|
SCT (gene)
Secretin is a hormone that regulates water homeostasis throughout the body and influences the environment of the duodenum by regulating secretions in the stomach, pancreas, and liver. It is a peptide hormone produced in the S cells of the duodenum, which are located in the intestinal glands. In humans, the secretin peptide is encoded by the SCT gene. Secretin helps regulate the pH of the duodenum by (1) inhibiting the secretion of gastric acid from the parietal cells of the stomach and (2) stimulating the production of bicarbonate from the ductal cells of the pancreas. It also stimulates the secretion of bicarbonate and water by cholangiocytes in the bile duct, protecting it from bile acids by controlling the pH and promoting the flow in the duct. Meanwhile, in concert with secretin's actions, the other main hormone simultaneously issued by the duodenum, cholecystokinin (CCK), is stimulating the gallbladder to contract, delivering its stored bile. Prosecretin is a precursor to ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Hormone
A hormone (from the Greek participle , "setting in motion") is a class of signaling molecules in multicellular organisms that are sent to distant organs by complex biological processes to regulate physiology and behavior. Hormones are required for the correct development of animals, plants and fungi. Due to the broad definition of a hormone (as a signaling molecule that exerts its effects far from its site of production), numerous kinds of molecules can be classified as hormones. Among the substances that can be considered hormones, are eicosanoids (e.g. prostaglandins and thromboxanes), steroids (e.g. oestrogen and brassinosteroid), amino acid derivatives (e.g. epinephrine and auxin), protein or peptides (e.g. insulin and CLE peptides), and gases (e.g. ethylene and nitric oxide). Hormones are used to communicate between organs and tissues. In vertebrates, hormones are responsible for regulating a variety of physiological processes and behavioral activities such as diges ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Osmoregulation
Osmoregulation is the active regulation of the osmotic pressure of an organism's body fluids, detected by osmoreceptors, to maintain the homeostasis of the organism's water content; that is, it maintains the fluid balance and the concentration of electrolytes (salts in solution which in this case is represented by body fluid) to keep the body fluids from becoming too diluted or concentrated. Osmotic pressure is a measure of the tendency of water to move into one solution from another by osmosis. The higher the osmotic pressure of a solution, the more water tends to move into it. Pressure must be exerted on the hypertonic side of a selectively permeable membrane to prevent diffusion of water by osmosis from the side containing pure water. Although there may be hourly and daily variations in osmotic balance, an animal is generally in an osmotic steady state over the long term. Organisms in aquatic and terrestrial environments must maintain the right concentration of solutes a ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Gastric Inhibitory Peptide
Glucose-dependent insulinotropic polypeptide (GIP), also known as Gastric inhibitory polypeptide or gastric inhibitory peptide (also abbreviated as GIP), is an inhibiting hormone of the secretin family of hormones. While it is a weak inhibitor of gastric acid secretion, its main role is to stimulate insulin secretion. GIP, along with glucagon-like peptide-1 (GLP-1), belongs to a class of molecules referred to as incretins. Synthesis and transport GIP is derived from a 153-amino acid proprotein encoded by the GIP gene and circulates as a biologically active 42-amino acid peptide. It is synthesized by K cells, which are found in the mucosa of the duodenum and the jejunum of the gastrointestinal tract. Like all endocrine hormones, it is transported by blood. Gastric inhibitory polypeptide receptors are seven-transmembrane proteins found on beta-cells in the pancreas. Functions It has traditionally been named ''gastrointestinal inhibitory peptide'' or ''gastric inhibitory pept ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Vasoactive Intestinal Peptide
Vasoactive intestinal peptide, also known as vasoactive intestinal polypeptide or VIP, is a peptide hormone that is vasoactive in the intestine. VIP is a peptide of 28 amino acid residues that belongs to a glucagon/secretin superfamily, the ligand of class II G protein–coupled receptors. VIP is produced in many tissues of vertebrates including the gut, pancreas, and suprachiasmatic nuclei of the hypothalamus in the brain. VIP stimulates contractility in the heart, causes vasodilation, increases glycogenolysis, lowers arterial blood pressure and relaxes the smooth muscle of trachea, stomach and gallbladder. In humans, the vasoactive intestinal peptide is encoded by the ''VIP'' gene. VIP has a half-life (t½) in the blood of about two minutes. Function In the body VIP has an effect on several tissues: In the digestive system, VIP seems to induce smooth muscle relaxation ( lower esophageal sphincter, stomach, gallbladder), stimulate secretion of water into pancreatic jui ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
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 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 stress. Glucagon belon ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Molecular Weight
