Caffeine Inhibits Ca2+-Mediated Potentiation of Inositol 1,4,5-Trisphosphate-Induced Ca2+ Release in Permeabilized Vascular Smooth Muscle Cells

Hirose, Kinjiro; Iino, Masae; Endo, Mitsufumi

doi:10.1006/bbrc.1993.1882

Cited by 45 publications

(20 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Single channel data analysis (Figure 2) revealed that caffeine affects mainly the frequency of openings (the opening rate constant, 13), leav- . This reasoning provides us with a qualitative explanation to the ability of increased levels of InsP3 to recover, at least partially, channel activity (this report) or restore InsP3-induced Ca release (Parker and Ivorra, 1991;Brown et al, 1992;Hirose et al, 1993) in the presence of caffeine. A more complicated model that takes into consideration the tetrameric structure of the InsP3 receptor complex (Supattapone et al, 1988;Chadwick et al, 1990), with an InsP3 binding site on each subunit, must be used for quantitative calculations.…”

Section: Discussionmentioning

confidence: 73%

“…Despite the ability of increased levels of InsP3 to overcome the inhibitory action of caffeine (this report; Parker and Ivorra, 1991;Brown et al, 1992;Hirose et al, 1993), caffeine is not a competitive inhibitor of the InsP3 receptor. In accord with data of Brown and colleagues (Brown et al, 1992), we found that caffeine had no substantial effect on InsP3 binding to the receptor (Figure 3).…”

Section: Discussionmentioning

confidence: 90%

“…Recently, Parker and Ivorra demonstrated an inhibitory action of caffeine on InsP3-induced Ca release in Xenopus oocytes (Parker and Ivorra, 1991) that was unlikely to be associated with activation of CICR because the ryanodine receptor is lacking in Xenopus oocytes (Parys et al, 1992). An inhibitory action of caffeine on InsP3-induced Ca release from cerebellar microsomes and permeabilized vascular smooth muscle has also been demonstrated (Brown et al, 1992;Hirose et al, 1993), suggesting a direct effect of caffeine on InsP3-gated Ca channels. However, the exact mechanism of the caffeine action on the InsP3 receptor remained to be elucidated.…”

Section: Introductionmentioning

confidence: 92%

See 2 more Smart Citations

Caffeine-induced inhibition of inositol(1,4,5)-trisphosphate-gated calcium channels from cerebellum.

Bezprozvanny

Bezprozvannaya

Ehrlich

1994

MBoC

View full text Add to dashboard Cite

Effects of the xanthine drug caffeine on inositol (1,4,5)-trisphosphate (InsP3)-gated calcium (Ca) channels from canine cerebellum were studied using single channels incorporated into planar lipid bilayers. Caffeine, used widely as an agonist of ryanodine receptors, inhibited the activity of InsP3-gated Ca channels in a noncooperative fashion with halfinhibition at 1.64 mM caffeine. The frequency of channel openings was decreased more than threefold after addition of 5 mM caffeine; there was only a small effect on mean open time of the channels, and the single channel conductance was unchanged. Increased InsP3 concentration overcame the inhibitory action of caffeine, but caffeine did not reduce specific [3H]InsP3 binding to the receptor. The inhibitory action of caffeine on InsP3 receptors suggests that the action of caffeine on the intracellular Ca pool must be interpreted with caution when both ryanodine receptors and InsP3 receptors are present in the cell.

show abstract

Section: Discussionmentioning

confidence: 73%

Section: Discussionmentioning

confidence: 90%

Section: Introductionmentioning

confidence: 92%

See 1 more Smart Citation

Caffeine-induced inhibition of inositol(1,4,5)-trisphosphate-gated calcium channels from cerebellum.

Bezprozvanny

Bezprozvannaya

Ehrlich

1994

MBoC

View full text Add to dashboard Cite

show abstract

“…4A) and presence of 10 mM caffeine (Fig. 4B), an inhibitor of the IP 3 receptor (35)(36)(37)(38). Inhibition of the IP 3 receptor therefore had no effect on capacitative Ca 2ϩ entry in COS-1 cells.…”

Section: Effect Of Overexpressing Pmr1 On Capacitative Camentioning

confidence: 87%

Baseline Cytosolic Ca2+ Oscillations Derived from a Non-endoplasmic Reticulum Ca2+Store

