Identification of a calcium-binding protein as a calcium-dependent regulator of brain adenylate cyclase.

Brostrom, Charles O.; Huang, Yung-Chen; Breckenridge, Bruce McL.; Wolff, Donald J.

doi:10.1073/pnas.72.1.64

Cited by 489 publications

(126 citation statements)

References 19 publications

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“…It was, however, quite stable and was stored frozen for periods up to 1 month with no loss of activity. DISCUSSION Brain adenylate cyclase shows a biphasic response to Ca2+ (1)(2)(3)(4)(5) and CDR mediates Ca2+ stimulation of the enzyme (3,(5)(6)(7)(8). Brostrom et al (8) recently proposed that brain cortex contains separate CDR-sensitive and -insensitive forms of adenylate cyclase.…”

Section: Resultsmentioning

confidence: 99%

Resolution of adenylate cyclase sensitive and insensitive to Ca2+ and calcium-dependent regulatory protein (CDR) by CDR-sepharose affinity chromatography.

Westcott¹,

Porte²,

Storm³

1979

Proc. Natl. Acad. Sci. U.S.A.

172

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Section: Resultsmentioning

confidence: 99%

Resolution of adenylate cyclase sensitive and insensitive to Ca2+ and calcium-dependent regulatory protein (CDR) by CDR-sepharose affinity chromatography.

Westcott¹,

Porte²,

Storm³

1979

Proc. Natl. Acad. Sci. U.S.A.

172

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“…It could be due to activation of adenylate cyclase or to inhibition of cyclic nucleotide phos-phodiesterase, but the latter seems less likely because the phosphodiesterase inhibitor 1-methyl-3-isobutylxanthine potentiates the calcium effect. Because a calcium-dependent regulator protein (calmodulin) has been shown to activate adenylate cyclase of brain (29) and to be present in spermatozoa (30,31), possibly in the acrosomal area (32), the activation of an acrosomal membrane adenylate cyclase (33) by a Ca2+_ calmodulin complex seems possible. The results also suggest that more than one Ca2+-dependent process is responsible for induction of the guinea pig sperm acrosome reaction.…”

Section: Discussionmentioning

confidence: 99%

Calcium-dependent increase in adenosine 3′,5′-monophosphate and induction of the acrosome reaction in guinea pig spermatozoa

Hyne

Garbers

1979

Proc. Natl. Acad. Sci. U.S.A.

107

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Experiments were designed to determine the interrelationship between cyclic AMP and Ca2+ during the processes of sperm capacitation and the acrosome reaction. In minimal culture media containing pyruvate and lactate as substrates, guinea pig spermatozoa required a minimum of 1.0-1.5 hr to capacitate in the presence of 1.7 mM Ca2+ and a minimum of 0.5-1.0 hr to capacitate in the absence of added Ca2+. Sperm cyclic AMP concentrations were increased by as much as 30-fold within 0.5 min after addition of cells to various media containing Ca2+, and the concentrations then remained increased for up to 4 hr. When the cells were added to several Ca2+-deficient media, however, cyclic AMP concentrations increased only about 3-fold within 0.5 min and then returned to basal concentrations within 2 min. D-600, a calcium transport antagonist, completely blocked the Ca2+-induced increase in sperm cyclic AMP concentrations. In contrast to capacitation, the acrosome reaction failed to occur in the absence of extracellular Ca2+. After capacitation of spermatozoa in a Ca2+-free medium, addition of Ca2+ caused an increase in sperm cyclic AMP concentrations within 1 min and a maximal number of spermatozoa showing an acrosome reaction within 10 min. The addition of 1-methyl-3-isobutylxanthine along with Ca2+ had a synergistic effect on the increase in cyclic AMP. Neither 1-methyl-3-isobutylxanthine nor 8-Br cyclic AMP induced an acrosome reaction in capacitated spermatozoa in the absence of Ca2+, but both significantly decreased the time required for maximal expression of the acrosome reaction in the presence of Ca2+. These results suggest that the sperm acrosome reaction is associated with both a primary transport of Ca2+ and a Ca2+±dependent increase in sperm cyclic AMP concentrations. Because a cyclic AMP analogue did not induce an acrosome reaction in the absence of added Ca2+, the increase in sperm cyclic AMP concentrations induced by Ca2+ probably reflects one of a number of Ca2+-dependent events associated with the acrosome reaction.

