Characterization of ATP-stimulated guanylate cyclase activation in rat lung membranes

Chang, Chung Ho; Kohse, Klaus P.; Chang, Bing; Hirata, Masato; Jiang, Bin; Douglas, Janice E.; Murad, Ferid

doi:10.1016/0167-4889(90)90071-k

Cited by 102 publications

(60 citation statements)

References 17 publications

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“…Moreover, the ability of ATP to stimulate the ANP receptor guanylate cyclase activity is lost upon solubilization in a nonionic detergent, as we observed for the photoreceptor enzyme. ATP, nonhydrolyzable ATP analogues, or ADP also enhance ligand-induced cyclase activation (40,41,43,44). Thus, ATP potentiates both basal cyclase activity and ligand stimulation throughout the family of receptor guanylate cyclases.…”

Section: Discussionmentioning

confidence: 96%

The Photoreceptor Guanylate Cyclase Is an Autophosphorylating Protein Kinase

Aparicio¹,

Applebury²

1996

Journal of Biological Chemistry

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The membrane guanylate cyclase of vertebrate photoreceptor rod outer segments plays a key role in controlling the levels of cGMP, the intracellular second messenger that mediates visual signaling (1-5). In the dark-adapted photoreceptor, the resting cGMP levels are set by the balance of synthesis and degradation due to the basal activities of the guanylate cyclase and the cGMP phosphodiesterase. Throughout the processes of phototriggering, photorecovery, and light adaptation, the activity of the guanylate cyclase appears to be modulated to control cGMP levels. Several factors are known to regulate the guanylate cyclase activity. Intracellular calcium concentration in the range of 0.1 to 1 M inhibits cyclase activity in the presence of small calcium-binding proteins, GCAPs 1 (6 -8). In contrast, a protein of 40 kDa, composed of a multimer of 6 -7-kDa peptides, activates the cyclase in a calcium-dependent manner with halfmaximal activation occurring between 2 and 5 M (9). In addition, guanylate cyclase activity has been reported to be modulated by ATP (10, 11) and by protein kinase C (12). The calcium regulation mediated by GCAPs is thought to be responsible for cyclase activation during photorecovery and light adaptation; however, the physiological significance of regulation by the other factors is unclear. In all cases, the mechanisms by which these factors control the activity of the photoreceptor guanylate cyclase are not understood.The primary structure of the photoreceptor membrane guanylate cyclase has been deduced from cDNA sequences isolated from human, bovine, and rat retinas (13-15). 2 The information indicates that it is a member of the family of membrane guanylate cyclases that function as receptors for peptide ligands. Four functional domains are characteristic of these proteins: an amino-terminal "extracellular" domain, a transmembrane region, an intracellular protein kinase-like domain, and a carboxylterminal guanylate cyclase catalytic domain (17)(18)(19). In other members of the family, binding of peptide ligands to the extracellular amino-terminal domains induces stimulation of cytoplasmic guanylate cyclase activity. Molecules known to function in this manner include receptors for ANP (GC-A) and CNP (GC-B), guanylin and Escherichia coli enterotoxin (GC-C), and the sea urchin egg peptides, speract and resact. Although no ligand has been identified for the photoreceptor guanylate cyclase, its structural similarity to the receptor guanylate cyclases suggests that it may be regulated in a similar manner.In this work, we have focused on the role of the kinase-like domain of the photoreceptor guanylate cyclase. Studies of other members of the receptor guanylate cyclase family clearly indicate that the kinase homology domain is required to transduce the ligand-binding signals and activate the guanylate cyclases (20 -22). ATP is required for ligand-mediated activation, but nonhydrolyzable ATP analogues work as well (17). No kinase activity has been measured for any receptor guanylate cyclase, and autoph...

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Section: Discussionmentioning

confidence: 96%

The Photoreceptor Guanylate Cyclase Is an Autophosphorylating Protein Kinase

Aparicio¹,

Applebury²

1996

Journal of Biological Chemistry

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“…Guanylyl Cyclase Assay in Membranes-GC activity in crude membranes was assayed as described (24). Briefly, the reaction was initiated by addition of 30 g of membrane protein in a final volume of 0.3 ml of solution containing 50 mM Tris-HCl (pH 7.5), 2 mM 3-isobutyl-1-methylxanthine, 1 mM GTP, 4 mM MgCl 2 , 0.1% (w/v) BSA, 7.5 mM creatine phosphate, and 15 units/ml creatine phosphokinase (250 units/mg of protein).…”

Section: Cell Culture and Stable Transfection Of Recombinant Receptors-mentioning

confidence: 99%

Molecular and Cellular Physiology of the Dissociation of Atrial Natriuretic Peptide from Guanylyl Cyclase A Receptors

