Receptor-independent sequestration of beta-adrenergic ligands by alveolar type II cells.
Identifieur interne : 000464 ( Ncbi/Curation ); précédent : 000463; suivant : 000465Receptor-independent sequestration of beta-adrenergic ligands by alveolar type II cells.
Auteurs : J P Fabisiak ; S R Rannels ; E S Vesell ; D E RannelsSource :
- The American journal of physiology [ 0002-9513 ] ; 1986.
Descripteurs français
- KwdFr :
- Alvéoles pulmonaires (métabolisme), Animaux, Cellules cultivées, Chloroquine (pharmacologie), Concentration en ions d'hydrogène, Iodocyanopindolol, Lignées consanguines de rats, Membrane cellulaire (métabolisme), Mâle, Pindolol (analogues et dérivés), Pindolol (métabolisme), Poumon (), Poumon (métabolisme), Propranolol (pharmacologie), Radio-isotopes de l'iode, Rats, Récepteurs bêta-adrénergiques (physiologie).
- MESH :
- analogues et dérivés : Pindolol.
- métabolisme : Alvéoles pulmonaires, Membrane cellulaire, Pindolol, Poumon.
- pharmacologie : Chloroquine, Propranolol.
- physiologie : Récepteurs bêta-adrénergiques.
- Animaux, Cellules cultivées, Concentration en ions d'hydrogène, Iodocyanopindolol, Lignées consanguines de rats, Mâle, Poumon, Radio-isotopes de l'iode, Rats.
English descriptors
- KwdEn :
- Animals, Cell Membrane (metabolism), Cells, Cultured, Chloroquine (pharmacology), Hydrogen-Ion Concentration, Iodine Radioisotopes, Iodocyanopindolol, Lung (drug effects), Lung (metabolism), Male, Pindolol (analogs & derivatives), Pindolol (metabolism), Propranolol (pharmacology), Pulmonary Alveoli (metabolism), Rats, Rats, Inbred Strains, Receptors, Adrenergic, beta (physiology).
- MESH :
- chemical , analogs & derivatives : Pindolol.
- chemical , metabolism : Pindolol.
- chemical , pharmacology : Chloroquine, Propranolol.
- drug effects : Lung.
- metabolism : Cell Membrane, Lung, Pulmonary Alveoli.
- chemical , physiology : Receptors, Adrenergic, beta.
- Animals, Cells, Cultured, Hydrogen-Ion Concentration, Iodine Radioisotopes, Iodocyanopindolol, Male, Rats, Rats, Inbred Strains.
Abstract
Numerous studies indicate that synthesis and secretion of surfactant by type II pneumocytes are modulated by the interaction of beta-adrenergic agonists with specific cell surface receptors. Two 125I-labeled beta-adrenergic ligands, l-iodopindolol (IPIN) and l-iodocyanopindolol (ICYP), were thus employed to investigate the properties of type II cell beta-receptors. Saturable, high-affinity, stereospecific binding to crude membrane fractions from whole rat lungs was exhibited by both ligands (IPIN, KD 283 pM, Bmax 508 fmol/mg protein; ICYP, KD 18 pM, Bmax 404). Type II cell membranes obtained by N2 cavitation also revealed stereospecific, saturable, high-affinity binding. In intact cells (37 degrees C) however, rapid, highly concentrative (cell/media greater than 1000), nonspecific ligand uptake compromised estimates of specific binding (specific/total binding less than 0.1). Total ligand uptake was inhibited at 4 degrees C, by decreasing pH within the physiological range (7-8) and by the lysosomotropic compound chloroquine (50-200 microM), without a detectable change in specific binding. Other basic drugs were also inhibitory at similar concentrations; acidic drugs had no effect. Even at 4 degrees C, specific binding remained low, as IPIN and ICYP were displaced less than 30% by l-alprenolol (1 microM). Physicochemical properties of IPIN and ICYP considered with the above studies suggest that passive ligand entry into intact pneumocytes and subsequent trapping of the protonated species in a cellular compartment of low pH may account for high nonspecific ligand uptake.
