sincalide and Carcinoid-Tumor

sincalide has been researched along with Carcinoid-Tumor* in 2 studies

Other Studies

2 other study(ies) available for sincalide and Carcinoid-Tumor

Article	Year
Characterization of gastrin/CCK receptors on gastric carcinoid tumor membrane of Mastomys natalensis. Regulatory peptides, 1993, Feb-18, Volume: 43, Issue:3 Recently, we identified the specific binding site for gastrin on the gastric carcinoid tumor of Mastomys (Praomys) natalensis. In this study, precise characterization of the gastrin binding site on these tumors was performed. Both 125I-human gastrin I (gastrin) and 125I-CCK-8 bound specifically to the cell membrane, and Scatchard analysis revealed a high affinity binding site for each ligand with similar Kd and Bmax values. The specific binding of both 125I-gastrin and 125I-CCK-8 was displaced in a concentration-dependent manner by various related peptides with a relative potency order of CCK-8 > or = gastrin < des(SO3)CCK-8. In addition, L364,718 as well as L365,260 displaced the binding of both ligands with similar potencies. Furthermore, not only gastrin but also CCK-8 increased [Ca2+]i in these tumor cells, the action of both being inhibited by L364,718 as well as by L365,260 (10(-7) M). These results suggest that the carcinoid tumor of Mastomys possesses a high affinity gastrin/CCK binding site coupled to the increase of [Ca2+]i. Topics: Animals; Carcinoid Tumor; Female; Gastrins; Humans; Kinetics; Male; Muridae; Neoplasm Transplantation; Receptors, Cholecystokinin; Sincalide; Stomach Neoplasms	1993
Cloning and characterization of gastrin receptor from ECL carcinoid tumor of Mastomys natalensis. Biochemical and biophysical research communications, 1992, Sep-16, Volume: 187, Issue:2 We report here the cDNA cloning of a putative gastrin receptor from enterochromaffin-like (ECL) carcinoid tumor of Mastomys natalensis. For this study, we used the polymerase chain reaction technique to amplify transmembrane domain sequences related to rat pancreatic cholecystokinin (CCK)-A receptor from the ECL tumor cDNA library. The amino acid sequence deduced from the cloned cDNA showed 85.7% and 49.0% identity to canine parietal cell gastrin receptor and rat pancreatic CCK-A receptor, respectively. Ligand binding studies using COS-7 cells transfected with the cDNA showed the same binding specificity for gastrin and CCK-8 as the gastrin receptor on the Mastomys carcinoid tumor membrane. Both gastrin and CCK-8 elevated free cytosolic calcium concentration in COS-7 cells expressing the cloned receptor. RNA blot analysis revealed the expression of the gastrin receptor in both Mastomys stomach and brain. Topics: Amino Acid Sequence; Animals; Base Sequence; Calcium; Carcinoid Tumor; Cloning, Molecular; DNA; Dogs; Female; Gastrins; Molecular Sequence Data; Muridae; Pancreas; Parietal Cells, Gastric; Rats; Receptors, Cholecystokinin; Sequence Homology, Nucleic Acid; Sincalide; Stomach Neoplasms; Transfection	1992

Article

Year

Characterization of gastrin/CCK receptors on gastric carcinoid tumor membrane of Mastomys natalensis.

Regulatory peptides, 1993, Feb-18, Volume: 43, Issue:3

Recently, we identified the specific binding site for gastrin on the gastric carcinoid tumor of Mastomys (Praomys) natalensis. In this study, precise characterization of the gastrin binding site on these tumors was performed. Both 125I-human gastrin I (gastrin) and 125I-CCK-8 bound specifically to the cell membrane, and Scatchard analysis revealed a high affinity binding site for each ligand with similar Kd and Bmax values. The specific binding of both 125I-gastrin and 125I-CCK-8 was displaced in a concentration-dependent manner by various related peptides with a relative potency order of CCK-8 > or = gastrin < des(SO3)CCK-8. In addition, L364,718 as well as L365,260 displaced the binding of both ligands with similar potencies. Furthermore, not only gastrin but also CCK-8 increased [Ca2+]i in these tumor cells, the action of both being inhibited by L364,718 as well as by L365,260 (10(-7) M). These results suggest that the carcinoid tumor of Mastomys possesses a high affinity gastrin/CCK binding site coupled to the increase of [Ca2+]i.

Topics: Animals; Carcinoid Tumor; Female; Gastrins; Humans; Kinetics; Male; Muridae; Neoplasm Transplantation; Receptors, Cholecystokinin; Sincalide; Stomach Neoplasms

1993

Cloning and characterization of gastrin receptor from ECL carcinoid tumor of Mastomys natalensis.

Biochemical and biophysical research communications, 1992, Sep-16, Volume: 187, Issue:2

We report here the cDNA cloning of a putative gastrin receptor from enterochromaffin-like (ECL) carcinoid tumor of Mastomys natalensis. For this study, we used the polymerase chain reaction technique to amplify transmembrane domain sequences related to rat pancreatic cholecystokinin (CCK)-A receptor from the ECL tumor cDNA library. The amino acid sequence deduced from the cloned cDNA showed 85.7% and 49.0% identity to canine parietal cell gastrin receptor and rat pancreatic CCK-A receptor, respectively. Ligand binding studies using COS-7 cells transfected with the cDNA showed the same binding specificity for gastrin and CCK-8 as the gastrin receptor on the Mastomys carcinoid tumor membrane. Both gastrin and CCK-8 elevated free cytosolic calcium concentration in COS-7 cells expressing the cloned receptor. RNA blot analysis revealed the expression of the gastrin receptor in both Mastomys stomach and brain.

Topics: Amino Acid Sequence; Animals; Base Sequence; Calcium; Carcinoid Tumor; Cloning, Molecular; DNA; Dogs; Female; Gastrins; Molecular Sequence Data; Muridae; Pancreas; Parietal Cells, Gastric; Rats; Receptors, Cholecystokinin; Sequence Homology, Nucleic Acid; Sincalide; Stomach Neoplasms; Transfection

1992