About Preptin, human

Preptin acquired from proinsulin-like advance agency II (proIGF-II) is buried from pancreatic islet beta-cells and enhances insulin secretion.

Pancreatic islet beta-cells bury the hormones insulin, amylin and pancreastatin. To seek for added beta-cell hormones, we antiseptic peptides from secretory granules abandoned from able murine beta TC6-F7 beta-cells. We articular a 34-amino-acid peptide (3948 Da), agnate to Asp(69)-Leu(102) of the proinsulin-like advance agency II E-peptide, which we accept termed 'preptin'. Preptin, is present in islet beta-cells and undergoes glucose-mediated co-secretion with insulin. Synthetic preptin increases insulin beard from glucose-stimulated beta TC6-F7 beef in a concentration-dependent and saturable manner. Preptin beverage into the isolated, perfused rat pancreas increases the additional appearance of glucose-mediated insulin beard by 30%, while anti-preptin immunoglobulin beverage decreases the aboriginal and additional phases of insulin beard by 29 and 26% respectively. These allegation advance that preptin is a physiological amplifier of glucose-mediated insulin secretion.

Preptin, accession peptide artefact of the pancreatic beta-cell, is osteogenic in vitro and in vivo.

Several hormones that adapt comestible cachet aswell appulse on cartilage metabolism. Preptin is a afresh abandoned 34-amino acerbic peptide hormone that is cosecreted with insulin and amylin from the pancreatic beta-cells. Preptin corresponds to Asp(69)-Leu(102) of pro-IGF-II. Added circulating levels of a pro-IGF-II peptide complexed with IGF-binding protein-2 accept been active in the top cartilage accumulation phenotype empiric in patients with abiding hepatitis C infection. We accept adjourned preptin's activities on bone. Preptin dose-dependently angry the admeasurement (cell amount and DNA synthesis) of primary fetal rat osteoblasts and osteoblast-like corpuscle curve at periphysiological concentrations (>10(-11) M). In addition, thymidine assimilation was angry in murine neonatal calvarial agency culture, acceptable absorption the admeasurement of beef from the osteoblast lineage. Preptin did not affect cartilage absorption in this model. Preptin induced phosphorylation of p42/p44 MAP kinases in osteoblastic beef in a dose-dependent address (10(-8)-10(-10) M), and its proliferative furnishings on primary osteoblasts were blocked by MAP kinase kinase inhibitors. Preptin aswell bargain osteoblast apoptosis induced by serum deprivation, abbreviation the amount of apoptotic beef by >20%. In vivo administering of preptin added cartilage breadth and mineralizing apparent in developed mice. These abstracts authenticate that preptin, which is cosecreted from the pancreatic beta-cell with amylin and insulin, is anabolic to cartilage and may accord to the canning of cartilage accumulation empiric in hyperinsulinemic states such as obesity.


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