scholarly journals Modulation of NAADP (nicotinic acid–adenine dinucleotide phosphate) receptors by K+ ions: evidence for multiple NAADP receptor conformations

2003 ◽  
Vol 375 (3) ◽  
pp. 805-812 ◽  
Author(s):  
George D. DICKINSON ◽  
Sandip PATEL
Keyword(s):  
Nicotinic Acid ◽  
Sea Urchin ◽  
Cell Types ◽  
Target Protein ◽  
Inhibitory Effects ◽  
Sea Urchin Eggs ◽  
Sea Urchin Egg ◽  
Multiple Conformations ◽  
Partial Dissociation ◽  
Low K

NAADP (nicotinic acid–adenine dinucleotide phosphate) mediates Ca2+ release from intracellular Ca2+ stores in a wide variety of cell types. In sea urchin eggs, subthreshold concentrations of NAADP can cause full inactivation of NAADP-induced Ca2+ release, an effect that may be related to the ability of the target protein to bind its ligand in an essentially irreversible manner. In the present study, we found that K+ ions inhibit dissociation of NAADP from sea urchin egg homogenates. In low K+-containing media, an addition of excess unlabelled NAADP effectively displaced bound radioligand whereas dilution of radioligand initiated only partial dissociation. The inhibitory effects of K+ on dissociation of NAADP were concentration dependent, reversible and persisted after detergent solubilization. Lowering [K+] of the medium decreased the sensitivity of NAADP receptors for their ligand in stimulating Ca2+ release, but it did not affect inactivation of NAADP-induced Ca2+ release by subthreshold concentrations of NAADP. Our results are consistent with the observation of multiple conformations of the NAADP receptor that are readily revealed in low K+-containing media.

scholarly journals Nicotinic acid-adenine dinucleotide phosphate mobilizes Ca2+ from a thapsigargin-insensitive pool

1996 ◽  
Vol 315 (3) ◽  
pp. 721-725 ◽  
Author(s):  
Armando A. GENAZZANI ◽  
Antony GALIONE
Keyword(s):  
Nicotinic Acid ◽  
Sea Urchin ◽  
Cross Talk ◽  
Inositol Trisphosphate ◽  
Sea Urchin Eggs ◽  
Bivalent Cations ◽  
Sea Urchin Egg ◽  
Different Characteristics ◽  
Degree Of Overlap

Nicotinic acid–adenine dinucleotide phosphate (NAADP) is a novel intracellular Ca2+ releasing agent recently described in sea-urchin eggs and egg homogenates. Ca2+ release by NAADP is independent of that induced by either inositol trisphosphate (InsP3) or cyclic adenosine dinucleotide phosphate (cADPR). We now report that in sea urchin egg homogenates, NAADP releases Ca2+ from a Ca2+ pool that is distinct from those that are sensitive to InsP3 and cADPR. This organelle has distinct Ca2+ uptake characteristics: it is insensitive to thapsigargin and cyclopiazoic acid, but maintenance of the pool shows some requirement for ATP. Although the different Ca2+ pools have different characteristics, there appears to be some degree of overlap or cross-talk between the NAADP- and cADPR/InsP3-sensitive Ca2+ pools. Ca2+-induced Ca2+ release is unlikely to account for the apparent overlap between stores, since NAADP-induced Ca2+ release, in contrast with that stimulated by cADPR, is not potentiated by bivalent cations.

scholarly journals Unique kinetics of nicotinic acid–adenine dinucleotide phosphate (NAADP) binding enhance the sensitivity of NAADP receptors for their ligand

2000 ◽  
Vol 352 (3) ◽  
pp. 725-729 ◽  
Author(s):  
Sandip PATEL ◽  
Grant C. CHURCHILL ◽  
Antony GALIONE
Keyword(s):  
Nicotinic Acid ◽  
Sea Urchin ◽  
Binding Sites ◽  
Cell Types ◽  
Unique Property ◽  
Single Class ◽  
High Affinity ◽  
Sea Urchin Egg ◽  
Low Concentrations ◽  
Kinetics Of

Nicotinic acidŐadenine dinucleotide phosphate (NAADP) is a novel and potent Ca2+-mobilizing agent in sea urchin eggs and other cell types. Little is known, however, concerning the properties of the putative intracellular NAADP receptor. In the present study we have characterized NAADP binding sites in sea urchin egg homogenates. [32P]NAADP bound to a single class of high-affinity sites that were reversibly inhibited by NaCl but insensitive to pH and Ca2+. Binding of [32P]NAADP was lost in preparations that did not mobilize Ca2+ in response to NAADP, indicating that [32P]NAADP probably binds to a receptor mediating Ca2+ mobilization. Addition of excess unlabelled NAADP, at various times after initiation of [32P]NAADP binding, did not result in displacement of bound [32P]NAADP. These data show that NAADP becomes irreversibly bound to its receptor immediately upon association. Accordingly, incubation of homogenates with low concentrations of NAADP resulted in maximal labelling of NAADP binding sites. This unique property renders NAADP receptors exquisitely sensitive to their ligand, thereby allowing detection of minute changes in NAADP levels.