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“…CaM has been demonstrated to regulate cyclic nucleotide metabolism (Brostrom et al, 1975), mitosis, cell cycle progression (Rasmussen & Means, 1989) and phosphorylation of oestrogen receptor (ER) (Migliaccio et al, 1984). It has also been reported that oestrogens influence the synthesis of CaM in the rabbit myometrium (Matsui et al, 1983) and in rat and human uteri (Yoshida et al, 1985).…”

mentioning

confidence: 99%

Calmodulin levels in oestrogen receptor positive and negative human breast tumours

Krishnaraju

Murugesan²,

Vij³

et al. 1991

Br J Cancer

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Calmodulin (CaM) is one of the intracellular calcium binding proteins which regulates the functions of proteins and enzymes associated with various cellular processes (for review Klee & Newton, 1985;Cohen, 1988). CaM has been demonstrated to regulate cyclic nucleotide metabolism (Brostrom et al., 1975), mitosis, cell cycle progression (Rasmussen & Means, 1989) and phosphorylation of oestrogen receptor (ER) (Migliaccio et al., 1984). It has also been reported that oestrogens influence the synthesis of CaM in the rabbit myometrium (Matsui et al., 1983) and in rat and human uteri (Yoshida et al., 1985). Since Wei and Hickie (1981) with minor modifications. The tissue was homogenised in three volumes of Tris-HCl pH 6.8 (buffer-A), consisting of 60 mM Tris-HCI and 1 mM EGTA and the supernatant was prepared by centrifuging the homogenate at 105,000 g for 1 h at 4°C. The pellet was rehomogenised with three volumes of buffer-A and the supernatant was prepared as described above. The supernatants from the first and second centrifugation were pooled and used for the assay of CaM in the soluble fraction. To assay the CaM in the particulate fraction, the pellet was homogenised in three volumes of buffer-B, consisting of buffer-A and 2% Triton-X 100. The homogenate was left at 4°C for 2 h and stirred intermittently. The supernatant was prepared by centrifuging the homogenate at 105,000 g for 1 h at 4°C. The pellet was rehomogenised with three volumes of buffer-B and the supernatant was prepared as described above. The supernatants from these two fractions were pooled and used for the assay. CaM in the soluble and particulate fractions were assayed according to the method of Veigl et al. (1984). Briefly, samples along with 100 ng of standard CaM (Purified bovine brain CaM, Sigma Chemical Co, St. Louis, USA) was electrophoresed on 1 mm thick, 15% polyacrylamide gels and stained with silver nitrate (Morrissey, 1981) Figure 1 Correlation of ER levels with calmodulin levels in ER+ breast tumours (r = 0.77, P<0.001, n = 23).

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Identification of a calcium-binding protein as a calcium-dependent regulator of brain adenylate cyclase.

Abstract: An activating factor of adenylate cyclase (EC 4.6

Cited by 489 publications

References 19 publications

Resolution of adenylate cyclase sensitive and insensitive to Ca2+ and calcium-dependent regulatory protein (CDR) by CDR-sepharose affinity chromatography.

Resolution of adenylate cyclase sensitive and insensitive to Ca2+ and calcium-dependent regulatory protein (CDR) by CDR-sepharose affinity chromatography.

Calcium-dependent increase in adenosine 3′,5′-monophosphate and induction of the acrosome reaction in guinea pig spermatozoa

Calmodulin levels in oestrogen receptor positive and negative human breast tumours

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