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Glucagon
Glucagon is a peptide hormone, produced by alpha cells of the pancreas. It raises concentration of glucose and fatty acids in the bloodstream, and is considered to be the main catabolic hormone of the body. It is also used as a Glucagon (medication), medication to treat a number of health conditions. Its effect is opposite to that of insulin, which lowers extracellular glucose. It is produced from proglucagon, encoded by the ''GCG'' gene. The pancreas releases glucagon when the amount of glucose in the bloodstream is too low. Glucagon causes the liver to engage in glycogenolysis: converting stored glycogen into glucose, which is released into the bloodstream. High blood-glucose levels, on the other hand, 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 stable. Glucagon increases energy expenditure and is elevated under conditions of ...
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Alpha Cells
Alpha cells (α cells) are endocrine cells that are found in the Islets of Langerhans in the pancreas. Alpha cells secrete the peptide hormone glucagon in order to increase glucose levels in the blood stream. Discovery Islets of Langerhans were first discussed by Paul Langerhans in his medical thesis in 1869. This same year, Laguesse named them after Langerhans. At first, there was a lot of controversy about what the Islets were made of and what they did. It appeared that all of the cells were the same within the Islet, but were histologically distinct from acini cells. Laguesse discovered that the cells within the Islets of Langerhans contained granules that distinguished them from acini cells. He also determined that these granules were products of the metabolism of the cells in which they were contained. Michael Lane was the one to discover that alpha cells were histologically different than beta cells in 1907. Before the function of alpha cells was discovered, the function o ...
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Glucagon (medication)
Glucagon, sold under the brand name Baqsimi among others, is a medication and hormone. As a medication it is used to treat low blood sugar, beta blocker overdose, calcium channel blocker overdose, and those with anaphylaxis who do not improve with epinephrine. It is given by injection into a vein, muscle, or under the skin. A version given in the nose is also available. Common side effects include vomiting. Other side effects include low blood potassium and low blood pressure. It is not recommended in people who have a pheochromocytoma or insulinoma. Use in pregnancy has not be found to be harmful to the baby. Glucagon is in the glycogenolytic family of medications. It works by causing the liver to break down glycogen into glucose. Glucagon was approved for medical use in the United States in 1960. It is on the World Health Organization's List of Essential Medicines. It is a manufactured form of the glucagon hormone. A generic version became available in the United S ...
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Pancreas
The pancreas is an organ of the digestive system and endocrine system of vertebrates. In humans, it is located in the abdomen behind the stomach and functions as a gland. The pancreas is a mixed or heterocrine gland, i.e. it has both an endocrine and a digestive exocrine function. 99% of the pancreas is exocrine and 1% is endocrine. As an endocrine gland, it functions mostly to regulate blood sugar levels, secreting the hormones insulin, glucagon, somatostatin, and pancreatic polypeptide. As a part of the digestive system, it functions as an exocrine gland secreting pancreatic juice into the duodenum through the pancreatic duct. This juice contains bicarbonate, which neutralizes acid entering the duodenum from the stomach; and digestive enzymes, which break down carbohydrates, proteins, and fats in food entering the duodenum from the stomach. Inflammation of the pancreas is known as pancreatitis, with common causes including chronic alcohol use and gallstones. Becaus ...
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Proglucagon
Proglucagon is a protein that is cleaved from preproglucagon. Preproglucagon in humans is encoded by the ''GCG'' gene. Proglucagon is a precursor of glucagon, and several other components. It is generated in the alpha cells of the pancreas and in the intestinal L cells in the distal ileum and colon. It is also cleaved into the following components in different organs: * Signal peptide (1-20) – removed from preproglucagon to form proglucagon * Glicentin (21–89) * Glicentin-related pancreatic polypeptide (GRPP, 21-50) * Oxyntomodulin (OXY or OXM, 53–89) * Glucagon (53–81) * Glucagon-like peptide 1 (GLP-1, 92–128) – first seven residues further cleaved * Glucagon-like peptide 2 (GLP-2, 146–178) Proglucagon itself is a protein with three repeats of slightly different secretin family hormones to be cleaved to form mature hormones. References Further reading * External links

* * * * {{Proglucagon Pancreatic hormones Precursor proteins ...
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Glucagon Hormone Family
Glucagon/gastric inhibitory polypeptide/secretin/vasoactive intestinal peptide hormones are a family of evolutionarily related peptide hormones that regulate activity of G-protein-coupled receptors from the secretin receptor family. A number of polypeptidic hormones, mainly expressed in the intestine or the pancreas, belong to a group of these structurally related peptides. One such hormone, glucagon, is widely distributed and produced in the alpha-cells of pancreatic islets. It affects glucose metabolism in the liver by inhibiting glycogen synthesis, stimulating glycogenolysis and enhancing gluconeogenesis. It also increases mobilisation of glucose, free fatty acids, and ketone bodies, which are metabolites produced in excess in diabetes mellitus. Glucagon is produced, like other peptide hormones, as part of a larger precursor (preproglucagon), which is cleaved to produce glucagon, glucagon-like protein I, glucagon-like protein II, and glicentin. The structure of gluca ...
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Insulin
Insulin (, from Latin ''insula'', 'island') is a peptide hormone produced by beta cells of the pancreatic islets encoded in humans by the ''INS'' gene. It is considered to be the main anabolic hormone of the body. It regulates the metabolism of carbohydrates, fats and protein by promoting the absorption of glucose from the blood into liver, fat and skeletal muscle cells. In these tissues the absorbed glucose is converted into either glycogen via glycogenesis or fats (triglycerides) via lipogenesis, or, in the case of the liver, into both. Glucose production and secretion by the liver is strongly inhibited by high concentrations of insulin in the blood. Circulating insulin also affects the synthesis of proteins in a wide variety of tissues. It is therefore an anabolic hormone, promoting the conversion of small molecules in the blood into large molecules inside the cells. Low insulin levels in the blood have the opposite effect by promoting widespread catabolism, especially o ...