Vieira

Gao

Nikonova

et al. 2001

Journal of Biological Chemistry

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Atrial natriuretic peptide (ANP), 1 a member of the natriuretic peptide family that includes brain natriuretic peptide and C-type natriuretic peptide, plays a fundamental role in the regulation of blood pressure, plasma volume, and renal function (1, 2). Two distinct classes of ANP receptors, named clearance and guanylyl cyclase (GC) receptors, have been biochemically and functionally well characterized (1, 3). Clearance receptors of ANP, the most abundant class of the natriuretic peptide receptors, have a single transmembrane domain, a short cytoplasmic tail of 37 amino acids, and an extracellular binding domain that has a significant homology to the extracellular domain of GC receptors (1, 4 -6). An extensive series of physiological, pharmacological, cellular, and genetic studies have shown that clearance receptors are importantly involved in the systemic and local clearance of ANP (7-11). This clearance function is accomplished by an efficient mechanism of receptor-mediated endocytosis. Endocytosed ANP is delivered to lysosomes, where it is hydrolyzed to its constituent amino acids, and the internalized receptors are recycled to the cell membrane (10, 12). The efficiency of this receptor-mediated endocytic mechanism is enhanced by a relatively low rate of dissociation of ANP from cell-surface receptors (12).Guanylyl cyclase subtype A (GCA) receptors mediate all of the known cardiovascular and renal effects of ANP (2, 13). GCA receptors have a single transmembrane domain, an extracellular ligand-binding domain, and a cytoplasmic domain constituted by a catalytic GC sequence and a tyrosine kinase-like (TK) sequence interposed between the transmembrane and the catalytic domains (14). Between the TK and GC sequences there is an amphipathic ␣-helical region that is involved in higher order oligomerization of GCA receptors (15,16). Under basal conditions, the TK domain has an inhibitory effect on GC activity. It has been postulated that upon ANP (or brain natriuretic peptide) binding to the extracellular domain, ATP binds to the TK domain and allosterically activates the catalytic GC domain (14,17).Previous studies in our laboratory have demonstrated that the native GCA in cultured glomerular mesangial and renomedullary interstitial cells is a constitutive membrane resident protein that does not undergo endocytosis and does not mediate lysosomal hydrolysis of ligand (18). Moreover, the dissociation of ANP from native GCA is very slow at subphysiological temperatures and increases exponentially at near physiological temperatures (18). We postulated that the rapid dissociation of ANP from surface GCA

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“…Studies with ANF-RGC and CNP-RGC show that the mere ligand binding to the receptor domain is not enough to maximally stimulate the cyclase activity [18,19]; obligatory in this activation process is an intervening step, which is regulated by ATP [20,21]. ATP binding causes an allosteric change in guanylate cyclase, bringing it to the activated-catalytic state.…”

Section: Introductionmentioning

confidence: 99%

The glycine residue of ATP regulatory module in receptor guanylate cyclases that is essential in natriuretic factor signaling

1993

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Atrial natriuretic factor (ANF) and C-type natriuretic peptide (CNP)-activated guanylate cyclases are single-chain transmembrane-spanning proteins, containing both ligand binding and catalytic activities. In both proteins, ligand binding to the extracellular receptor domain activates the cytosolic catalytic domain, generating the second messenger cyclic GMP. Obligatory in this activation process is an ATP-dependent step. ATP directly binds to a deBned ATP-regulatory module (ARM) sequence motif in the cyclases and through ARM bridges the events of ligand binding and signal transduction. These ARM sequence motifs are respectively represented by GlySo'-Xa-Gl$05-Xa-Xa-Xa-Gly509 and Gly@-Xa-Xa-XaGly"' in the case of ANF receptor guanylate cyclase (ANF-RGC) and CNP receptor guanylate cyclase (CNP-RGC). Through genetic remodeling techniques, we now show that ARM-GlJo5 in ANF-RGC and the corresponding ARM-Gly"% in CNP-RGC are critical for ANF and CNP signaling, and other ARM-Gly residues have minimal effect in the respective signaling processes.Guanylate cyclase; ATP-regulatory module; Atrial natriuretic factor receptor; Type C natriuretic peptide receptor

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Characterization of ATP-stimulated guanylate cyclase activation in rat lung membranes

Cited by 102 publications

References 17 publications

The Photoreceptor Guanylate Cyclase Is an Autophosphorylating Protein Kinase

The Photoreceptor Guanylate Cyclase Is an Autophosphorylating Protein Kinase

Molecular and Cellular Physiology of the Dissociation of Atrial Natriuretic Peptide from Guanylyl Cyclase A Receptors

The glycine residue of ATP regulatory module in receptor guanylate cyclases that is essential in natriuretic factor signaling

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