Molecular Determinants of the Clearance Function of Type C Receptors of Natriuretic Peptides

Cohen, David E.; Koh, Gou Young; Nikonova, Lena N.; Porter, J G; Maack, Thomas

doi:10.1074/jbc.271.16.9863

Cited by 67 publications

(47 citation statements)

References 26 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Our results cannot be attributed to a putative defect of CHO cells to effectuate receptor endocytosis or to an intrinsic decrease in receptor affinity in these cells. Indeed, we have previously shown that clearance receptors of natriuretic peptides stably transfected into CHO cells undergo robust endocytosis and have very low receptor-ligand dissociation at 37°C (12). Thus, the lack of appreciable endocytosis and the rapid receptorligand dissociation of native GCA in primary culture cells or of GCA stably transfected into CHO cells are likely to reflect the dynamics of this receptor under physiological conditions.…”

Section: Discussionmentioning

confidence: 99%

“…Fate I-ANP-(1-28) in intact cells was determined by chase experiments as previously described (10,12). Briefly, CHO cells stably transfected with GCAWT or mutant GCA receptors were grown to near confluence in six-well plates.…”

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

confidence: 99%

“…Competition Binding Experiments in Cell Monolayers-Equilibrium competition binding experiments were performed in intact cells at 4°C to obtain the apparent density (B max ) and apparent equilibrium dissociation constant (K i ) of ANP-specific binding sites as previously described (10,12). Cells plated in 24-well plates to near confluence were incubated for 3-4 h at 4°C with binding solution containing trace amounts of Membrane Preparation-CHOGCAWT or CHOGCACYT Ϫ cells were grown to confluence in 850-cm 2 roller bottles.…”

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

confidence: 99%

“…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).…”

mentioning

confidence: 99%

See 3 more Smart Citations

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

Self Cite

View full text Add to dashboard Cite

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

show abstract

Section: Discussionmentioning

confidence: 99%

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

confidence: 99%

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

confidence: 99%

mentioning

confidence: 99%

See 2 more Smart Citations

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

Self Cite

View full text Add to dashboard Cite

show abstract

“…The clearance receptor lacks the GCase domain and is not a GCasecoupled signaling receptor (18). Rather, the receptor mediates metabolic clearance of natriuretic peptides from the circulation (19,20). Nevertheless, the clearance receptor has considerable sequence homology with the corresponding extracellular and transmembrane regions of the ANP receptor and, consequently, is expected to have a similar overall structure.…”

mentioning

confidence: 99%

Constitutive Activation and Uncoupling of the Atrial Natriuretic Peptide Receptor by Mutations at the Dimer Interface

Qiu

Ogawa

Miyagi

et al. 2004

Journal of Biological Chemistry

View full text Add to dashboard Cite

The crystal packing of the extracellular hormone binding domain of the atrial natriuretic peptide (ANP) receptor contains two possible dimer pairs, the head-tohead (hh) and tail-to-tail (tt) dimer pairs associated through the membrane-distal and membrane-proximal subdomains, respectively. The tt-dimer structure has been proposed previously (van den Akker, F., Zhang, X., Miyagi, M., Huo, X., Misono, K. S., and Yee, V. C. (2000) Nature 406, 101-104). However, no direct evidence is available to identify the physiological dimer form. Here we report site-directed mutagenesis studies of residues at the two alternative dimer interfaces in the full-length receptor expressed on COS cells. The Trp 74 to Arg mutation (W74R) or D71R at the hh-dimer interface caused partial constitutive guanylate cyclase activation, whereas mutation F96D or H99D caused receptor uncoupling. In contrast, mutation Y196D or L225D at the ttinterface had no such effect. His 99 modification at the hh-dimer interface by ethoxyformic anhydride abolished ANP binding. These results suggest that the hhdimer represents the physiological structure. Recently, we determined the crystal structure of ANPR complexed with ANP and proposed a hormone-induced rotation mechanism mediating transmembrane signaling (H. Ogawa, Y. Qiu, C. M. Ogata, and K. S. Misono, submitted for publication). The observed effects of mutations are consistent with the ANP-induced structural change identified from the crystal structures with and without ANP and support the proposed rotation mechanism for ANP receptor signaling. Atrial natriuretic peptide (ANP)1 is a hormone secreted from the heart in response to atrial distension. ANP plays a major role in the regulation of blood pressure and electrolytes-fluid volume homeostasis through its natriuretic (1) and vasorelaxant activities (2, 3). ANP also has an antitrophic activity, through which it regulates maintenance and remodeling of the cardiovascular system (4 -7). Transgenic animals lacking the ANP gene develop salt-sensitive hypertension (8), and those lacking the ANP receptor gene develop salt-insensitive essential hypertension accompanied by severe cardiac hypertrophy (9), implicating the ANP and ANP receptor system in cardiovascular pathophysiology. The hormonal actions of ANP are mediated by a cell membrane receptor carrying intrinsic guanylate cyclase (GCase) activity. The receptor occurs as a dimer of a single span transmembrane polypeptide containing an extracellular hormone binding domain and an intracellular domain consisting of an ATP-dependent regulatory domain and a GCase catalytic domain (10). ANP binding stimulates GCase activity and elevates intracellular cGMP levels. cGMP, in turn, mediates hormonal actions via cGMP-regulated ion channels, protein kinases, and phosphodiesterases (11). The ANP receptor belongs to the family of GCase-coupled receptors which includes retinal GCases (12), olfactory GCases (13), and guanylin and enterotoxin receptors (14). These receptors have a similar overall molecular topology and may ...

show abstract

Atrial Natriuretic Peptide and Other Natriuretic Factors in Cirrhosis

Villa¹

2005

Ascites and Renal Dysfunction in Liver Disease

View full text Add to dashboard Cite

Molecular Determinants of the Clearance Function of Type C Receptors of Natriuretic Peptides

Cited by 67 publications

References 26 publications

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

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

Constitutive Activation and Uncoupling of the Atrial Natriuretic Peptide Receptor by Mutations at the Dimer Interface

Atrial Natriuretic Peptide and Other Natriuretic Factors in Cirrhosis

Contact Info

Product

Resources

About