WordNet

a hormone secreted by the pancreas; stimulates increases in blood sugar levels in the blood (thus opposing the action of insulin)

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2014/12/17 20:05:03」(JST)

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Glucagon is a peptide hormone, produced by alpha cells of the pancreas, that raises the concentration of glucose in the bloodstream. Its effect is opposite that of insulin, which lowers the glucose concentration.^[1] The pancreas releases glucagon when the concentration of glucose in the bloodstream falls too low. Glucagon causes the liver to convert stored glycogen into glucose, which is released into the bloodstream. High blood glucose levels stimulate the release of insulin. Insulin allows glucose to be taken up and used by insulin-dependent tissues. Thus, glucagon and insulin are part of a feedback system that keeps blood glucose levels at a stable level. Glucagon belongs to a family of several other related hormones.

1 Function
2 Medical uses
- 2.1 Hypoglycemia
- 2.2 Beta blocker overdose
- 2.3 Anaphylaxis
- 2.4 Impacted food bolus
3 Adverse effects
- 3.1 Contraindications
4 Mechanism of action
5 Physiology
- 5.1 Production
- 5.2 Regulation
6 Structure
7 Pathology
8 History
- 8.1 Etymology
9 See also
10 References
11 Further reading

Function

Glucagon generally elevates the concentration of glucose in the blood by promoting gluconeogenesis and glycogenolysis.

Glucose is stored in the liver in the form of the polysaccharide glycogen, which is a glucan (a polymer made up of glucose molecules). Liver cells (hepatocytes) have glucagon receptors. When glucagon binds to the glucagon receptors, the liver cells convert the glycogen into individual glucose molecules and release them into the bloodstream, in a process known as glycogenolysis. As these stores become depleted, glucagon then encourages the liver and kidney to synthesize additional glucose by gluconeogenesis. Glucagon turns off glycolysis in the liver, causing glycolytic intermediates to be shuttled to gluconeogenesis.

Glucagon also regulates the rate of glucose production through lipolysis. Glucagon induces lipolysis in humans under conditions of insulin suppression (such as Diabetes mellitus type 1).^[2]

Glucagon production appears to be dependent on the central nervous system through pathways yet to be defined. In invertebrate animals, eyestalk removal has been reported to affect glucagon production. Excising the eyestalk in young crayfish produces glucagon-induced hyperglycemia.^[3]

Medical uses

Hypoglycemia

An injectable form of glucagon is vital first aid in cases of severe hypoglycemia when the victim is unconscious or for other reasons cannot take glucose orally. The dose for an adult is typically 1 milligram, and the glucagon is given by intramuscular, intravenous or subcutaneous injection, and quickly raises blood glucose levels. To use the injectable form, it must be reconstituted prior to use, a step that requires a sterile diluent to be injected into a vial containing powdered glucagon, because the hormone is highly unstable when dissolved in solution. When dissolved in a fluid state, glucagon can form amyloid fibrils, or tightly woven chains of proteins made up of the individual glucagon peptides, and once glucagon begins to fibrilize, it becomes useless when injected, as the glucagon cannot be absorbed and used by the body. The reconstitution process makes using glucagon cumbersome, although there are a number of products now in development from a number of companies that aim to make the product easier to use.

Beta blocker overdose

Anecdotal evidence suggests a benefit of higher doses of glucagon in the treatment of overdose with beta blockers; the likely mechanism of action is the increase of cAMP in the myocardium, in effect bypassing the β-adrenergic second messenger system.^[4]

Anaphylaxis

Some people who have anaphylaxis and are on beta blockers are resistant to epinephrine. In this situation glucagon intravenously may be useful to treat their low blood pressure.^[5]

Impacted food bolus

Glucagon relaxes the lower esophageal sphincter and may be used in those with an impacted food bolus in the esophagus ("steakhouse syndrome").^[6] There is little evidence for glucagon's effectiveness in this condition,^[7]^[8]^[9] and glucagon may induce nausea and vomiting,^[9] but considering the safety of glucagon this is still considered an acceptable option as long it does not lead to delays in arranging other treatments.^[10]^[11]

Adverse effects

Glucagon acts very quickly; common side-effects include headache and nausea.

