Tissue specificity and physiological relevance of various isoforms of adenylyl cyclase

Defer, Nicole; Best‐Belpomme, Martin; Hanoune, Jacques

doi:10.1152/ajprenal.2000.279.3.f400

Cited by 358 publications

(343 citation statements)

References 200 publications

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“…Although, there is not definite evidence for it, the best hypothesis to explain the attenuating effect of CPA on dopamine-evoked NHE3 inhibition is a CPA-dependent suppression of AC, most probably type VI AC in the case of the low dose of CPA, whereas overall depression of AC activity may explain the effects exerted by micromolar concentrations of CPA. The latter speculation is consistent with results documenting that all forms of AC are sensitive to very high concentrations of intracellular Ca 2ϩ (in the submillimolar range) [for review, see (33)]. …”

Section: Discussionsupporting

confidence: 88%

“…Currently, it is not known which subtype of AC is involved in CPA-induced activation of NHE3. As found by Northern blot analysis, at least five AC isoforms are expressed in rat kidney (type IV, type V, type VI, type VII, and type IX) [for review, see (33)]. Of these isoforms, types V and VI are inhibitable by calcium, and type VI mRNA is expressed along the entire nephron, whereas type V mRNA is restricted to the glomerulus and the initial portion of the collecting duct (34).…”

Section: Discussionmentioning

confidence: 99%

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Bimodal Acute Effects of A1 Adenosine Receptor Activation on Na+/H+ Exchanger 3 in Opossum Kidney Cells

Sole¹,

Cerull²,

Petzke³

et al. 2003

Journal of the American Society of Nephrology

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Abstract. Regulation of renal apical Na ϩ /H ϩ exchanger 3 (NHE3) activity by adenosine has been suggested to contribute to acute control of mammalian Na ϩ homeostasis. The mechanism by which adenosine controls NHE3 activity in a renal cell line was examined. The adenosine analog, N 6 -cyclopentyladenosine (CPA) exerts a bimodal effect on NHE3: CPA concentrations Ͼ10 Ϫ8 M inactivate NHE3, whereas concentrations Ͻ10 Ϫ8 M stimulate NHE3 activity. Acute CPA-induced control of NHE3 was blocked by antagonists of A 1 adenosine receptors and inhibition of phospholipase C, pretreatment with BAPTA-AM (chelator of cellular calcium), and exposure to pertussis toxin. Stimulatory and to some extent also inhibitory CPA concentrations attenuated 8-bromo-cAMP and dopaminemediated inhibition of NHE3. BAPTA eliminated the ability of a stimulatory dose of CPA to attenuate 8-bromo-cAMP-induced suppression of NHE3 activity. Upon inhibition of protein kinase C, CPA at an inhibitory dose provoked activation of NHE3, which is partially reverted by 8-bromo-cAMP and suppressed by pre-incubation with BAPTA-AM. Cytochalasin B, an actin-modifying agent, selectively prevented downregulation but did not affect upregulation of NHE3 activity by CPA. In conclusion, these observations demonstrate that (1) CPA modulates NHE3 activity by elevation of cellular Ca 2ϩ exerting a negative control on adenylate cyclase activity, (2) protein kinase C is the determining factor leading to CPAinduced downregulation of NHE3 activity, and (3) alterations of surface NHE3 abundance may contribute to A 1 adenosine receptor-dependent inhibition of NHE3 activity.

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Section: Discussionsupporting

confidence: 88%

Section: Discussionmentioning

confidence: 99%

Bimodal Acute Effects of A1 Adenosine Receptor Activation on Na+/H+ Exchanger 3 in Opossum Kidney Cells

Sole¹,

Cerull²,

Petzke³

et al. 2003

Journal of the American Society of Nephrology

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“…In the central nervous system the highest expression of mAC III is exhibited in the olfactory neuroepithelium, whereas the important site of mAC VIII expression is the hypothalamus (35). G␣ olf has the capacity to stimulate both mAC III and mAC VIII (36, 37), whereas both enzymes are unaffected by G␣ i or G␤␥ (38). Increased Ca 2ϩ concentration has the opposite effects on mAC isoforms III and VIII.…”

Section: Discussionmentioning

confidence: 99%

Particulate Adenylate Cyclase Plays a Key Role in Human Sperm Olfactory Receptor-mediated Chemotaxis