Ryanodine Activates Sea Urchin Eggs. (sea urchin egg/activation/ryanodine/inositol phosphate/heparin)

1992 ◽  
Vol 34 (1) ◽  
pp. 37-42 ◽  
Author(s):  
C. Sardet ◽  
I. Gillot ◽  
A. Ruscher ◽  
P. Payan ◽  
J.-P. Girard ◽  
...  
Keyword(s):  
Sea Urchin ◽  
Inositol Phosphate ◽  
Egg Activation ◽  
Sea Urchin Eggs ◽  
Sea Urchin Egg

The Respiratory and Glycolytic Enzymes of Sea-Urchin Eggs

1954 ◽  
Vol 31 (2) ◽  
pp. 208-217
Author(s):  
MARTYNAS YČAS
Keyword(s):  
Cytochrome C ◽  
Sea Urchin ◽  
Strongylocentrotus Purpuratus ◽  
Lactic Dehydrogenase ◽  
Glycolytic Pathway ◽  
Endogenous Respiration ◽  
Centrifugal Field ◽  
Lytechinus Pictus ◽  
Sea Urchin Eggs ◽  
Sea Urchin Egg

1. Activity corresponding to phosphoglucomutase, phosphohexoisomerase, aldolase, triosephosphate dehydrogenase, enolase and lactic dehydrogenase has been demonstrated in homogenates prepared from unfertilized sea-urchin eggs (Strongylocentrotus purpuratus and Lytechinus pictus). 2. The presence of cytochromes a and b1 has been confirmed. These cytochromes sediment in a relatively low centrifugal field. 3. No cytochrome c could be demonstrated, although cytochrome c is both reduced and oxidized by homogenates, and addition of cytochrome c increases the endogenous respiration and oxidation of succinate. 4. These results support the view that the usual glycolytic pathway operates in the sea-urchin egg and is the principal route of oxidation of carbohydrate.

scholarly journals Actin in triton-treated cortical preparations of unfertilized and fertilized sea urchin eggs.

1979 ◽  
Vol 82 (1) ◽  
pp. 212-226 ◽  
Author(s):  
A Spudich ◽  
J A Spudich
Keyword(s):  
Electron Microscopy ◽  
Sea Urchin ◽  
Actin Filaments ◽  
Cell Types ◽  
Optical Diffraction ◽  
Muscle Actin ◽  
Sea Urchin Eggs ◽  
Inner Surface ◽  
Low Ionic Strength ◽  
Helical Parameters

Triton-treated cortical fragments of unfertilized and fertilized sea urchin eggs prepared in the presence of greater than or equal to 5 mM EGTA contain 15-30% of the total egg actin. However, actin filaments are not readily apparent by electron microscopy on the cortical fragments of unfertilized eggs but are numerous on those of fertilized eggs. The majority of the actin associated with cortical fragments of unfertilized eggs is solubilized by dialysis against a low ionic strength buffer at pH 7.5. This soluble actin preparation (less than 50% pure actin) does not form proper filaments in 0.1 M KCl and 3 mM MgCl2, whereas actin purified from this preparation does, as judged by electron microscopy. Optical diffraction analysis reveals that these purified actin filaments have helical parameters very similar to those of muscle actin. Furthermore, the properties of the purified actin with regard to activation of myosin ATPase are similar to those of actin from other cell types. The possibility that actin is maintained in a nonfilamentous form on the inner surface of the unfertilized egg plasma membrane and is induced to assemble upon fertilization is discussed.

scholarly journals STUDIES ON SULFHYDRYL GROUPS DURING CELL DIVISION OF SEA URCHIN EGG

1960 ◽  
Vol 8 (3) ◽  
pp. 603-607 ◽  
Author(s):  
Hikoichi Sakai
Keyword(s):  
Cell Division ◽  
Sea Urchin ◽  
Sulfhydryl Groups ◽  
Cell Stage ◽  
Sea Urchin Eggs ◽  
Maximum Value ◽  
Sea Urchin Egg ◽  
Egg Cortex

Masses of cortices of both unfertilized and fertilized sea urchin eggs can be isolated by crushing eggs in hypotonic MaCl2 (0.1 M) solution. The amount of cortical material in terms of protein-N increases steadily after fertilization until the monaster stage and thereafter remains almost constant until well into the two-cell stage. The amount of bound—SH per protein-N of the egg cortex also increases after fertilization, reaches a maximum value at the amphiaster stage and thereafter decreases rapidly as the cleavage of the cell proceeds.

Sign in / Sign up

Export Citation Format

Share Document