Drug interactions: Glucagon interacts only with oral anticoagulants, increasing the tendency to bleed.^[12]

Contraindications

While glucagon can be used clinically to treat various forms of hypoglycemia, it is severely contraindicated in patients with pheochromocytoma, as the drug interaction with elevated levels of adrenaline produced by the tumor may produce an exponential increase in blood sugar levels, leading to a hyperglycemic state, which may incur a fatal elevation in blood pressure.^[13] Likewise, glucagon is contraindicated in patients with an insulinoma, as its use may lead to rebound hypoglycemia.^[13]

Mechanism of action

Glucagon binds to the glucagon receptor, a G protein-coupled receptor, located in the plasma membrane. The conformation change in the receptor activates G proteins, a heterotrimeric protein with α, β, and γ subunits. When the G protein interacts with the receptor, it undergoes a conformational change that results in the replacement of the GDP molecule that was bound to the α subunit with a GTP molecule. This substitution results in the releasing of the α subunit from the β and γ subunits. The alpha subunit specifically activates the next enzyme in the cascade, adenylate cyclase.

Adenylate cyclase manufactures cyclic adenosine monophosphate (cyclic AMP or cAMP), which activates protein kinase A (cAMP-dependent protein kinase). This enzyme, in turn, activates phosphorylase kinase, which, in turn, phosphorylates glycogen phosphorylase, converting into the active form called phosphorylase A. Phosphorylase A is the enzyme responsible for the release of glucose-1-phosphate from glycogen polymers.

Additionally, the coordinated control of glycolysis and gluconeogenesis in the liver is adjusted by the phosphorylation state of the enzymes that catalyze the formation of a potent activator of glycolysis called fructose-2,6-bisphosphate.^[14] The enzyme protein kinase A that was stimulated by the cascade initiated by glucagon will also phosphorylate a single serine residue of the bifunctional polypeptide chain containing both the enzymes fructose-2,6-bisphosphatase and phosphofructokinase-2. This covalent phosphorylation initiated by glucagon activates the former and inhibits the latter. This regulates the reaction catalyzing fructose-2,6-bisphosphate (a potent activator of phosphofructokinase-1, the enzyme that is the primary regulatory step of glycolysis)^[15] by slowing the rate of its formation, thereby inhibiting the flux of the glycolysis pathway and allowing gluconeogenesis to predominate. This process is reversible in the absence of glucagon (and thus, the presence of insulin).

Glucagon stimulation of PKA also inactivates the glycolytic enzyme pyruvate kinase.^[16]

Physiology

Production

A microscopic image stained for glucagon

The hormone is synthesized and secreted from alpha cells (α-cells) of the islets of Langerhans, which are located in the endocrine portion of the pancreas. In rodents, the alpha cells are located in the outer rim of the islet. Human islet structure is much less segregated, and alpha cells are distributed throughout the islet in close proximity to beta cells.

Regulation

Secretion of glucagon is stimulated by:

Hypoglycemia
Epinephrine (via β2, α2,^[17] and α1^[18] adrenergic receptors)
Arginine
Alanine (often from muscle-derived pyruvate/glutamate transamination (see alanine transaminase reaction).
Acetylcholine^[19]
Cholecystokinin

Secretion of glucagon is inhibited by:

Somatostatin
Insulin (via GABA)^[20]
PPARγ/retinoid X receptor heterodimer.^[21]
Increased free fatty acids and keto acids into the blood^{[citation needed]}
Increased urea production

Structure

Glucagon is a 29-amino acid polypeptide. Its primary structure in humans is: NH₂-His-Ser-Gln-Gly-Thr-Phe-Thr-Ser-Asp-Tyr-Ser-Lys-Tyr-Leu-Asp-Ser-Arg-Arg-Ala-Gln-Asp-Phe-Val-Gln-Trp-Leu-Met-Asn-Thr-COOH.

The polypeptide has a molecular weight of 3485 daltons. Glucagon is a peptide (nonsteroid) hormone.

Glucagon is generated from the cleavage of proglucagon by proprotein convertase 2 in pancreatic islet α cells. In intestinal L cells, proglucagon is cleaved to the alternate products glicentin, GLP-1 (an incretin), IP-2, and GLP-2 (promotes intestinal growth).^[22]

Pathology

Abnormally elevated levels of glucagon may be caused by pancreatic tumors, such as glucagonoma, symptoms of which include necrolytic migratory erythema, reduced amino acids, and hyperglycemia. It may occur alone or in the context of multiple endocrine neoplasia type 1.

History

In the 1920s, Kimball and Murlin studied pancreatic extracts, and found an additional substance with hyperglycemic properties. They described glucagon in 1923.^[23] The amino acid sequence of glucagon was described in the late 1950s.^[24] A more complete understanding of its role in physiology and disease was not established until the 1970s, when a specific radioimmunoassay was developed.

