Peptide PHI

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Rat Peptide histidine isoleucine (PHI) structure Rat Peptide histidine isoleucine (PHI) structure.gif
Rat Peptide histidine isoleucine (PHI) structure

Peptide PHI, also known as peptide histidine isoleucine , is a peptide which functions as a hormone. This peptide contains a composition of 27 amino acids with histidine on the N-terminus and isoleucine on the C-terminus. It was originally isolated from the mammalian small intestine amongst mammalian neurons called intramural neurons which function in the motor activity of the intestinal walls. [1] An example of this was revealed in a study that demonstrated that this peptide regulates water and electrolyte transportation in the human jejunum; similar to its inhibitory effects on fluid absorption in the small intestine of pigs and rats. [2]

Peptide histidine isoleucine (PHI) is part of family that plays a vital role in the cell growth rate such as in the intestine as well as in brain. [3] It was derived from glucagon family called the pituitary adenylate cyclase-activating polypeptide (PACAP) and it has an amino acid sequence homology to vasoactive intestinal peptide, secretin, glucagon, and other growth hormone releasing factor. [4] Human studies have shown that the release of PHI into the stomach regulates the neuroendocrine cell processes that affect gastrointestinal physiology. This peptide is present within the central nervous system that help regulate food consumption behavior, while at peripheral nervous system this peptide accumulates in the stomach which controls the digestion of food. [5]

It also plays a role in the regulation of prolactin in humans. [6] It functions specifically function in the G protein signaling pathway through G protein, which is a transmembrane protein that causes the cascade phosphorylation. It is located throughout the entire length of intestine while PHI is mostly concentrated in the colon region. [7]

Related Research Articles

Peptides are short chains of amino acids linked by peptide bonds. A polypeptide is a longer, continuous, unbranched peptide chain. Polypeptides which have a molecular mass of 10,000 Da or more are called proteins. Chains of fewer than twenty amino acids are called oligopeptides, and include dipeptides, tripeptides, and tetrapeptides.

<span class="mw-page-title-main">Secretin</span> Hormone involved in stomach, pancreas and liver secretions

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.

<span class="mw-page-title-main">Gastric acid</span> Digestive fluid formed in the stomach

Gastric acid, gastric juice, or stomach acid is a digestive fluid formed within the stomach lining. With a pH between 1 and 3, gastric acid plays a key role in digestion of proteins by activating digestive enzymes, which together break down the long chains of amino acids of proteins. Gastric acid is regulated in feedback systems to increase production when needed, such as after a meal. Other cells in the stomach produce bicarbonate, a base, to buffer the fluid, ensuring a regulated pH. These cells also produce mucus – a viscous barrier to prevent gastric acid from damaging the stomach. The pancreas further produces large amounts of bicarbonate and secretes bicarbonate through the pancreatic duct to the duodenum to neutralize gastric acid passing into the digestive tract.

<span class="mw-page-title-main">Vasoactive intestinal peptide</span> Hormone that affects blood pressure / heart rate

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, cortex, 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.

<span class="mw-page-title-main">Incretin</span> Group of gastrointestinal hormones

Incretins are a group of metabolic hormones that stimulate a decrease in blood glucose levels. Incretins are released after eating and augment the secretion of insulin released from pancreatic beta cells of the islets of Langerhans by a blood-glucose–dependent mechanism.

<span class="mw-page-title-main">Glucose-dependent insulinotropic polypeptide</span> Mammalian protein found in Homo sapiens

Glucose-dependent insulinotropic polypeptide, 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, being an incretin, is to stimulate insulin secretion.

Enteroglucagon is a peptide hormone derived from preproglucagon. It is a gastrointestinal hormone, secreted from mucosal cells primarily of the colon and terminal ileum. It consists of 37 amino acids. Enteroglucagon is released when fats and glucose are present in the small intestine; which decrease the motility to allow sufficient time for these nutrients to be absorbed.

<span class="mw-page-title-main">Peptide YY</span> Peptide released from cells in the ileum and colon in response to feeding

Peptide YY (PYY) also known as peptide tyrosine tyrosine is a peptide that in humans is encoded by the PYY gene. Peptide YY is a short peptide released from cells in the ileum and colon in response to feeding. In the blood, gut, and other elements of periphery, PYY acts to reduce appetite; similarly, when injected directly into the central nervous system, PYY is also anorexigenic, i.e., it reduces appetite.

<span class="mw-page-title-main">Galanin</span>

Galanin is a neuropeptide encoded by the GAL gene, that is widely expressed in the brain, spinal cord, and gut of humans as well as other mammals. Galanin signaling occurs through three G protein-coupled receptors.

There are two known receptors for the vasoactive intestinal peptide (VIP) termed VPAC1 and VPAC2. These receptors bind both VIP and pituitary adenylate cyclase-activating polypeptide (PACAP) to some degree. Both receptors are members of the 7 transmembrane G protein-coupled receptor family.

<span class="mw-page-title-main">Enteroendocrine cell</span>

Enteroendocrine cells are specialized cells of the gastrointestinal tract and pancreas with endocrine function. They produce gastrointestinal hormones or peptides in response to various stimuli and release them into the bloodstream for systemic effect, diffuse them as local messengers, or transmit them to the enteric nervous system to activate nervous responses. Enteroendocrine cells of the intestine are the most numerous endocrine cells of the body. They constitute an enteric endocrine system as a subset of the endocrine system just as the enteric nervous system is a subset of the nervous system. In a sense they are known to act as chemoreceptors, initiating digestive actions and detecting harmful substances and initiating protective responses. Enteroendocrine cells are located in the stomach, in the intestine and in the pancreas. Microbiota plays key roles in the intestinal immune and metabolic responses in these enteroendocrine cells via their fermentation product, acetate.

