Specific receptors for atriopeptin III in rabbit lung

Olins, Gillian M.; Patton, Dennis R.; Tjoeng, Foe S.; Blehm, Delores J.

doi:10.1016/0006-291x(86)91090-9

Cited by 32 publications

(4 citation statements)

References 14 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Experimental data suggest that ANF can exert pulmonary vasodilating activity. Specific binding sites for ANF have been demonstrated in the lung (19,20) and extraction of circulating ANF occurs during its passage across the lung (21). Moreover, ANF induces relaxation of pulmonary arteries from various animal species, an effect that may result from intracellular cyclic GMP production (22,23).…”

Section: Introductionmentioning

confidence: 99%

Atrial natriuretic factor in chronic obstructive lung disease with pulmonary hypertension. Physiological correlates and response to peptide infusion.

Adnot

Andrivet²,

Chabrier³

et al. 1989

J. Clin. Invest.

View full text Add to dashboard Cite

To investigate the physiological role of atrial natriuretic factor (ANF) in patients with hypoxic pulmonary hypertension secondary to chronic obstructive lung disease (COLD), we infused synthetic a-human ANF in seven such patients, and investigated the physiological correlates to circulating peptide levels in 24 patients with COLD.ANF infusion, at incremental rates of 0.01, 0.03, and 0.1 Mg/kg . min, increased basal plasma immunoreactive (ir) ANF (136±38 pg/ml) by 3-, 10-, and 26-fold, respectively, and reduced pulmonary artery pressure (from 33±3 to 25±2 mmHg, P < 0.001) and systemic arterial pressure (from 88±4 to 79±4 mmHg, P < 0.001) in a dose-related fashion. Cardiac index increased by 13.5% (P < 0.01) while heart rate was unchanged. Cardiac filling pressures decreased at 0.1 Mg/kg min ANF. Pulmonary and systemic vascular resistance fell by 37% (P < 0.001) and 19% (P < 0.001), respectively. Arterial oxygenation was impaired during ANF infusion, suggesting partial reversal of hypoxic pulmonary vasoconstriction. Plasma renin activity remained unchanged but aldosterone fell by 44% (P < 0.01).The levels of plasma irANF in 24 patients correlated directly with the degree of hemoconcentration (r = 0.67, P < 0.001), respiratory acidosis (r = -0.65, P < 0.001), and pulmonary hypertension (r = 0.52, P < 0.01). The results suggest that ANF may serve as a potent pulmonary vasodilator involved in the circulatory homeostasis of patients with COLD.

show abstract

Section: Introductionmentioning

confidence: 99%

Atrial natriuretic factor in chronic obstructive lung disease with pulmonary hypertension. Physiological correlates and response to peptide infusion.

Adnot

Andrivet²,

Chabrier³

et al. 1989

J. Clin. Invest.

View full text Add to dashboard Cite

show abstract

“…Rabbit lung membranes were used to study the competitive binding of atrial natriuretic peptides and were prepared as previously described. 16 The binding assay consisted of 0.25 mL of a solution containing 50 mM Tris pH 7.5, 0.1% bovine serum albumin, 100 µg of membrane protein, and [125I]-ANP-(103-126) (2-3 X 104 cpm) in the absence or presence of unlabeled peptide. The competition experiment was initiated by the addition of membranes and the mixture was incubated at 25 °C for 30 min.…”

Section: Methodsmentioning

confidence: 99%

Identification of structural requirements for analogs of atrial natriuretic peptide (ANP) to discriminate between ANP receptor subtypes

Bovy

O'Neal²,

Olins³

et al. 1989

J. Med. Chem.

Self Cite

View full text Add to dashboard Cite

The structure-activity relationships for affinity and selective binding of atrial natriuretic peptide (ANP) and analogues to guanylate cyclase coupled (CC) and non-cyclase coupled (NC) receptors in rabbit lung membranes are described. We have designed a series of peptides to try to identify the minimal sequence involved in specific recognition of each receptor subtype. The affinity of the peptides was determined from competitive binding experiments. Several peptides derived from the rat ANP sequence, e.g., des-[Phe106, Gly107, Ala115, Gln116]ANP-(103-125)NH2 (4), des-[Cys105,121]ANP-(104-126) (5), and [Acm-Cys105]ANP-(105-114)NH2 (9) have high affinity and selectivity for the noncoupled site. Peptide 4 was the most selective ligand with an affinity superior to that of ANP-(103-126). This compound does not displace the radiolabeled ligand from the guanylate cyclase coupled receptor at the highest concentration tested (100 nM). The structure-activity relationship for affinity and selectivity is discussed. Comparison of the peptide sequences suggests that the structural feature responsible for recognition of the NC site resides in a single sequence of seven contiguous amino acids from the cyclic core of the hormone. The corresponding heptapeptide retains affinity to the guanylate cyclase uncoupled binding site and is proposed to encompass the minimal sequence for specific recognition of the non-guanylate cyclase coupled ANP receptor.

show abstract

“…Receptor-binding properties of atrial peptides were studied by measuring the displacement of lzsI-labelled AP(99-126) from the rabbit lung membrane receptor [15]. Atrial peptides were assayed for vasorelaxant activity using norepinephrine-contracted rabbit thoracic aortic strips [2].…”

Section: Ap Receptor-binding and Bioactivity Assaysmentioning

confidence: 99%

Phosphorylation of high‐ and low‐molecular‐mass atrial natriuretic peptide analogs by cyclic AMP‐dependent protein kinase

Olins¹,

Mehta²,

Blehm³

et al. 1987

FEBS Letters

Self Cite

View full text Add to dashboard Cite

Synthetic high-and low-molecular-mass atrial peptides were phosphorylated in vitro by cyclic AMP-dependent protein kinase and [3zp]ATP. From a series of atrial peptide analogs, it was deduced that the amino acid sequence, Argl°l-Ser TM of atriopeptin was required for optimal phosphorylation. Phosphorylated AP(99-126) was less potent than the parent atriopeptin in vasorelaxant activity and receptor-binding properties. These results indicate that the presence of a phosphate group at the N-terminus of AP(9%126) decreases the interaction of the peptide with its receptor and, as a consequence, decreases bioactivity. These observations are in contrast to those of Rittenhouse et al. [(1986) J. Biol. Chem. 261, 7607 7610] who reported that phosphorylation of AP(101 126) enhanced the stimulation of Na/K/CI cotransport in cultured vascular smooth muscle cells.

show abstract

Specific receptors for atriopeptin III in rabbit lung

Cited by 32 publications

References 14 publications

Atrial natriuretic factor in chronic obstructive lung disease with pulmonary hypertension. Physiological correlates and response to peptide infusion.

Atrial natriuretic factor in chronic obstructive lung disease with pulmonary hypertension. Physiological correlates and response to peptide infusion.

Identification of structural requirements for analogs of atrial natriuretic peptide (ANP) to discriminate between ANP receptor subtypes

Phosphorylation of high‐ and low‐molecular‐mass atrial natriuretic peptide analogs by cyclic AMP‐dependent protein kinase

Contact Info

Product

Resources

About