Etymology

Glucagon was named in 1923, probably from the Greek γλυκός sweet, and ἄγειν to lead.^[25]

References

^ Reece J, Campbell N (2002). Biology. San Francisco: Benjamin Cummings. ISBN 0-8053-6624-5.
^ LILJENQUIST, JOHN E. et al (January 1974). "Effects of Glucagon on Lipolysis and Ketogenesis in Normal and Diabetic Men". J Clin Invest. 53 (1): 190–7. doi:10.1172/JCI107537. PMC 301453. PMID 4808635.
^ Leinen RL, Giannini AJ (1983). "Effect of eyestalk removal on glucagon induced hyperglycemia in crayfish". Society for Neuroscience Abstracts 9: 604.
^ White CM (May 1999). "A review of potential cardiovascular uses of intravenous glucagon administration". J Clin Pharmacol 39 (5): 442–7. PMID 10234590.
^ Tang AW (2003). "A practical guide to anaphylaxis". Am Fam Physician 68 (7): 1325–32. PMID 14567487.
^ Ko HH, Enns R (October 2008). "Review of food bolus management". Can. J. Gastroenterol. 22 (10): 805–8. PMC 2661297. PMID 18925301.
^ Arora S, Galich P (March 2009). "Myth: glucagon is an effective first-line therapy for esophageal foreign body impaction". CJEM 11 (2): 169–71. PMID 19272219.
^ Leopard, D; Fishpool, S; Winter, S (Sep 2011). "The management of oesophageal soft food bolus obstruction: a systematic review.". Annals of the Royal College of Surgeons of England 93 (6): 441–4. doi:10.1308/003588411X588090. PMC 3369328. PMID 21929913.
^ ^a ^b Weant, KA; Weant, MP (Apr 1, 2012). "Safety and efficacy of glucagon for the relief of acute esophageal food impaction.". American journal of health-system pharmacy : AJHP : official journal of the American Society of Health-System Pharmacists 69 (7): 573–7. doi:10.2146/ajhp100587. PMID 22441787.
^ Ikenberry, Steven O.; Jue, Terry L.; Anderson, Michelle A.; Appalaneni, Vasundhara; Banerjee, Subhas; Ben-Menachem, Tamir; Decker, G. Anton; Fanelli, Robert D.; Fisher, Laurel R.; Fukami, Norio; Harrison, M. Edwyn; Jain, Rajeev; Khan, Khalid M.; Krinsky, Mary Lee; Maple, John T.; Sharaf, Ravi; Strohmeyer, Laura; Dominitz, Jason A. (June 2011). "Management of ingested foreign bodies and food impactions". Gastrointestinal Endoscopy 73 (6): 1085–1091. doi:10.1016/j.gie.2010.11.010. PMID 21628009. Cite uses deprecated parameters (help)
^ Chauvin, A; Viala, J; Marteau, P; Hermann, P; Dray, X (Jul 2013). "Management and endoscopic techniques for digestive foreign body and food bolus impaction.". Digestive and liver disease : official journal of the Italian Society of Gastroenterology and the Italian Association for the Study of the Liver 45 (7): 529–42. doi:10.1016/j.dld.2012.11.002. PMID 23266207.
^ Koch-Weser J (March 1970). "Potentiation by glucagon of the hypoprothrombinemic action of warfarin". Ann. Intern. Med. 72 (3): 331–5. doi:10.7326/0003-4819-72-3-331. PMID 5415418.
^ ^a ^b "Information for the Physician: Glucagon for Injection (rDNA origin)". Eli Lilly and Company. Retrieved 2011-11-19.
^ Hue L, Rider MH (1987). "Role of fructose 2,6-bisphosphate in the control of glycolysis in mammalian tissues". Biochem. J. 245 (2): 313–24. PMC 1148124. PMID 2822019.
^ Claus TH, El-Maghrabi MR, Regen DM, Stewart HB, McGrane M, Kountz PD, Nyfeler F, Pilkis J, Pilkis SJ (1984). "The role of fructose 2,6-bisphosphate in the regulation of carbohydrate metabolism". Curr. Top. Cell. Regul. 23: 57–86. PMID 6327193.
^ Feliú JE, Hue L, Hers HG (1976). "Hormonal control of pyruvate kinase activity and of gluconeogenesis in isolated hepatocytes". Proc. Natl. Acad. Sci. U.S.A. 73 (8): 2762–6. doi:10.1073/pnas.73.8.2762. PMC 430732. PMID 183209.
^ Layden BT, Durai V, Lowe WL (2010). "G-Protein-Coupled Receptors, Pancreatic Islets, and Diabetes". Nature Education 3 (9): 13.
^ Skoglund G, Lundquist I, Ahrén B (November 1987). "Alpha 1- and alpha 2-adrenoceptor activation increases plasma glucagon levels in the mouse". Eur. J. Pharmacol. 143 (1): 83–8. doi:10.1016/0014-2999(87)90737-0. PMID 2891547.
^ Honey RN, Weir GC (October 1980). "Acetylcholine stimulates insulin, glucagon, and somatostatin release in the perfused chicken pancreas". Endocrinology 107 (4): 1065–8. doi:10.1210/endo-107-4-1065. PMID 6105951.
^ Xu E, Kumar M, Zhang Y, Ju W, Obata T, Zhang N, Liu S, Wendt A, Deng S, Ebina Y, Wheeler MB, Braun M, Wang Q (January 2006). "Intra-islet insulin suppresses glucagon release via GABA-GABAA receptor system". Cell Metab. 3 (1): 47–58. doi:10.1016/j.cmet.2005.11.015. PMID 16399504.
^ Krätzner R, Fröhlich F, Lepler K, Schröder M, Röher K, Dickel C, Tzvetkov MV, Quentin T, Oetjen E, Knepel W. (October 2007). "A Peroxisome Proliferator-Activated Receptor γ-Retinoid X Receptor Heterodimer Physically Interacts with the Transcriptional Activator PAX6 to Inhibit Glucagon Gene Transcription". Molecular Pharmacology 73 (2): 509–517. doi:10.1124/mol.107.035568. PMID 17962386.
^ Orskov C, Holst JJ, Poulsen SS, Kirkegaard P (November 1987). "Pancreatic and intestinal processing of proglucagon in man". Diabetologia 30 (11): 874–81. PMID 3446554.
^ Kimball C, Murlin J (1923). "Aqueous extracts of pancreas III. Some precipitation reactions of insulin". J. Biol. Chem. 58 (1): 337–348.
^ Bromer W, Winn L, Behrens O (1957). "The amino acid sequence of glucagon V. Location of amide groups, acid degradation studies and summary of sequential evidence". J. Am. Chem. Soc. 79 (11): 2807–2810. doi:10.1021/ja01568a038.
^ glucagon on dictionary.com

