Synthesis and biological properties of two dimeric forms of human α‐atrial natriuretic peptide

Kambayashi, Yoshikazu; Kawabata, Tomoji; Hara, Shinji; Yamauchi, Akira; Ueda, Akira; Kono, Michihito; Doteuchi, Masami; Nakamura, Masuhisa; Inouye, Ken

doi:10.1016/0014-5793(86)81003-1

Cited by 16 publications

(12 citation statements)

References 18 publications

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“…It has recently been shown that synthetic phANP, an antiparallel dimer of cu-hANP, has biological properties similar to natural ,&hANP [4,5]. The present study first demonstrates that synthetic &hANP binds to cultured rat VSMCs in the same manner as a-hANP in terms of time-and temperature-dependency.…”

Section: Discussionsupporting

confidence: 62%

“…Division, National Cardiovascular Center Research Institute, S&a, Osaka 565, Japan been synthesized and its biological activity has been determined [4,5]. Interestingly, natural [2] as well as synthetic fi-hANP [4,5] exhibits a slower onset and longer duration of action than a-hANP, the mechanism of which remains obscure.…”

Section: Hypertensionendocrinementioning

confidence: 99%

“…Interestingly, natural [2] as well as synthetic fi-hANP [4,5] exhibits a slower onset and longer duration of action than a-hANP, the mechanism of which remains obscure. Using cultured rat vascular smooth muscle cells (VSMCs) which have specific receptors for ANP functionally coupled to the guanylate cyclase system [6], we have clarified the cellular mechanism of binding, internalization and degradation of a-rat (r) ANP [7].…”

Section: Hypertensionendocrinementioning

confidence: 99%

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Binding of synthetic β‐human atrial natriuretic peptide to cultured rat vascular smooth muscle cells

et al. 1987

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We have studied the effects of synthetic p-human atria1 natriuretic peptide (j?-hANP), an antiparallel dimer of a-hANP, on receptor binding and cGMP generation in cultured rat vascular smooth muscle cells and compared the effects with those of a-hANP. Characteristics of temperature-dependent binding and degradation of 1Z51-~-hANP were similar to those of lZSI-a-hANP. Scatchard analysis indicated a single class of binding sites for b-hANP with a maximal binding capacity one-half that of a-hANP. Parallel and antiparallel dimers were equipotent in inhibiting the binding and stimulating intracellular cGMP formation, of which the maximal effect was about one-half that of a-hANP. Reverse-phase high performance liquid chromatography revealed that most of b-hANP added to cells was converted to a small molecular mass component corresponding to a-hANP after incubation. These data suggest that the less potent effect of p-hANP in receptor binding and cGMP generation may be partly accounted for by the possible conversion of /J-hANP to a-hANP at the site of target cells.

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Section: Discussionsupporting

confidence: 62%

Section: Hypertensionendocrinementioning

confidence: 99%

Section: Hypertensionendocrinementioning

confidence: 99%

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Binding of synthetic β‐human atrial natriuretic peptide to cultured rat vascular smooth muscle cells

et al. 1987

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“…Although the characteristic pattern of action of ,&ANP in vasorelaxation and natriuresis [2,3] may be explained, at least in part, by the slow conversion of ,&ANP into a-ANP in human plasma or at target tissues [5-7,161, it has been a matter of controversy as to whether fl-ANP itself is biologically active. The present investigation has also shown that ,&ANP inhibits the a-ANP-induced production of intracellular cGMP in cultured VSMC with an apparent ICSO value of 2.13 x lo-' M, which is about one-third that of analog III and this ratio is comparable to that one between the 1% values of &ANP and analog III for receptor binding.…”

Section: Discussionmentioning

confidence: 99%

“…Human cu-ANP and &ANP [3] were synthesized by solution methods in these laboratories. '251-labeled human (u-ANP (1800 Ci/mmol) was purchased from Amersham and aminopeptidase M from Pierce.…”

Section: Methodsmentioning

confidence: 99%

A dicarba analog of β‐atrial natriuretic peptide (β‐ANP) inhibits guanosine 3′,5′‐cyclic monophosphate production induced by α‐ANP in cultured rat vascular smooth muscle cells

et al. 1989

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The synthesis and biological properties are described of [As~'~~']-/l-ANP-(7-28) (Asu, L-a-aminosuberic acid), a dicarba analog of p-atria1 natriuretic peptide (8-ANP, an antiparallel dimer of human a-ANP with the chains linked by 7-23' and 7-23 disulfide bonds). This Asu-analog (referred to as analog III) displaced 12SI-a-ANP specifically bound to cultured rat vascular smooth muscle cells (VSMC) with an apparent Ki of 2.1 x 10-s M, but did not stimulate formation of intracellular cGMP at 10-8-10-5 M. Analog III inhibited the a-ANP-stimulated cGMP production in VSMC competitively with a pA, value of 7.45 and behaved as an antagonist of a-ANP in rat aorta smooth muscle relaxation. In addition, /I-ANP was also shown to inhibit the a-ANP-induced cGMP production in a dose-dependent manner. The mechanism of action of /I-ANP is also discussed.Atria1 natriuretic peptide analog; Atria1 natriuretic peptide receptor antagonist; Receptor binding; cyclic GMP production; Vasorelaxation; (Cultured vascular smoothmuscle cell)

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Direct measurement of α‐human atrial natriuretic polypeptide in plasma by sensitive enzyme immunoassay

Hashida

Ishikawa

Mukoyama

et al. 1988

Clinical Laboratory Analysis

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a-Human atrial natriuretic polypeptide (a-was 30-90 fg (10-30 attomo1es)ltube and hANP) in plasma was directly measured 0.6-2.3 ng (0.2-0.75 pmol)/L using 0.04-without extraction by sensitive sandwich 0.05 ml of plasma. The lower detection enzyme immunoassay. Polystyrene balls limit was obtained using monoclonal antiwere coated with monoclonal anti-a-hANP a-hANP (ring) IgG,. Plasma hANP levels (ring) lgG, specific for the N-terminal half of healthy men in a supine position after of the ring structure including Met-12 resi-an overnight fast were 24.5 f 13.2 (SD) due of a-hANP or monoclonal anti-a-hANP nglL and tended to decrease (15.3 f 8.5 (N-terminus) lgG, specific for the N-termi-[SD] ng/L) after intravenous administration nus of a-hANP. Rabbit anti-a-hANP (C-ter-of furosemide and subsequent one hour minus) Fab' specific for the C-terminus of walking. The present sandwich enzyme a-hANP was conjugated to horseradish immunoassay could be modified further to peroxidase. The polystyrene ball was in-improve the detection limit of plasma 01-cubated with a-hANP standards or plasma hANP (0.2 nglL) or to perform a less timeand, after washing, with the conjugate, and consuming one-step sandwich enzyme imbound peroxidase activity was assayed by munoassay without much loss of the fluorimetry (two-step sandwich enzyme im-sensitivity. munoassay). The detection limit of a-hANP

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Synthesis and biological properties of two dimeric forms of human α‐atrial natriuretic peptide

Cited by 16 publications

References 18 publications

Binding of synthetic β‐human atrial natriuretic peptide to cultured rat vascular smooth muscle cells

Binding of synthetic β‐human atrial natriuretic peptide to cultured rat vascular smooth muscle cells

A dicarba analog of β‐atrial natriuretic peptide (β‐ANP) inhibits guanosine 3′,5′‐cyclic monophosphate production induced by α‐ANP in cultured rat vascular smooth muscle cells

Direct measurement of α‐human atrial natriuretic polypeptide in plasma by sensitive enzyme immunoassay

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