A molecule is a group of two or more atoms held together by attractive forces known as chemical bonds; depending on context, the term may or may not include ions which satisfy this criterion. In quantum physics, organic chemistry, and biochemistry, the distinction from ions is dropped and ''molecule'' is often used when referring to polyatomic ions. A molecule may be homonuclear, that is, it consists of atoms of one chemical element, e.g. two atoms in the oxygen molecule (O2); or it may be heteronuclear, a chemical compound composed of more than one element, e.g. water (two hydrogen atoms and one oxygen atom; H2O). In the kinetic theory of gases, the term ''molecule'' is often used for any gaseous particle regardless of its composition. This relaxes the requirement that a molecule contains two or more atoms, since the noble gases are individual atoms. Atoms and complexes connected by non-covalent interactions, such as hydrogen bonds or ionic bonds, are typically not ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Amino Acids
Amino acids are organic compounds that contain both amino and carboxylic acid functional groups. Although hundreds of amino acids exist in nature, by far the most important are the alpha-amino acids, which comprise proteins. Only 22 alpha amino acids appear in the genetic code. Amino acids can be classified according to the locations of the core structural functional groups, as Alpha and beta carbon, alpha- , beta- , gamma- or delta- amino acids; other categories relate to Chemical polarity, polarity, ionization, and side chain group type (aliphatic, Open-chain compound, acyclic, aromatic, containing hydroxyl or sulfur, etc.). In the form of proteins, amino acid ''residues'' form the second-largest component ( water being the largest) of human muscles and other tissues. Beyond their role as residues in proteins, amino acids participate in a number of processes such as neurotransmitter transport and biosynthesis. It is thought that they played a key role in enabling li ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
C-terminus
The C-terminus (also known as the carboxyl-terminus, carboxy-terminus, C-terminal tail, C-terminal end, or COOH-terminus) is the end of an amino acid chain (protein or polypeptide), terminated by a free carboxyl group (-COOH). When the protein is translated from messenger RNA, it is created from N-terminus to C-terminus. The convention for writing peptide sequences is to put the C-terminal end on the right and write the sequence from N- to C-terminus. Chemistry Each amino acid has a carboxyl group and an amine group. Amino acids link to one another to form a chain by a dehydration reaction which joins the amine group of one amino acid to the carboxyl group of the next. Thus polypeptide chains have an end with an unbound carboxyl group, the C-terminus, and an end with an unbound amine group, the N-terminus. Proteins are naturally synthesized starting from the N-terminus and ending at the C-terminus. Function C-terminal retention signals While the N-terminus of a protein often co ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
N-terminus
The N-terminus (also known as the amino-terminus, NH2-terminus, N-terminal end or amine-terminus) is the start of a protein or polypeptide, referring to the free amine group (-NH2) located at the end of a polypeptide. Within a peptide, the amine group is bonded to the carboxylic group of another amino acid, making it a chain. That leaves a free carboxylic group at one end of the peptide, called the C-terminus, and a free amine group on the other end called the N-terminus. By convention, peptide sequences are written N-terminus to C-terminus, left to right (in LTR writing systems). This correlates the translation direction to the text direction, because when a protein is translated from messenger RNA, it is created from the N-terminus to the C-terminus, as amino acids are added to the carboxyl end of the protein. Chemistry Each amino acid has an amine group and a carboxylic group. Amino acids link to one another by peptide bonds which form through a dehydration reaction ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Ernest Starling
Ernest Henry Starling (17 April 1866 – 2 May 1927) was a British physiologist who contributed many fundamental ideas to this subject. These ideas were important parts of the British contribution to physiology, which at that time led the world. He made at least four significant contributions: 1. In the capillary, water is forced out through the pores in the wall by hydrostatic pressure and driven in by the osmotic pressure of plasma proteins (or oncotic pressure). These opposing forces approximately balance; which is known as Starling's Principle. 2. The discovery of the hormone secretinwith his brother-in-law William Baylissand the introduction of the word hormone. 3. The analysis of the heart's activity as a pump, which is known as the Frank–Starling law. 4. Several fundamental observations on the action of the kidneys. These include evidence for the existence of vasopressin, the anti-diuretic hormone. He also wrote the leading textbook of physiology in English, which ra ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
William Bayliss
Sir William Maddock Bayliss (2 May 1860 – 27 August 1924) was an English physiologist. Life He was born in Wednesbury, Staffordshire but shortly thereafter his father, a successful merchant of ornamental ironwork, moved his family to a house he had built on West Heath Road in Hampstead in north London, which he named St Cuthberts. It stood in four acres of gardens. William was his sole heir. He began to study medicine at University College London in 1880, but dropped out when he failed anatomy. Attracted to physiology, he studied under John Burdon Sanderson at Wadham College, Oxford, where he won a first class degree, investigating electrical changes occurring during salivary secretion. He returned to University College London in 1888 as an assistant to Edward Sharpey-Schafer. In 1890 he began to collaborate with Ernest Starling, who was at Guy's Hospital, on the electrical activity of the heart. They complemented each other in many ways: for instance, Bayliss dealt w ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
