Id |
Subject |
Object |
Predicate |
Lexical cue |
T1 |
0-150 |
Sentence |
denotes |
Pituitary adenylate cyclase activating polypeptide is an extraordinarily potent intra-pancreatic regulator of insulin secretion from islet beta-cells. |
T2 |
151-242 |
Sentence |
denotes |
Insulin secretion from pancreatic islets is controlled by peptides as well as by nutrients. |
T3 |
243-334 |
Sentence |
denotes |
We report here a novel, extraordinarily potent peptidergic regulation of insulin secretion. |
T4 |
335-521 |
Sentence |
denotes |
A 27-residue form of pituitary adenylate cyclase activating polypeptide (PACAP27) as low as 10(-14) to 10(-13) M stimulated insulin release from rat islets in a glucose-dependent manner. |
T5 |
522-609 |
Sentence |
denotes |
PACAP27 also increased cytosolic free Ca2+ concentration ([Ca2+]i) in islet beta-cells. |
T6 |
610-707 |
Sentence |
denotes |
Nitrendipine, a blocker of the L-type Ca2+ channel, abolished both [Ca2+]i and insulin responses. |
T7 |
708-930 |
Sentence |
denotes |
Vasoactive intestinal peptide, a peptide exhibiting 68% amino acid homology with PACAP, also increased [Ca2+]i in beta-cells but only at concentrations in the nanomolar range, indicating that PACAP27 is 4 logs more potent. |
T8 |
931-1072 |
Sentence |
denotes |
A 38-residue form of the peptide (PACAP38) stimulated insulin release and increased beta-cell [Ca2+]i in a manner similar to that of PACAP27. |
T9 |
1073-1170 |
Sentence |
denotes |
PACAP-like immunoreactivity was demonstrated in pancreatic nerve fibers, islets, and capillaries. |
T10 |
1171-1490 |
Sentence |
denotes |
The results indicate that PACAP is a physiologically occurring peptide in pancreas and that PACAP, in a glucose-dependent manner, activates beta-cells presumably via a high affinity PACAP-selective receptor, raises [Ca2+]i by increasing the activity of L-type Ca2+ channels, and consequently stimulates insulin release. |
T11 |
1491-1563 |
Sentence |
denotes |
PACAP appears to be by far the most potent insulinotropic peptide known. |
T1 |
0-150 |
Sentence |
denotes |
Pituitary adenylate cyclase activating polypeptide is an extraordinarily potent intra-pancreatic regulator of insulin secretion from islet beta-cells. |
T2 |
151-242 |
Sentence |
denotes |
Insulin secretion from pancreatic islets is controlled by peptides as well as by nutrients. |
T3 |
243-334 |
Sentence |
denotes |
We report here a novel, extraordinarily potent peptidergic regulation of insulin secretion. |
T4 |
335-521 |
Sentence |
denotes |
A 27-residue form of pituitary adenylate cyclase activating polypeptide (PACAP27) as low as 10(-14) to 10(-13) M stimulated insulin release from rat islets in a glucose-dependent manner. |
T5 |
522-609 |
Sentence |
denotes |
PACAP27 also increased cytosolic free Ca2+ concentration ([Ca2+]i) in islet beta-cells. |
T6 |
610-707 |
Sentence |
denotes |
Nitrendipine, a blocker of the L-type Ca2+ channel, abolished both [Ca2+]i and insulin responses. |
T7 |
708-930 |
Sentence |
denotes |
Vasoactive intestinal peptide, a peptide exhibiting 68% amino acid homology with PACAP, also increased [Ca2+]i in beta-cells but only at concentrations in the nanomolar range, indicating that PACAP27 is 4 logs more potent. |
T8 |
931-1072 |
Sentence |
denotes |
A 38-residue form of the peptide (PACAP38) stimulated insulin release and increased beta-cell [Ca2+]i in a manner similar to that of PACAP27. |
T9 |
1073-1170 |
Sentence |
denotes |
PACAP-like immunoreactivity was demonstrated in pancreatic nerve fibers, islets, and capillaries. |
T10 |
1171-1490 |
Sentence |
denotes |
The results indicate that PACAP is a physiologically occurring peptide in pancreas and that PACAP, in a glucose-dependent manner, activates beta-cells presumably via a high affinity PACAP-selective receptor, raises [Ca2+]i by increasing the activity of L-type Ca2+ channels, and consequently stimulates insulin release. |
T11 |
1491-1563 |
Sentence |
denotes |
PACAP appears to be by far the most potent insulinotropic peptide known. |