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      Preptin derived from proinsulin-like growth factor II (proIGF-II) is secreted from pancreatic islet beta-cells and enhances insulin secretion.

      Biochemical Journal
      Amino Acid Sequence, Animals, Antibodies, pharmacology, Cell Line, Cell Separation, Down-Regulation, immunology, Glucose, Humans, In Vitro Techniques, Insulin, agonists, secretion, Insulin-Like Growth Factor II, isolation & purification, physiology, Islets of Langerhans, drug effects, Male, Mice, Molecular Sequence Data, Peptide Fragments, Perfusion, Protein Precursors, Rats, Rats, Wistar, Secretory Vesicles, chemistry

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          Abstract

          Pancreatic islet beta-cells secrete the hormones insulin, amylin and pancreastatin. To search for further beta-cell hormones, we purified peptides from secretory granules isolated from cultured murine beta TC6-F7 beta-cells. We identified a 34-amino-acid peptide (3948 Da), corresponding to Asp(69)-Leu(102) of the proinsulin-like growth factor II E-peptide, which we have termed 'preptin'. Preptin, is present in islet beta-cells and undergoes glucose-mediated co-secretion with insulin. Synthetic preptin increases insulin secretion from glucose-stimulated beta TC6-F7 cells in a concentration-dependent and saturable manner. Preptin infusion into the isolated, perfused rat pancreas increases the second phase of glucose-mediated insulin secretion by 30%, while anti-preptin immunoglobulin infusion decreases the first and second phases of insulin secretion by 29 and 26% respectively. These findings suggest that preptin is a physiological amplifier of glucose-mediated insulin secretion.

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