Spehr

Schwane

Riffell

et al. 2004

Journal of Biological Chemistry

142

131

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Human sperm chemotaxis is a critical component of the fertilization process, but the molecular basis for this behavior remains unclear. Recent evidence shows that chemotactic responses depend on activation of the sperm olfactory receptor, hOR17-4. Certain floral scents, including bourgeonal, activate hOR17-4, trigger pronounced Ca 2؉ fluxes, and evoke chemotaxis. Here, we provide evidence that hOR17-4 activation is coupled to a cAMP-mediated signaling cascade. Multidimensional protein identification technology was used to identify potential components of a G-protein-coupled cAMP transduction pathway in human sperm. These products included various membrane-associated adenylate cyclase (mAC) isoforms and the G olf -subunit. Using immunocytochemistry, specific mAC isoforms were localized to particular cell regions. Whereas mAC III occurred in the sperm head and midpiece, mAC VIII was distributed predominantly in the flagellum. In contrast, G olf was found mostly in the flagellum and midpiece. The observed spatial distribution patterns largely correspond to the spatiotemporal character of hOR17-4-induced Ca 2؉ changes. Behavioral and Ca 2؉ signaling responses of human sperm to bourgeonal were bioassayed in the presence, or absence, of the adenylate cyclase antagonist SQ22536. This specific agent inhibits particulate AC, but not soluble AC, activation. Upon incubation with SQ22536, cells ceased to exhibit Ca 2؉ signaling, chemotaxis, and hyperactivation (faster swim speed and flagellar beat rate) in response to bourgeonal. Particulate AC is therefore required for induction of hOR17-4-mediated human sperm behavior and represents a promising target for future design of contraceptive drugs.

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“…These conditions seem to depend on the isoform of adenylyl cyclase involved or on the interruption of a previous long-term exposure to D 2 receptor agonists (Yao et al, 2002;Kudlacek et al, 2003;Vortherms and Watts, 2004). In any case, the main isoform of adenylyl cyclase in the striatum is AC5, and co-stimulation of G s -and G i -coupled receptors shows antagonistic interactions at the AC5 level (Chern, 2000;Defer et al, 2000). In fact, D 2 receptor stimulation has been shown to counteract cAMP accumulation induced by A 2A receptor stimulation in membrane preparations from mouse striatum (Lee et al, 2002).…”

Section: Discussionmentioning

confidence: 99%

Stimulation of Adenosine Receptors Selectively Activates Gene Expression in Striatal Enkephalinergic Neurons

Karcz-Kubicha

Ferré

Diaz-Ruiz

et al. 2006

Neuropsychopharmacol

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In the striatum, adenosine A 2A and dopamine D 2 receptors exert reciprocal antagonistic interactions that modulate the function of GABAergic enkephalinergic neurons. We have previously shown that stimulation of adenosine A 1 receptors allows the stimulation of A 2A receptors to overcome a tonic inhibitory effect of D 2 receptors and induce striatal expression of c-fos. In the present work, by studying co-localization of c-Fos immunoreactivity and preproenkephalin and preprodynorphin transcripts, we show that co-administration of the A 1 receptor agonist CPA and the A 2A receptor agonist CGS 21680 increases the striatal expression of c-fos in GABAergic enkephalinergic but not in GABAergic dynorphinergic neurons. Co-administration of CPA and CGS 21680 also induced a significant increase in the striatal expression of preproenkephalin. The results underscore the role of adenosine in the activation of gene expression in the GABAergic enkephalinergic neuron.

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Tissue specificity and physiological relevance of various isoforms of adenylyl cyclase

Cited by 358 publications

References 200 publications

Bimodal Acute Effects of A1 Adenosine Receptor Activation on Na+/H+ Exchanger 3 in Opossum Kidney Cells

Bimodal Acute Effects of A1 Adenosine Receptor Activation on Na+/H+ Exchanger 3 in Opossum Kidney Cells

Particulate Adenylate Cyclase Plays a Key Role in Human Sperm Olfactory Receptor-mediated Chemotaxis

Stimulation of Adenosine Receptors Selectively Activates Gene Expression in Striatal Enkephalinergic Neurons

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