UpToDate Contents

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1. 2型糖尿病の治療のためのジペプチジルペプチダーゼ4（DPP-4）阻害剤 dipeptidyl peptidase 4 dpp 4 inhibitors for the treatment of type 2 diabetes mellitus
2. 乳児および小児における低血糖に対するアプローチ approach to hypoglycemia in infants and children
3. 2型糖尿病治療のためのGlucagon-like peptide-1受容体拮抗剤 glucagon like peptide 1 receptor agonists for the treatment of type 2 diabetes mellitus
4. Management and outcome of neonatal hypoglycemia
5. 糖尿病でない成人における低血糖症：診断的アプローチ hypoglycemia in adults without diabetes mellitus diagnostic approach

English Journal

Expression and purification of optimized rolGLP-1, a novel GLP-1 analog, in Escherichia coli BL21(DE3) and its good glucoregulatory effect on type 2 diabetic mice.

Ma B, Tu P, Zhao X, Zhang Y, Wang Y, Ma C, Ji Y, Li X, Abbas SA, Li M1.
Current pharmaceutical biotechnology.Curr Pharm Biotechnol.2014 Nov;14(11):985-94.
Glucagon-like peptide-1 (GLP-1) is an incretin hormone that decreases postprandial glycemic excursions by enhancing insulin secretion but with short half-life due to rapid inactivation by enzymatic N-terminal truncation. Therefore, efforts are being made to improve the stability of GLP-1 via modifyi
PMID 24372241

Body weight loss, reduced urge for palatable food and increased release of GLP-1 through daily supplementation with green-plant membranes for three months in overweight women.

Montelius C1, Erlandsson D1, Vitija E1, Stenblom EL1, Egecioglu E1, Erlanson-Albertsson C2.
Appetite.Appetite.2014 Oct;81:295-304. doi: 10.1016/j.appet.2014.06.101. Epub 2014 Jun 30.
The frequency of obesity has risen dramatically in recent years but only few effective and safe drugs are available. We investigated if green-plant membranes, previously shown to reduce subjective hunger and promote satiety signals, could affect body weight when given long-term. 38 women (40-65 ye
PMID 24993695

Developments of glucagon like peptide-1 (GLP-1) and long-acting analogs in clinical and preclinical studies for treatment of type 2 diabetes.

