American Journal of Physiology-Endocrinology and Metabolism 280, no. 4 (2001): E562—E569. http://dx.doi.org/10.1152/ajpendo.2001.280.4.e562.

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The present study investigated the role of amylin in lipid metabolism and its possible implications for insulin resistance. In 5- to 7-h-fasted conscious rats, infusion of rat amylin (5 nmol/h for 4 h) elevated plasma glucose, lactate, and insulin ( P <0.05 vs. control, repeated-measures ANOVA) with peak values occurring within 60 min. Despite the insulin rise, plasma nonesterified fatty acids (NEFA) and glycerol were also elevated ( P < 0.001 vs. control), and these elevations (80% above basal) were sustained over the 4-h infusion period. Although unaltered in plasma, triglyceride conte

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Riediger, Thomas, Matthias Rauch, and Herbert A. Schmid. "Actions of amylin on subfornical organ neurons and on drinking behavior in rats." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 276, no. 2 (1999): R514—R521. http://dx.doi.org/10.1152/ajpregu.1999.276.2.r514.

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Amylin, a peptide hormone secreted by pancreatic β-cells after food intake, contributes to metabolic control by regulating nutrient influx into the blood, whereas insulin promotes nutrient efflux and storage. We now report that amylin activates neurons in the subfornical organ (SFO), a structure in which the lack of a functional blood-brain barrier and the presence of a high density of amylin receptors may render it accessible and sensitive to circulating amylin. In an in vitro slice preparation of the rat SFO, 73% of 78 neurons were excited by superfusion with rat amylin (10−8–10−7M); the rem

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Roth, Jonathan D., Heather Hughes, Eric Kendall, Alain D. Baron та Christen M. Anderson. "Antiobesity Effects of the β-Cell Hormone Amylin in Diet-Induced Obese Rats: Effects on Food Intake, Body Weight, Composition, Energy Expenditure, and Gene Expression". Endocrinology 147, № 12 (2006): 5855–64. http://dx.doi.org/10.1210/en.2006-0393.

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Effects of amylin and pair feeding (PF) on body weight and metabolic parameters were characterized in diet-induced obesity-prone rats. Peripherally administered rat amylin (300 μg/kg·d, 22d) reduced food intake and slowed weight gain: approximately 10% (P &lt; 0.05), similar to PF. Fat loss was 3-fold greater in amylin-treated rats vs. PF (P &lt; 0.05). Whereas PF decreased lean tissue (P &lt; 0.05 vs. vehicle controls; VEH), amylin did not. During wk 1, amylin and PF reduced 24-h respiratory quotient (mean ± se, 0.82 ± 0.0, 0.81 ± 0.0, respectively; P &lt; 0.05) similar to VEH

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Congiu, Terenzio, Mawadda Alghrably, Abdul-Hamid Emwas, et al. "Undercover Toxic Ménage à Trois of Amylin, Copper (II) and Metformin in Human Embryonic Kidney Cells." Pharmaceutics 13, no. 6 (2021): 830. http://dx.doi.org/10.3390/pharmaceutics13060830.

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In recent decades, type 2 diabetes complications have been correlated with amylin aggregation, copper homeostasis and metformin side effects. However, each factor was analyzed separately, and only in some rare cases copper/amylin or copper/metformin complexes were considered. We demonstrate for the first time that binary metformin/amylin and tertiary copper (II)/amylin/metformin complexes of high cellular toxicity are formed and lead to the formation of aggregated multi-level lamellar structures on the cell membrane. Considering the increased concentration of amylin, copper (II) and metformin

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Lutz, Thomas A., and Christelle Le Foll. "Endogenous amylin contributes to birth of microglial cells in arcuate nucleus of hypothalamus and area postrema during fetal development." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 316, no. 6 (2019): R791—R801. http://dx.doi.org/10.1152/ajpregu.00004.2019.

