Role of Ca2+ in proteolysis-inducing factor (PIF)-induced atrophy of skeletal muscle.
Identifieur interne : 000980 ( Ncbi/Checkpoint ); précédent : 000979; suivant : 000981Role of Ca2+ in proteolysis-inducing factor (PIF)-induced atrophy of skeletal muscle.
Auteurs : K A Mirza [Royaume-Uni] ; M J TisdaleSource :
- Cellular signalling [ 1873-3913 ] ; 2012.
Descripteurs français
- KwdFr :
- Angiotensine-II (pharmacologie), Animaux, Atrophie (métabolisme), Calcium (métabolisme), Chélateurs (pharmacologie), Composés du bore (pharmacologie), Facteur de nécrose tumorale alpha (pharmacologie), Lignée cellulaire, Lipopolysaccharides (pharmacologie), Muscles squelettiques (), Muscles squelettiques (anatomopathologie), Muscles squelettiques (métabolisme), Oestrènes (pharmacologie), Protéoglycanes (pharmacologie), Pyrrolidones (pharmacologie), Récepteurs à l'inositol 1,4,5-triphosphate (antagonistes et inhibiteurs), Récepteurs à l'inositol 1,4,5-triphosphate (métabolisme), Souris, Transduction du signal (), Type C Phospholipases (antagonistes et inhibiteurs), Type C Phospholipases (métabolisme), Zinc (métabolisme).
- MESH :
- anatomopathologie : Muscles squelettiques.
- antagonistes et inhibiteurs : Récepteurs à l'inositol 1,4,5-triphosphate, Type C Phospholipases.
- métabolisme : Atrophie, Calcium, Muscles squelettiques, Récepteurs à l'inositol 1,4,5-triphosphate, Type C Phospholipases, Zinc.
- pharmacologie : Angiotensine-II, Chélateurs, Composés du bore, Facteur de nécrose tumorale alpha, Lipopolysaccharides, Oestrènes, Protéoglycanes, Pyrrolidones.
- Animaux, Lignée cellulaire, Muscles squelettiques, Souris, Transduction du signal.
English descriptors
- KwdEn :
- Angiotensin II (pharmacology), Animals, Atrophy (metabolism), Boron Compounds (pharmacology), Calcium (metabolism), Cell Line, Chelating Agents (pharmacology), Estrenes (pharmacology), Inositol 1,4,5-Trisphosphate Receptors (antagonists & inhibitors), Inositol 1,4,5-Trisphosphate Receptors (metabolism), Lipopolysaccharides (pharmacology), Mice, Muscle, Skeletal (drug effects), Muscle, Skeletal (metabolism), Muscle, Skeletal (pathology), Proteoglycans (pharmacology), Pyrrolidinones (pharmacology), Signal Transduction (drug effects), Tumor Necrosis Factor-alpha (pharmacology), Type C Phospholipases (antagonists & inhibitors), Type C Phospholipases (metabolism), Zinc (metabolism).
- MESH :
- chemical , antagonists & inhibitors : Inositol 1,4,5-Trisphosphate Receptors, Type C Phospholipases.
- chemical , metabolism : Calcium, Inositol 1,4,5-Trisphosphate Receptors, Type C Phospholipases, Zinc.
- chemical , pharmacology : Angiotensin II, Boron Compounds, Chelating Agents, Estrenes, Lipopolysaccharides, Proteoglycans, Pyrrolidinones, Tumor Necrosis Factor-alpha.
- drug effects : Muscle, Skeletal, Signal Transduction.
- metabolism : Atrophy, Muscle, Skeletal.
- pathology : Muscle, Skeletal.
- Animals, Cell Line, Mice.
Abstract
Proteolysis-inducing factor (PIF) induces muscle loss in cancer cachexia through a high affinity membrane bound receptor. This study investigates the mechanism by which the PIF receptor communicates to intracellular signalling pathways. C(2)C(12) murine myoblasts were used as a model using PIF purified from MAC16 tumours. Calcium imaging was determined using fura-4-acetoxymethyl ester (Fura-4-AM). PIF induced a rapid rise in Ca(2+)(i), which was completely attenuated by a anti-receptor antibody, or peptides representing 20 mers of the N-terminus of the PIF receptor. Other agents catabolic for skeletal muscle including angiotensin II (AngII) tumour necrosis factor-α (TNF-α) and lipopolysaccharide (LPS) also induced a rise in Ca(2+)(i), but this was not attenuated by anti-PIF-receptor antibody. The rise in Ca(2+)(i) induced by PIF and AngII was completely attenuated by the Zn(2+) chelator D-myo-inositol-1,2,6-triphosphate, and this was reversed by administration of exogenous Zn(2+). The Ca(2+)(i) rise induced by PIF was independent of the presence of extracellular Ca(2+), and attenuated by the Ca(2+) pump inhibitor thapsigargin, suggesting that the Ca(2+)(i) rise was due to release from intracellular stores. This rise in Ca(2+)(i) induced by PIF was attenuated by both the phospholipase C inhibitor U73122 and 2-APB, an inhibitor of the inositol 1,4,5-triphosphate receptor, suggesting the involvement of a G-protein. Binding of the PIF to its receptor in skeletal muscle triggers a rise in Ca(2+)(i), which initiates a signalling cascade leading to a depression in protein synthesis, and an increase in protein degradation.