Li Y, Tang L, Gong M1.
Current pharmaceutical biotechnology.Curr Pharm Biotechnol.2014 Oct;14(9):835-41.
The outstanding physiological functions of glucagon-like peptide-1 make it a promising drug candidate for blood glucose regulation in type 2 diabetes. However, the short half-life of GLP-1 limited its widely clinical utility due to the rapid degradation by dipeptidyl peptidase IV (DPP-IV) and renal
PMID 24372261

Japanese Journal

消化管ペプチドの神経を介したエネルギー代謝調節機構 : 消化管と中枢の臓器連関 (特集ホルモン作用と臓器相関)

土持若葉,上野浩晶,中里雅光
内分泌・糖尿病・代謝内科 38(1), 3-8, 2014-01
NAID 40019957511

Immunohistochemical Study on Glucagon-Like Peptide-1 (GLP-1) and Pituitary Adenylate Cyclase Activating Peptide (PACAP) in the Small Intestine of Muscovy Duck during the Prehatching and Posthatching Periods

Ding Baoan,Lenzi Carla,Pirone Andrea
Journal of poultry science 51(1), 35-41, 2014-01
NAID 40019956444

治療薬 GLP-1受容体作動薬による治療 (特集糖尿病 : 診断・治療Update)

原田範雄,稲垣暢也
最新医学 69(1), 97-104, 2014-01
NAID 40019939355

Related Pictures

★リンクテーブル★

リンク元	「グルカゴン」
拡張検索	「glucagon receptor」「glucagon-propranolol test」「propranolol-glucagon test」「glucagonoma syndrome」「preproglucagon」

「グルカゴン」

Glucagon
Clinical data
Legal status	?
Identifiers
CAS number
ATC code	?
PubChem	CID 16186314
IUPHAR ligand	1136
ChemSpider	10481928
UNII	76LA80IG2G
ChEMBL	CHEMBL266481
Chemical data
Formula	C153H225N43O49S
Mol. mass	3482.747314
	InChI InChI=1S/C153H225N43O49S/c1-72(2)52-97(133(226)176-96(47-51-246-11)132(225)184-104(60-115(159)209)143(236)196-123(78(10)203)151(244)245)179-137(230)103(58-83-64-167-89-29-19-18-28-87(83)89)183-131(224)95(43-46-114(158)208)177-148(241)120(74(5)6)194-141(234)101(54-79-24-14-12-15-25-79)182-138(231)105(61-117(211)212)185-130(223)94(42-45-113(157)207)171-124(217)75(7)170-127(220)91(31-22-49-165-152(160)161)172-128(221)92(32-23-50-166-153(162)163)174-146(239)110(69-199)191-140(233)107(63-119(215)216)186-134(227)98(53-73(3)4)178-135(228)99(56-81-33-37-85(204)38-34-81)180-129(222)90(30-20-21-48-154)173-145(238)109(68-198)190-136(229)100(57-82-35-39-86(205)40-36-82)181-139(232)106(62-118(213)214)187-147(240)111(70-200)192-150(243)122(77(9)202)195-142(235)102(55-80-26-16-13-17-27-80)188-149(242)121(76(8)201)193-116(210)66-168-126(219)93(41-44-112(156)206)175-144(237)108(67-197)189-125(218)88(155)59-84-65-164-71-169-84/h12-19,24-29,33-40,64-65,71-78,88,90-111,120-123,167,197-205H,20-23,30-32,41-63,66-70,154-155H2,1-11H3,(H2,156,206)(H2,157,207)(H2,158,208)(H2,159,209)(H,164,169)(H,168,219)(H,170,220)(H,171,217)(H,172,221)(H,173,238)(H,174,239)(H,175,237)(H,176,226)(H,177,241)(H,178,228)(H,179,230)(H,180,222)(H,181,232)(H,182,231)(H,183,224)(H,184,225)(H,185,223)(H,186,227)(H,187,240)(H,188,242)(H,189,218)(H,190,229)(H,191,233)(H,192,243)(H,193,210)(H,194,234)(H,195,235)(H,196,236)(H,211,212)(H,213,214)(H,215,216)(H,244,245)(H4,160,161,165)(H4,162,163,166)/t75-,76+,77+,78?,88-,90-,91-,92-,93-,94-,95-,96-,97-,98-,99-,100-,101-,102-,103-,104-,105-,106-,107-,108-,109-,110-,111-,120-,121-,122-,123-/m0/s1 ; Key:MASNOZXLGMXCHN-GVLKBUBXSA-N ;
(what is this?) (verify)