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Amylin acts in the area postrema (AP) and arcuate nucleus (ARC) to control food intake. Amylin also increases axonal fiber outgrowth from the AP→nucleus tractus solitarius and from ARC→hypothalamic paraventricular nucleus. More recently, exogenous amylin infusion for 4 wk was shown to increase neurogenesis in adult rats in the AP. Furthermore, amylin has been shown to enhance leptin signaling in the ARC and ventromedial nucleus of the hypothalamus (VMN). Thus, we hypothesized that endogenous amylin could be a critical factor in regulating cell birth in the ARC and AP and that amylin could also

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Edvinsson, Lars, Peter J. Goadsby, and Rolf Uddman. "Amylin: Localization, Effects on Cerebral Arteries and on Local Cerebral Blood Flow in the Cat." Scientific World JOURNAL 1 (2001): 168–80. http://dx.doi.org/10.1100/tsw.2001.23.

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Amylin and adrenomedullin are two peptides structurally related to calcitonin gene-related peptide (CGRP). We studied the occurrence of amylin in trigeminal ganglia and cerebral blood vessels of the cat with immunocytochemistry and evaluated the role of amylin and adrenomedullin in the cerebral circulation by in vitro and in vivo pharmacology. Immunocytochemistry revealed that numerous nerve cell bodies in the trigeminal ganglion contained CGRP immunoreactivity (-ir); some of these also expressed amylin-ir but none adrenomedullin-ir. There were numerous nerve fibres surrounding cerebral blood

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Flood, J. F., S. A. Farr, H. J. Perry III, F. E. Kaiser, P. M. K. Morley, and J. E. Morley. "Effects of amylin on appetite regulation and memory." Canadian Journal of Physiology and Pharmacology 73, no. 7 (1995): 1042–46. http://dx.doi.org/10.1139/y95-147.

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Amylin has been demonstrated to decrease food intake in mice and rats. Amylin is effective when delivered both peripherally and directly into the central nervous system. Amylin's effect on food intake is not aversive. Amylin may produce its effect on food intake by modulating nitric oxide synthesis. Calcitonin gene related peptide also decreases food intake after peripheral and central administration. In addition, amylin has been demonstrated to modulate memory at both peripheral and central sites.Key words: appetite, retention, satiety, memory, amylin.

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KO, Tetsumori, Wataru TAKAYAMA, Takanori NISHIMORI, Shinsuke KAKUTA, Hiroo YANAGIBASHI, and Makoto SUGAYA. "A case of Amyand's hernia." Nihon Rinsho Geka Gakkai Zasshi (Journal of Japan Surgical Association) 73, no. 9 (2012): 2431–38. http://dx.doi.org/10.3919/jjsa.73.2431.

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Beaumont, K., C. X. Moore, R. A. Pittner, et al. "Differential antagonism of amylin's metabolic and vascular actions with amylin receptor antagonists." Canadian Journal of Physiology and Pharmacology 73, no. 7 (1995): 1025–29. http://dx.doi.org/10.1139/y95-144.

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High affinity amylin binding sites are present in the rat nucleus accumbens. These sites bind [125I]amylin with an affinity of 27 pM and have high affinity for salmon calcitonin (sCT) and moderately high affinity for calcitonin gene related peptide (CGRP). N-terminally truncated peptides were tested for their ability to compete for [125I]amylin binding to these sites and to antagonize the metabolic and vascular actions of amylin. CGRP(8–37), sCT(8–32), and ac-[Asn30,Tyr32]sCT(8–32) (AC187) inhibited [125I]amylin binding to rat nucleus accumbens. Order of potency at inhibiting amylin binding (A

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Pieber, T. R., J. Roitelman, Y. Lee, K. L. Luskey, and D. T. Stein. "Direct plasma radioimmunoassay for rat amylin-(1-37): concentrations with acquired and genetic obesity." American Journal of Physiology-Endocrinology and Metabolism 267, no. 1 (1994): E156—E164. http://dx.doi.org/10.1152/ajpendo.1994.267.1.e156.

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Amylin (islet-associated polypeptide) is a 37-amino acid peptide that is cosecreted with insulin from the pancreatic beta-cell. Accurate measurement of its plasma levels is important for delineating the physiological range over which amylin acts. We describe a reproducible, highly specific, and sensitive radioimmunoassay for direct measurement of plasma amylin-(1-37). We measured changes in portal and systemic plasma amylin and insulin in three groups of anesthetized rats: lean young adult and old adult Wistar rats with acquired obesity, and Wistar fatty [WDF/TaFa (fa/fa)] rats, a model of gen

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Hay, Debbie L. "Amylin." Headache: The Journal of Head and Face Pain 57 (May 2017): 89–96. http://dx.doi.org/10.1111/head.13077.

