peptide-phi and Insulinoma

peptide-phi has been researched along with Insulinoma* in 2 studies

Other Studies

2 other study(ies) available for peptide-phi and Insulinoma

Article	Year
Binding sites for peptide-histidine-isoleucine (PHI) on rat insulinoma-derived RINm5F cells. Molecular and cellular endocrinology, 1988, Volume: 60, Issue:2-3 Specific binding sites for 125I-labelled rat peptide-histidine-isoleucine (PHI) were identified on rat insulinoma-derived RINm5F cells. The concentrations of peptides producing half-maximal displacement of label were rat PHI, 0.36 +/- 0.14 nM, vasoactive intestinal polypeptide (VIP), 0.38 +/- 0.13 nM and secretin, approximately 0.2 microM. Glucagon and glucagon-like peptide-1(7-36)amide were without effect on binding. PHI and VIP produced dose-dependent increases in cAMP production in the cells that were significantly (P less than 0.05) above unstimulated rates for ligand concentrations between 10(-8) and 10(-6) M. Both PHI and VIP produced a small but significant (P less than 0.05) enhancement in the rate of release of immunoreactive insulin from the cells but the effect was not dose dependent. Topics: Adenoma, Islet Cell; Adenylyl Cyclases; Animals; Cyclic AMP; Enzyme Activation; Insulin; Insulin Secretion; Insulinoma; Iodine Radioisotopes; Pancreatic Neoplasms; Peptide PHI; Rats; Receptors, Cell Surface; Receptors, Peptide; Tumor Cells, Cultured; Vasoactive Intestinal Peptide	1988
Structure of the human vasoactive intestinal polypeptide gene. DNA (Mary Ann Liebert, Inc.), 1985, Volume: 4, Issue:4 Vasoactive intestinal polypeptide (VIP) is a 28-amino-acid hormone produced primarily by neural tissues. The amino acid sequence of VIP is similar to that of a number of gastrointestinal hormones, including glucagon and secretin. VIP is synthesized as part of a polyprotein, pre-proVIP, which generates, in addition to VIP, an additional bioactive peptide known as PHM. As a first step toward understanding the molecular basis of pre-proVIP gene expression, we have isolated the pre-proVIP gene and have determined its structure. The gene is approximately 9 kb long and is interrupted by six introns which appear to divide the gene into functional domains. One of the introns occurs within the 3'-untranslated region of the gene. Topics: Amino Acid Sequence; Base Sequence; DNA; Gene Expression Regulation; Genes; Humans; Insulinoma; Islets of Langerhans; Peptide PHI; Peptides; Protein Precursors; Transcription, Genetic; Vasoactive Intestinal Peptide	1985

Article

Year

Binding sites for peptide-histidine-isoleucine (PHI) on rat insulinoma-derived RINm5F cells.

Molecular and cellular endocrinology, 1988, Volume: 60, Issue:2-3

Specific binding sites for 125I-labelled rat peptide-histidine-isoleucine (PHI) were identified on rat insulinoma-derived RINm5F cells. The concentrations of peptides producing half-maximal displacement of label were rat PHI, 0.36 +/- 0.14 nM, vasoactive intestinal polypeptide (VIP), 0.38 +/- 0.13 nM and secretin, approximately 0.2 microM. Glucagon and glucagon-like peptide-1(7-36)amide were without effect on binding. PHI and VIP produced dose-dependent increases in cAMP production in the cells that were significantly (P less than 0.05) above unstimulated rates for ligand concentrations between 10(-8) and 10(-6) M. Both PHI and VIP produced a small but significant (P less than 0.05) enhancement in the rate of release of immunoreactive insulin from the cells but the effect was not dose dependent.

Topics: Adenoma, Islet Cell; Adenylyl Cyclases; Animals; Cyclic AMP; Enzyme Activation; Insulin; Insulin Secretion; Insulinoma; Iodine Radioisotopes; Pancreatic Neoplasms; Peptide PHI; Rats; Receptors, Cell Surface; Receptors, Peptide; Tumor Cells, Cultured; Vasoactive Intestinal Peptide

1988

Structure of the human vasoactive intestinal polypeptide gene.

DNA (Mary Ann Liebert, Inc.), 1985, Volume: 4, Issue:4

Vasoactive intestinal polypeptide (VIP) is a 28-amino-acid hormone produced primarily by neural tissues. The amino acid sequence of VIP is similar to that of a number of gastrointestinal hormones, including glucagon and secretin. VIP is synthesized as part of a polyprotein, pre-proVIP, which generates, in addition to VIP, an additional bioactive peptide known as PHM. As a first step toward understanding the molecular basis of pre-proVIP gene expression, we have isolated the pre-proVIP gene and have determined its structure. The gene is approximately 9 kb long and is interrupted by six introns which appear to divide the gene into functional domains. One of the introns occurs within the 3'-untranslated region of the gene.

Topics: Amino Acid Sequence; Base Sequence; DNA; Gene Expression Regulation; Genes; Humans; Insulinoma; Islets of Langerhans; Peptide PHI; Peptides; Protein Precursors; Transcription, Genetic; Vasoactive Intestinal Peptide

1985