iloprost and Thrombocythemia--Essential

iloprost has been researched along with Thrombocythemia--Essential* in 1 studies

Other Studies

1 other study(ies) available for iloprost and Thrombocythemia--Essential

Article	Year
Cloning and expression of a cDNA for the human prostacyclin receptor. FEBS letters, 1994, May-09, Volume: 344, Issue:1 A functional cDNA for the human prostacyclin receptor was isolated from a cDNA library of CMK cells, a human megakaryocytic leukaemia cell line. The cDNA encodes a protein consisting of 386 amino acid residues with seven putative transmembrane domains and a deduced molecular weight of 40,956. [3H]Iloprost specifically bound to the membrane of CHO cells stably expressing the cDNA with a Kd of 3.3 nM. This binding was displaced by unlabelled prostanoids in the order of iloprost = cicaprost >> carbacyclin > prostaglandin E1 (PGE1) > STA2. PGE2, PGD2 and PGF 2 alpha did not inhibit it. Iloprost in a concentration-dependent manner increased the cAMP level and generated inositol trisphosphate in these cells, indicating that this human receptor can couple to multiple signal transduction pathways. Topics: Amino Acid Sequence; Animals; Base Sequence; Binding, Competitive; CHO Cells; Cloning, Molecular; Cricetinae; DNA, Complementary; Gene Expression; Gene Transfer Techniques; Humans; Iloprost; Mice; Molecular Sequence Data; Receptors, Epoprostenol; Receptors, Prostaglandin; Recombinant Proteins; Thrombocythemia, Essential; Tumor Cells, Cultured	1994

Article

Year

Cloning and expression of a cDNA for the human prostacyclin receptor.

FEBS letters, 1994, May-09, Volume: 344, Issue:1

A functional cDNA for the human prostacyclin receptor was isolated from a cDNA library of CMK cells, a human megakaryocytic leukaemia cell line. The cDNA encodes a protein consisting of 386 amino acid residues with seven putative transmembrane domains and a deduced molecular weight of 40,956. [3H]Iloprost specifically bound to the membrane of CHO cells stably expressing the cDNA with a Kd of 3.3 nM. This binding was displaced by unlabelled prostanoids in the order of iloprost = cicaprost >> carbacyclin > prostaglandin E1 (PGE1) > STA2. PGE2, PGD2 and PGF 2 alpha did not inhibit it. Iloprost in a concentration-dependent manner increased the cAMP level and generated inositol trisphosphate in these cells, indicating that this human receptor can couple to multiple signal transduction pathways.

Topics: Amino Acid Sequence; Animals; Base Sequence; Binding, Competitive; CHO Cells; Cloning, Molecular; Cricetinae; DNA, Complementary; Gene Expression; Gene Transfer Techniques; Humans; Iloprost; Mice; Molecular Sequence Data; Receptors, Epoprostenol; Receptors, Prostaglandin; Recombinant Proteins; Thrombocythemia, Essential; Tumor Cells, Cultured

1994