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Phillips, Liza Kirsty, and Michael Horowitz. "Amylin." Current Opinion in Endocrinology & Diabetes 13, no. 2 (2006): 191–98. http://dx.doi.org/10.1097/01.med.0000216969.59375.39.

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Jara-Almonte Edwards, Beatriz, and John E. Morley. "Amylin." Life Sciences 51, no. 25 (1992): 1899–912. http://dx.doi.org/10.1016/0024-3205(92)90106-y.

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Guerreiro, Luiz H., Daniel DA Silva, Mauro Sola-Penna, Daniella M. Mizurini, and Luís M. T. R. Lima. "Amylin induces hypoglycemia in mice." Anais da Academia Brasileira de Ciências 85, no. 1 (2013): 349–54. http://dx.doi.org/10.1590/s0001-37652013005000011.

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Amylin is a 37-aminoacid pancreatic protein that exerts control over several metabolic events such as glycemia and lacticemia. Amylin has long been shown to induce increases in arterial plasma glucose. We decided to investigate whether amylin plays additional roles in the glucose metabolism. We evaluated glucose homeostasis using whole blood from the tail tip of fasting, conscious, unrestrained normal and streptozotocyn-induced diabetic mice following subcutaneous administration of mouse amylin. Subcutaneous injection of 1 μg mouse amylin caused a transient decrease in whole blood glucose in b

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Wookey, Peter J., Loredanna Xuereb, Christos Tikellis, and Mark E. Cooper. "Amylin in the Periphery." Scientific World JOURNAL 3 (2003): 163–75. http://dx.doi.org/10.1100/tsw.2003.17.

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Amylin (islet amyloid polypeptide) is a peptide synthesized principally in the b-cells of the pancreatic islets together with insulin and has actions as a hormone, growth factor, and modifier of behavior. As a hormone, amylin acts to modify gastric motility, renal resorption, and has metabolic actions. It is postulated that the principal function of amylin as a hormone is the activation of physiological processes associated with feeding. As a growth factor, amylin acts on bone cells, renal proximal tubular cells, and islet b-cells. Amylin has important targets in the brain that mediate its act

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Gómez-Foix, A. M., J. E. Rodriguez-Gil, and J. J. Guinovart. "Anti-insulin effects of amylin and calcitonin-gene-related peptide on hepatic glycogen metabolism." Biochemical Journal 276, no. 3 (1991): 607–10. http://dx.doi.org/10.1042/bj2760607.

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To evaluate the effects of amylin and calcitonin-gene-related peptide (CGRP) as anti-insulin agents in hepatic tissue, we have studied whether these two agents counteracted the action of insulin on glycogen metabolism in isolated rat hepatocytes. In this system insulin stimulates [14C]glucose incorporation into glycogen and activates glycogen synthase. Incubation of the cells with insulin in the presence of amylin or CGRP markedly blocked the insulin stimulation of these two parameters, whereas amylin or CGRP acting alone did not induce any effect. We also examined the ability of amylin and CG

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Harris, P. J., M. E. Cooper, S. Hiranyachattada, et al. "Amylin stimulates proximal tubular sodium transport and cell proliferation in the rat kidney." American Journal of Physiology-Renal Physiology 272, no. 1 (1997): F13—F21. http://dx.doi.org/10.1152/ajprenal.1997.272.1.f13.

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In autoradiographic studies in anesthetized rats, 125I-labeled amylin binding was associated with proximal convoluted tubules but not distal tubules, interstitium, or glomeruli in the renal cortex. Split-drop micropuncture experiments showed that perfusion of the peritubular capillaries with amylin (10(-9) M) stimulated proximal tubular fluid absorption by 28%. This effect was inhibited by luminal addition of ethylisopropylamiloride, indicating mediation by a brush-border Na+/H+ exchanger. Intravenous infusion of an amylin binding antagonist, AC-187, reduced proximal fluid reabsorption (22%) i

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