<span class="mw-page-title-main">Secretin receptor</span> Protein-coding gene in the species Homo sapiens

The secretin receptor is a protein that in humans is encoded by the SCTR gene. This protein is a G protein-coupled receptor which binds secretin and is the leading member of the secretin receptor family, also called class B GPCR subfamily.

<span class="mw-page-title-main">Gastric inhibitory polypeptide receptor</span> Protein-coding gene in the species Homo sapiens

The gastric inhibitory polypeptide receptor (GIP-R), also known as the glucose-dependent insulinotropic polypeptide receptor, is a protein that in humans is encoded by the GIPR gene.

<span class="mw-page-title-main">Glucagon-like peptide-2 receptor</span> Protein-coding gene in the species Homo sapiens

Glucagon-like peptide-2 receptor (GLP-2R) is a protein that in human is encoded by the GLP2R gene located on chromosome 17.

<span class="mw-page-title-main">VIPR2</span> Protein-coding gene in the species Homo sapiens

Vasoactive intestinal peptide receptor 2 also known as VPAC2, is a G-protein coupled receptor that in humans is encoded by the VIPR2 gene.

Secretin receptor family consists of secretin receptors regulated by peptide hormones from the glucagon hormone family. The family is different from adhesion G protein-coupled receptors.

<span class="mw-page-title-main">Secretin family</span>

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.

<span class="mw-page-title-main">Aviptadil</span> Synthetic vasoactive intestinal peptide

Aviptadil is an injectable synthetic formulation of human vasoactive intestinal peptide (VIP). VIP was discovered in 1970, and has been used to treat various inflammatory conditions, such as acute respiratory distress syndrome (ARDS), asthma, and chronic obstructive pulmonary disease (COPD).

Prolactin-releasing hormone, also known as PRLH, is a hypothetical human hormone or hormone releasing factor. Existence of this factor has been hypothesized as prolactin is the only currently known hormone for which almost exclusively negative regulating factors are known but few stimulating factor. Its secretion is mediated by estrogen from placenta during pregnancy to elevate blood level of prolactin. While many prolactin stimulating and enhancing factors are well known those have primary functions other than stimulating prolactin release and the search for hypothetical releasing factor or factors continues.


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References

  1. ↑ Curro, Diego; Preziosi, Paolo; Ragazzoni, Enzo; Ciabattoni, Giovanni (1994). "Peptide histidine isoleucine-like immunoreactivity release from the rat gastric fundus". British Journal of Pharmacology. 113 (2): 541–549. doi:10.1111/j.1476-5381.1994.tb17023.x. PMC   1510139 . PMID   7834206.
  2. ↑ Moriarty, K; Hegarty, J; Tatemoto, K; Mutt, V; Christofides, N; Bloom, S; Wood, J (June 1, 1984). "Effect of peptide histidine isoleucine on water and electrolyte transport in the human jejunum". Gut. 25 (6): 624–628. doi: 10.1136/gut.25.6.624 . PMC   1432383 . PMID   6547400.
  3. ↑ Tatemoto, Kazuhiko; Mutt, Viktor (June 1980). "Isolation of two novel candidate hormones using a chemical method for finding naturally occurring polypeptides". Nature. 285 (5764): 417–418. doi:10.1038/285417a0. ISSN   1476-4687. PMID   6892950. S2CID   4262014.
  4. ↑ Lelièvre, Vincent; Pineau, Nicolas; Du, Joanna; Wen, Chia-Hui; Nguyen, Thinh; Janet, Thierry; Muller, Jean-Marc; Waschek, James A. (1998-07-31). "Differential Effects of Peptide Histidine Isoleucine (PHI) and Related Peptides on Stimulation and Suppression of Neuroblastoma Cell Proliferation: A NOVEL VIP-INDEPENDENT ACTION OF PHI VIA MAP KINASE". Journal of Biological Chemistry. 273 (31): 19685–19690. doi: 10.1074/jbc.273.31.19685 . ISSN   0021-9258. PMID   9677397.
  5. ↑ Olszewski, Pawel; Wirth, Michelle; Shaw, Timothy; Grace, Martha; Levine, Allen (February 20, 2003). "Peptides that Regulate Food Intake Effect of peptide histidine isoleucine on consummatory behavior in rats". American Journal of Physiology. Regulatory, Integrative and Comparative Physiology. 284 (6): R1445–R1453. doi:10.1152/ajpregu.00554.2002. PMID   12595279.
  6. ↑ Kulick R, Chaiseha Y, Kang S, Rozenboim I, El Halawani M (2005). "The relative importance of vasoactive intestinal peptide and peptide histidine isoleucine as physiological regulators of prolactin in the domestic turkey". Gen Comp Endocrinol. 142 (3): 267–273. doi:10.1016/j.ygcen.2004.12.024. PMID   15935152.
  7. ↑ Yiangou, Y.; Christofides, N.D.; Blank, M.A.; Yanaihara, N.; Tatemoto, K.; Bishop, A.E.; Polak, J.M.; Bloom, S.R. (September 1985). "Molecular forms of peptide histidine isoleucine-like immunoreactivity in the gastrointestinal tract". Gastroenterology. 89 (3): 516–524. doi: 10.1016/0016-5085(85)90445-7 . ISSN   0016-5085. PMID   3839480.


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