DOI: 10.1016/j.cellsig.2012.07.016
PubMed: 22820507
Affiliations:
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xml:lang="fr"><term>Angiotensine-II (pharmacologie)</term><term>Animaux</term><term>Atrophie (métabolisme)</term><term>Calcium (métabolisme)</term><term>Chélateurs (pharmacologie)</term><term>Composés du bore (pharmacologie)</term><term>Facteur de nécrose tumorale alpha (pharmacologie)</term><term>Lignée cellulaire</term><term>Lipopolysaccharides (pharmacologie)</term><term>Muscles squelettiques ()</term><term>Muscles squelettiques (anatomopathologie)</term><term>Muscles squelettiques (métabolisme)</term><term>Oestrènes (pharmacologie)</term><term>Protéoglycanes (pharmacologie)</term><term>Pyrrolidones (pharmacologie)</term><term>Récepteurs à l'inositol 1,4,5-triphosphate (antagonistes et inhibiteurs)</term><term>Récepteurs à l'inositol 1,4,5-triphosphate (métabolisme)</term><term>Souris</term><term>Transduction du signal ()</term><term>Type C Phospholipases (antagonistes et inhibiteurs)</term><term>Type C Phospholipases (métabolisme)</term><term>Zinc 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scheme="MESH" xml:lang="en"><term>Animals</term><term>Cell Line</term><term>Mice</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Lignée cellulaire</term><term>Muscles squelettiques</term><term>Souris</term><term>Transduction du signal</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Proteolysis-inducing factor (PIF) induces muscle loss in cancer cachexia through a high affinity membrane bound receptor. This study investigates the mechanism by which the PIF receptor communicates to intracellular signalling pathways. C(2)C(12) murine myoblasts were used as a model using PIF purified from MAC16 tumours. Calcium imaging was determined using fura-4-acetoxymethyl ester (Fura-4-AM). PIF induced a rapid rise in Ca(2+)(i), which was completely attenuated by a anti-receptor antibody, or peptides representing 20 mers of the N-terminus of the PIF receptor. Other agents catabolic for skeletal muscle including angiotensin II (AngII) tumour necrosis factor-α (TNF-α) and lipopolysaccharide (LPS) also induced a rise in Ca(2+)(i), but this was not attenuated by anti-PIF-receptor antibody. The rise in Ca(2+)(i) induced by PIF and AngII was completely attenuated by the Zn(2+) chelator D-myo-inositol-1,2,6-triphosphate, and this was reversed by administration of exogenous Zn(2+). The Ca(2+)(i) rise induced by PIF was independent of the presence of extracellular Ca(2+), and attenuated by the Ca(2+) pump inhibitor thapsigargin, suggesting that the Ca(2+)(i) rise was due to release from intracellular stores. This rise in Ca(2+)(i) induced by PIF was attenuated by both the phospholipase C inhibitor U73122 and 2-APB, an inhibitor of the inositol 1,4,5-triphosphate receptor, suggesting the involvement of a G-protein. Binding of the PIF to its receptor in skeletal muscle triggers a rise in Ca(2+)(i), which initiates a signalling cascade leading to a depression in protein synthesis, and an increase in protein degradation.</div></front></TEI><affiliations><list><country><li>Royaume-Uni</li></country><region><li>Angleterre</li><li>Midlands de l'Ouest</li></region><settlement><li>Birmingham</li></settlement></list><tree><noCountry><name sortKey="Tisdale, M J" sort="Tisdale, M J" uniqKey="Tisdale M" first="M J" last="Tisdale">M J Tisdale</name></noCountry><country name="Royaume-Uni"><region name="Angleterre"><name sortKey="Mirza, K A" sort="Mirza, K A" uniqKey="Mirza K" first="K A" last="Mirza">K A Mirza</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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