DOI: 10.1152/ajpcell.1986.250.6.C871
PubMed: 3013016
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pubmed:3013016Le document en format XML
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Vesell</name></author><author><name sortKey="Rannels, D E" sort="Rannels, D E" uniqKey="Rannels D" first="D E" last="Rannels">D E Rannels</name></author></analytic><series><title level="j">The American journal of physiology</title><idno type="ISSN">0002-9513</idno><imprint><date when="1986" type="published">1986</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>Cell Membrane (metabolism)</term><term>Cells, Cultured</term><term>Chloroquine (pharmacology)</term><term>Hydrogen-Ion Concentration</term><term>Iodine Radioisotopes</term><term>Iodocyanopindolol</term><term>Lung (drug effects)</term><term>Lung (metabolism)</term><term>Male</term><term>Pindolol (analogs & derivatives)</term><term>Pindolol (metabolism)</term><term>Propranolol (pharmacology)</term><term>Pulmonary Alveoli (metabolism)</term><term>Rats</term><term>Rats, Inbred Strains</term><term>Receptors, Adrenergic, beta (physiology)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Alvéoles pulmonaires (métabolisme)</term><term>Animaux</term><term>Cellules cultivées</term><term>Chloroquine (pharmacologie)</term><term>Concentration en ions d'hydrogène</term><term>Iodocyanopindolol</term><term>Lignées consanguines de rats</term><term>Membrane cellulaire (métabolisme)</term><term>Mâle</term><term>Pindolol (analogues et dérivés)</term><term>Pindolol (métabolisme)</term><term>Poumon ()</term><term>Poumon (métabolisme)</term><term>Propranolol (pharmacologie)</term><term>Radio-isotopes de l'iode</term><term>Rats</term><term>Récepteurs bêta-adrénergiques (physiologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analogs & derivatives" xml:lang="en"><term>Pindolol</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Pindolol</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Chloroquine</term><term>Propranolol</term></keywords><keywords scheme="MESH" qualifier="analogues et dérivés" xml:lang="fr"><term>Pindolol</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Lung</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Cell Membrane</term><term>Lung</term><term>Pulmonary Alveoli</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Alvéoles pulmonaires</term><term>Membrane cellulaire</term><term>Pindolol</term><term>Poumon</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Chloroquine</term><term>Propranolol</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Récepteurs bêta-adrénergiques</term></keywords><keywords scheme="MESH" type="chemical" qualifier="physiology" xml:lang="en"><term>Receptors, Adrenergic, beta</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Cells, Cultured</term><term>Hydrogen-Ion Concentration</term><term>Iodine Radioisotopes</term><term>Iodocyanopindolol</term><term>Male</term><term>Rats</term><term>Rats, Inbred Strains</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Cellules cultivées</term><term>Concentration en ions d'hydrogène</term><term>Iodocyanopindolol</term><term>Lignées consanguines de rats</term><term>Mâle</term><term>Poumon</term><term>Radio-isotopes de l'iode</term><term>Rats</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Numerous studies indicate that synthesis and secretion of surfactant by type II pneumocytes are modulated by the interaction of beta-adrenergic agonists with specific cell surface receptors. Two 125I-labeled beta-adrenergic ligands, l-iodopindolol (IPIN) and l-iodocyanopindolol (ICYP), were thus employed to investigate the properties of type II cell beta-receptors. Saturable, high-affinity, stereospecific binding to crude membrane fractions from whole rat lungs was exhibited by both ligands (IPIN, KD 283 pM, Bmax 508 fmol/mg protein; ICYP, KD 18 pM, Bmax 404). Type II cell membranes obtained by N2 cavitation also revealed stereospecific, saturable, high-affinity binding. In intact cells (37 degrees C) however, rapid, highly concentrative (cell/media greater than 1000), nonspecific ligand uptake compromised estimates of specific binding (specific/total binding less than 0.1). Total ligand uptake was inhibited at 4 degrees C, by decreasing pH within the physiological range (7-8) and by the lysosomotropic compound chloroquine (50-200 microM), without a detectable change in specific binding. Other basic drugs were also inhibitory at similar concentrations; acidic drugs had no effect. Even at 4 degrees C, specific binding remained low, as IPIN and ICYP were displaced less than 30% by l-alprenolol (1 microM). Physicochemical properties of IPIN and ICYP considered with the above studies suggest that passive ligand entry into intact pneumocytes and subsequent trapping of the protonated species in a cellular compartment of low pH may account for high nonspecific ligand uptake.</div></front></TEI></record>Pour manipuler ce document sous Unix (Dilib)
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