Adenylate cyclase activity from Hirudo medicinalis segmental ganglia: modulation by calcium and calmodulin

Ferretti, Maria Enrica; Pareschi, Maria Cristina; Buzzi, Marco; Biondi, Carla

doi:10.1016/0300-9629(94)00142-g

Cited by 3 publications

(2 citation statements)

References 33 publications

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“…5-HT receptors linked to adenylyl cyclase activity have been described in the leech central nervous system (Ferretti et al, 1995), and multiple effects on membrane K ϩ currents (Acosta-Urquidi et al, 1989) and transporters (Catarsi and Brunelli, 1991;Catarsi et al, 1993) have been reported using this pathway in central neurons. In the giant glial cells, 5-HT evoked a membrane hyperpolarization (Walz and Schlue, 1982) and a Ca 2ϩ influx into soma and dendrites .…”

Section: -Ht Receptor In the Giant Glial Cellmentioning

confidence: 98%

5‐Hydroxytryptamine activates a barium‐sensitive, cAMP‐mediated potassium conductance in the leech giant glial cell

Britz

Hirth

Schneider

et al. 2004

Glia

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5-Hydroxytryptamine (5-HT), a neurotransmitter and neuromodulator in the central nervous system of the leech Hirudo medicinalis hyperpolarizes the giant glial cell in the neuropil of segmental ganglia at micromolar concentrations. The 5-HT-evoked glial response (EC(50) approximately 2.5 microM) is mediated by a non-desensitizing, G-protein-coupled receptor and due to activation of a Ca(2+)-independent K(+) conductance. The adenylyl cyclase inhibitor SQ22,536 blocks the response to 5-HT; in the presence of 1 mM db-cAMP, but not of 1 mM db-cGMP, the glial response is suppressed. The 5-HT-evoked response is reduced by Ba(2+) with half-maximal inhibition at 50 microM Ba(2+). The results suggest that release of 5-HT from serotonergic neurons, or the maintenance of micromolar levels of extracellular 5-HT in the ganglion, may help to set the glial membrane potential close to the K(+) equilibrium potential.

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Section: -Ht Receptor In the Giant Glial Cellmentioning

confidence: 98%

5‐Hydroxytryptamine activates a barium‐sensitive, cAMP‐mediated potassium conductance in the leech giant glial cell

Britz

Hirth

Schneider

et al. 2004

Glia

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“…It is also found in adenylate cyclase [47]. Grp78 and adenylate cyclase have been shown to be regulated by calcium [5][6][7]48]. The biological significance of this metal-binding site in the ATPase domains of heat shock proteins remains to be seen.…”

Section: The Second Calcium-binding Sitementioning

confidence: 99%

Human Hsp70 molecular chaperone binds two calcium ions within the ATPase domain

et al. 1997

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The structural similarity of hATPase and bATPase and the sequence similarity within the Hsp70 chaperone family suggest a universal mechanism of ATP hydrolysis among all Hsp70 molecular chaperones. Two calcium ions have been found in the hATPase structure. One corresponds to the magnesium site in bATPase and appears to be important for ATP hydrolysis and in vitro phosphorylation. Local changes in protein structure as a result of calcium binding may facilitate phosphorylation. A small, but significant, movement of metal ions and sidechains could position catalytically important threonine residues for phosphorylation. The second calcium site represents a new calcium-binding motif that can play a role in the stabilization of protein structure. We discuss how the information about catalytic events in the active site could be transmitted to the peptide-binding domain.

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Structural-functional characteristics of the adenylyl cyclase signaling system regulated by biogenic amines and peptide hormones in muscles of the earthworm Lumbricus terrestris

Шпаков

Shpakova

Kuznetsova

et al. 2008

J Evol Biochem Phys

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Adenylate cyclase activity from Hirudo medicinalis segmental ganglia: modulation by calcium and calmodulin

Cited by 3 publications

References 33 publications

5‐Hydroxytryptamine activates a barium‐sensitive, cAMP‐mediated potassium conductance in the leech giant glial cell

5‐Hydroxytryptamine activates a barium‐sensitive, cAMP‐mediated potassium conductance in the leech giant glial cell

Human Hsp70 molecular chaperone binds two calcium ions within the ATPase domain

Structural-functional characteristics of the adenylyl cyclase signaling system regulated by biogenic amines and peptide hormones in muscles of the earthworm Lumbricus terrestris

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