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Glucose
Glucose is a simple sugar with the molecular formula . Glucose is overall the most abundant monosaccharide, a subcategory of carbohydrates. Glucose is mainly made by plants and most algae during photosynthesis from water and carbon dioxide, using energy from sunlight, where it is used to make cellulose in cell walls, the most abundant carbohydrate in the world. In energy metabolism, glucose is the most important source of energy in all organisms. Glucose for metabolism is stored as a polymer, in plants mainly as starch and amylopectin, and in animals as glycogen. Glucose circulates in the blood of animals as blood sugar. The naturally occurring form of glucose is -glucose, while -glucose is produced synthetically in comparatively small amounts and is less biologically active. Glucose is a monosaccharide containing six carbon atoms and an aldehyde group, and is therefore an aldohexose. The glucose molecule can exist in an open-chain (acyclic) as well as ring (cyclic) form. Gluco ...
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Glycogenolysis
Glycogenolysis is the breakdown of glycogen (n) to glucose-1-phosphate and glycogen (n-1). Glycogen branches are catabolized by the sequential removal of glucose monomers via phosphorolysis, by the enzyme glycogen phosphorylase. Mechanism The overall reaction for the breakdown of glycogen to glucose-1-phosphate is: : glycogen(n residues) + Pi glycogen(n-1 residues) + glucose-1-phosphate Here, glycogen phosphorylase cleaves the bond linking a terminal glucose residue to a glycogen branch by substitution of a phosphoryl group for the α →4linkage. Glucose-1-phosphate is converted to glucose-6-phosphate (which often ends up in glycolysis) by the enzyme phosphoglucomutase. Glucose residues are phosphorolysed from branches of glycogen until four residues before a glucose that is branched with a α →6linkage. Glycogen debranching enzyme then transfers three of the remaining four glucose units to the end of another glycogen branch. This exposes the α →6branching point, which ...
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Glycogen
Glycogen is a multibranched polysaccharide of glucose that serves as a form of energy storage in animals, fungi, and bacteria. The polysaccharide structure represents the main storage form of glucose in the body. Glycogen functions as one of two forms of energy reserves, glycogen being for short-term and the other form being triglyceride stores in adipose tissue (i.e., body fat) for long-term storage. In humans, glycogen is made and stored primarily in the cells of the liver and skeletal muscle. In the liver, glycogen can make up 5–6% of the organ's fresh weight, and the liver of an adult, weighing 1.5 kg, can store roughly 100–120 grams of glycogen. In skeletal muscle, glycogen is found in a low concentration (1–2% of the muscle mass) and the skeletal muscle of an adult weighing 70 kg stores roughly 400 grams of glycogen. The amount of glycogen stored in the body—particularly within the muscles and liver—mostly depends on physical training, bas ...
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Peptide Hormone
Peptide hormones or protein hormones are hormones whose molecules are peptide, or proteins, respectively. The latter have longer amino acid chain lengths than the former. These hormones have an effect on the endocrine system of animals, including humans. Most hormones can be classified as either amino acid–based hormones (amine, peptide, or protein) or steroid hormones. The former are water-soluble and act on the surface of target cells via second messenger system, second messengers; the latter, being lipid-soluble, move through the plasma membranes of target cells (both cell membrane, cytoplasmic and nuclear membrane, nuclear) to act within their cell nucleus, nuclei. Like all peptides and proteins, peptide hormones and protein hormones are synthesized in cell (biology), cells from amino acids according to Messenger RNA, mRNA transcripts, which are synthesized from DNA templates inside the cell nucleus. Preprohormones, peptide hormone precursors, are then processed in several sta ...
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Catabolic
Catabolism () is the set of metabolic pathways that breaks down molecules into smaller units that are either oxidized to release energy or used in other anabolic reactions. Catabolism breaks down large molecules (such as polysaccharides, lipids, nucleic acids, and proteins) into smaller units (such as monosaccharides, fatty acids, nucleotides, and amino acids, respectively). Catabolism is the breaking-down aspect of metabolism, whereas anabolism is the building-up aspect. Cells use the monomers released from breaking down polymers to either construct new polymer molecules or degrade the monomers further to simple waste products, releasing energy. Cellular wastes include lactic acid, acetic acid, carbon dioxide, ammonia, and urea. The formation of these wastes is usually an oxidation process involving a release of chemical free energy, some of which is lost as heat, but the rest of which is used to drive the synthesis of adenosine triphosphate (ATP). This molecule acts as a way fo ...
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Phenylalanine
Phenylalanine (symbol Phe or F) is an essential α-amino acid with the formula . It can be viewed as a benzyl group substituted for the methyl group of alanine, or a phenyl group in place of a terminal hydrogen of alanine. This essential amino acid is classified as neutral, and nonpolar because of the inert and hydrophobic nature of the benzyl side chain. The L-isomer is used to biochemically form proteins coded for by DNA. Phenylalanine is a precursor for tyrosine, the monoamine neurotransmitters dopamine, norepinephrine (noradrenaline), and epinephrine (adrenaline), and the skin pigment melanin. It is encoded by the codons UUU and UUC. Phenylalanine is found naturally in the milk of mammals. It is used in the manufacture of food and drink products and sold as a nutritional supplement for its analgesic and antidepressant effects. It is a direct precursor to the neuromodulator phenethylamine, a commonly used dietary supplement. As an essential amino acid, phenylalanine is n ...
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