pancreatic polypeptide

Pancreatic polypeptide, a peptide produced by the pancreas's endocrine PP cells, modulates pancreatic secretory functions and influences hepatic glycogen levels and gastrointestinal secretion [1].

Pancreatic Polypeptide, rat acetate is an agonist of NPY receptor, with high affinity at NPYR4.

Pancreatic Polypeptide (human) acetate is a C-terminally amidated 36 amino acid peptide, which acts as a neuropeptide Y (NPY) Y4 Y5 receptor agonist.

Pancreatic Polypeptide, rat, is an agonist of the NPY receptor with high affinity at NPYR4. Pancreatic Polypeptide (PP) is a 36-amino acid, C-terminally amidated peptide and a member of the PP-fold peptide family. It is produced and secreted by the PP cells of the islets of Langerhans.

Endogenous high affinity agonist for human NPY Y4 receptor (Ki = 0.056 nM). Believed to play an important role in the function of the gastrointestinal tract.

Agonist at Y4 neuropeptide Y receptors.

[cPP1-7,NPY19-23,Ala31,Aib32,Gln34]-hPancreatic Polypeptide is a potent and selective neuropeptide Y Y5 receptor agonist, exhibiting a binding affinity with an IC50 of 0.24 nM for the hY5 receptor, and significantly stimulates food intake [1].

Potent, selective peptide agonist for the neuropeptide Y Y5 receptor (IC50 values for inhibition of NPY binding to human Y5, Y1, Y2 and Y4 receptors are 0.24, 530, > 500, and 51 nM respectively, Ki at Y5 = 0.1 - 0.15 nM). Stimulates food intake in vivo.

Porcine pancreatic elastase is a serine protease composed of a single polypeptide chain with 240 amino acid residues. It has the ability to hydrolyze polypeptides and proteins, and can induce emphysema in hamsters.

Gastrin-releasing peptide (GRP) is a neuropeptide that stimulates gastrin release. It binds to (Ki = 300 nM) and stimulates amylase secretion in rat pancreatic AR42J cells (EC50 = 0.3 nM). GRP increases proliferation of human liver carcinoma HepG2 and MHCC97H cells but does not affect the proliferation of normal HL-7702 liver cells at a concentration of 1 nM. In vivo, GRP (0.35 nmol/kg/h) increases both pancreatic exocrine secretion and pancreatic polypeptide (PP) release in rats. It dose-dependently stimulates gastrin, pancreatic amylase, lipase, bilirubin, and acid output and induces gallbladder contraction in humans when administered at doses ranging from 1 to 27 pmol/kg per hour.

Amylin, amide, human TFA, a 37-amino acid polypeptide, functions as a pancreatic hormone cosecreted with insulin, playing distinct roles in metabolism and glucose homeostasis by regulating blood sugar through inhibiting glucagon secretion, delaying gastric emptying, and promoting satiety [1].

Amylin (IAPP), feline TFA, a 37-amino acid polypeptide derived from felines, is a principal secretion product of the pancreatic islets' β-cells. This regulatory peptide notably inhibits the secretion of insulin and glucagon [1].

GIP, rat TFA (glucose-dependent insulinotropic polypeptide), a 42-amino acid peptide secreted by K cells in the duodenum and jejunum, promotes insulin release from pancreatic beta cells, supports beta cell proliferation, and enhances their survival. This rat-origin bioactive peptide, along with GLP (gastric-like peptide), belongs to the intestinal insulinotropic hormone family and is implicated in lipid homeostasis and potentially in the pathogenesis of obesity. Recent research suggests GIP's multifaceted role in these metabolic processes.

GIP (rat) (Glucose-dependent Insulinotropic Polypeptide), also known as Gastric Inhibitory Polypeptide, is a biologically active 42-amino acid peptide secreted by the K cells of the duodenum and jejunum following food consumption. It belongs to the incretin hormone peptide family, which includes GLP (Gastric-like Peptide), and it not only stimulates insulin release from pancreatic islet β-cells but also may encourage β-cell proliferation and survival. Additionally, recent research indicates GIP may have a role in lipid regulation and could contribute to the development of obesity.