Missiaen¹,

Acker²,

Parys³

et al. 2001

Journal of Biological Chemistry

View full text Add to dashboard Cite

) is an intracellular second messenger used by many cells to release Ca 2ϩ from their internal stores (6). IP 3 acts on the IP 3 receptor, which is an important Ca 2ϩ release channel in the endoplasmic reticulum (7). There is, however, increasing evidence that IP 3 receptors are also localized in the Golgi apparatus (8 -12). The role of this latter organelle in the generation of cytosolic Ca 2ϩ signals is not well known, partly because the mechanism by which the Golgi complex takes up Ca 2ϩ is less well understood compared with the Ca 2ϩ transport into the endoplasmic reticulum mediated by the sarco(endo)plasmic reticulum Ca 2ϩ -ATPase (SERCA). The Golgi apparatus expresses a specific Ca 2ϩ pump belonging to the Pmr1 family of Ca 2ϩ -transport ATPases (13). Pmr1 is insensitive to the inhibitor thapsigargin (14), in contrast to the SERCA Ca 2ϩ pumps in the sarco-and endoplasmic reticulum (15).We expressed the Pmr1 Ca 2ϩ pump of Caenorhabditis elegans (12) in COS-1 cells and pretreated the cells with thapsigargin to prevent SERCA-mediated Ca 2ϩ uptake in the endoplasmic reticulum. We demonstrate that a Ca 2ϩ store filled by the Pmr1 Ca 2ϩ pump and probably belonging to the Golgi compartment can set up baseline Ca 2ϩ spiking. EXPERIMENTAL PROCEDURESCell Culture and Transfection-COS-1 cells and HeLa cells were cultured as described previously (12, 16). The culture medium was replaced every 2 to 3 days. The cells were plated at a density of 2500 cells/cm 2 in Coverglass Chambers (Nunc Inc., Naperville, IL) or at a density of 10,000 cells/cm 2 in 12-well clusters (Costar, MA). Four days after plating, COS-1 cells were transiently transfected with Pmr1 from C. elegans or with the rabbit SERCA1a in pMT2 vector and investigated 3 days later (12). The full-length rabbit SERCA1a clone was kindly provided by Drs. J. P. Andersen and B. Vilsen (Department of Physiology, University of Aarhus, Denmark). Some cells were transfected with pig SERCA2a or SERCA2b in pSV57 (17).Immunofluorescence-Immunofluorescence microscopy was done as described previously (12). The primary antiserum Celpmrloop against Pmr1 was raised against a recombinant protein corresponding to the putative large cytoplasmic loop between transmembrane segments 4 and 5 of Pmr1 from C. elegans (12). The primary antiserum 809-27 against rabbit SERCA1 was kindly provided by Dr. J. Møller (Department of Biophysics, University of Aarhus, Denmark) (18). The antiserum against SERCA2a was described previously (19). The antibody against the 58K protein of the Golgi apparatus (clone 58K-9) was purchased from Abcams (Cambridge, UK).45 Ca 2ϩ Uptake-Fluxes were performed on saponin-permeabilized cells at 25°C as described previously (20). The cells were permeabilized by treating them for 10 min with 20 g/ml saponin at 25°C in a medium containing 120 mM KCl, 30 mM imidazole-HCl (pH 6.8), 2 mM MgCl 2 , 1 mM ATP and 1 mM EGTA. The non-mitochondrial Ca 2ϩ stores were loaded for 45 min in loading medium containing 120 mM KCl, 30 mM imidazole-HCl (pH 6.8), 5 mM MgCl 2 , 5 mM ATP, ...

show abstract

“…Next, we tested the effect of caffeine, which inhibits IP 3 -induced Ca 2+ release in different cell types (25,26). Caffeine-treated parasites and untreated controls were seeded onto HeLa cells and incubated as described above.…”

Section: Metacyclic Trypomastigote Ca 2+ Required For Host Cell Invasmentioning

confidence: 99%

Signal transduction induced in Trypanosoma cruzi metacyclic trypomastigotes during the invasion of mammalian cells

Yoshida

Favoreto

Ferreira

et al. 2000

Braz J Med Biol Res

View full text Add to dashboard Cite

Penetration of Trypanosoma cruzi into mammalian cells depends on the activation of the parasites protein tyrosine kinase and on the increase in cytosolic Ca 2+ concentration. We used metacyclic trypomastigotes, the T. cruzi developmental forms that initiate infection in mammalian hosts, to investigate the association of these two events and to identify the various components of the parasite signal transduction pathway involved in host cell invasion. We have found that i) both the protein tyrosine kinase activation, as measured by phosphorylation of a 175-kDa protein (p175), and Ca 2+ mobilization were induced in the metacyclic forms by the HeLa cell extract but not by the extract of T. cruzi-resistant K562 cells; ii) treatment of parasites with the tyrosine kinase inhibitor genistein blocked both p175 phosphorylation and the increase in cytosolic Ca 2+ concentration; iii) the recombinant protein J18, which contains the full-length sequence of gp82, a metacyclic stage surface glycoprotein involved in target cell invasion, interfered with tyrosine kinase and Ca 2+ responses, whereas the monoclonal antibody 3F6 directed at gp82 induced parasite p175 phosphorylation and Ca 2+ mobilization; iv) treatment of metacyclic forms with phospholipase C inhibitor U73122 blocked Ca 2+ signaling and impaired the ability of the parasites to enter HeLa cells, and v) drugs such as heparin, a competitive IP 3 -receptor blocker, caffeine, which affects Ca 2+ release from IP 3 -sensitive stores, in addition to thapsigargin, which depletes intracellular Ca 2+ compartments and lithium ion, reduced the parasite infectivity. Taken together, these data suggest that protein tyrosine kinase, phospholipase C and IP 3 are involved in the signaling cascade that is initiated on the parasite cell surface by gp82 and leads to Ca 2+ mobilization required for target cell invasion.

show abstract

Caffeine Inhibits Ca2+-Mediated Potentiation of Inositol 1,4,5-Trisphosphate-Induced Ca2+ Release in Permeabilized Vascular Smooth Muscle Cells

Cited by 45 publications

References 0 publications

Caffeine-induced inhibition of inositol(1,4,5)-trisphosphate-gated calcium channels from cerebellum.

Caffeine-induced inhibition of inositol(1,4,5)-trisphosphate-gated calcium channels from cerebellum.

Baseline Cytosolic Ca2+ Oscillations Derived from a Non-endoplasmic Reticulum Ca2+Store

Signal transduction induced in Trypanosoma cruzi metacyclic trypomastigotes during the invasion of mammalian cells

Contact Info

Product

Resources

About