Glucagon
	; PDB rendering based on 1GCN.
Available structures
PDB	Ortholog search: PDBe, RCSB
List of PDB id codes
	1BH0, 1D0R, 1NAU, 2G49, 2L63, 2L64, 2M5P, 2M5Q, 3IOL, 4APD
Identifiers
Symbols	GCG ; GLP1; GLP2; GRPP
External IDs	OMIM: 138030 MGI: 95674 HomoloGene: 136497 ChEMBL: 5736 GeneCards: GCG Gene
Gene ontology
Molecular function	• receptor binding; • hormone activity; • protein binding; • glucagon receptor binding; • identical protein binding;
Cellular component	• extracellular region; • extracellular space; • endoplasmic reticulum lumen; • plasma membrane; • secretory granule lumen;
Biological process	• energy reserve metabolic process; • signal transduction; • G-protein coupled receptor signaling pathway; • adenylate cyclase-modulating G-protein coupled receptor signaling pathway; • feeding behavior; • cell proliferation; • protein kinase A signaling; • positive regulation of peptidyl-threonine phosphorylation; • positive regulation of cAMP biosynthetic process; • positive regulation of protein binding; • positive regulation of peptidyl-serine phosphorylation; • positive regulation of insulin secretion involved in cellular response to glucose stimulus; • response to starvation; • negative regulation of apoptotic process; • cellular protein metabolic process; • small molecule metabolic process; • positive regulation of protein kinase activity; • regulation of insulin secretion; • positive regulation of ERK1 and ERK2 cascade; • cellular response to glucagon stimulus; • positive regulation of calcium ion import; • negative regulation of execution phase of apoptosis; • negative regulation of intrinsic apoptotic signaling pathway;
	Sources: Amigo / QuickGO
RNA expression pattern
	More reference expression data
Orthologs
	This box: view; talk; edit;

　　[★]

英: glucagon (Z)
商: グルカゴンGノボ
関: ホルモン

分類

消化管ホルモン

性状

ペプチド
3.5kDa

産生組織

膵臓 - α細胞

標的組織

全身？
主に肝臓

受容体

作用

血糖上昇作用

血糖上昇：グリコーゲン分解促進　→　血糖値上昇

慢性膵炎などで膵内分泌機能が低下した場合、低血糖を起こすとグルカゴンの分泌も低下しているため、糖尿病患者のインスリン投与過多による低血糖よりも重篤らしい。

インスリン分泌促進作用
成長ホルモン分泌促進作用
消化管運動抑制作用：消化管内視鏡を行うとき、副交感神経拮抗薬で消化管の運動を押さえますが、現病として緑内障がある時には、グルカゴンを代わりに使うことがあります。ケド高いらしい。(2020年現在1mg \1600-1800)

分泌の調整

亢進：アミノ酸(アルギニン)、グルコース(↓血糖)
抑制：グルコース(↑血糖値)、遊離脂酸、ソマトスタチン

分子機構

生合成

臨床関連

グルカゴン欠乏
グルカゴン過剰

グルカゴノーマ

薬効薬理

1. 消化管に対する作用

消化管の運動を抑制し、胃酸、膵液の分泌を抑制する。これは平滑筋への直接作用による弛緩作用と考えられている。

2. 血糖値に対する作用

グルカゴンは肝臓のアデニル酸シクラーゼを活性化させ、細胞内cAMP濃度を上昇させる。これにより、グリコーゲンの分解及び糖新生を促進させ、血糖値が上昇する。

3. 下垂体に対する作用

グルカゴン投与により一時的に血糖値が上昇するが、60～90分後にリバウンド作用により血糖値が低下する。その時、下垂体からの成長ホルモン分泌を刺激すると考えられている。

禁忌

グルカゴンGノボ注射用1mg

1. 褐色細胞腫及びその疑いのある患者〔急激な昇圧発作を起こすことがある。〕
2. 本剤の成分に対し過敏症の既往歴のある患者

参考

グルカゴンGノボ注射用1mg

http://www.info.pmda.go.jp/go/pack/7229402D1036_1_02/7229402D1036_1_02?view=body

「glucagon receptor」

　　[★]

グルカゴン受容体、グルカゴンレセプター

「glucagon-propranolol test」

　　[★] プロプラノロール・グルカゴン試験

「propranolol-glucagon test」