Neuropeptide Y (NPY) reduces myocardial perfusion and inhibits the force of contraction of the isolated perfused rabbit heart

Allen, Janet M.; Bircham, P. M. M.; Edwards, A V; Tatemoto, Kazuhiko; Bloom, S.R.

doi:10.1016/0167-0115(83)90143-x

Cited by 170 publications

(34 citation statements)

References 7 publications

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“…22,43 In the isolated rabbit heart, NPY has been reported to reduce myocardial perfusion together with the force of contraction. 44,45 Other studies failed how ever to detect a direct action of NPY on the heart mus cle. 46,47 The most striking cardiac effects of NPY ob served using in vitro preparations appear to be a prejunctional suppression of stimulated norepinephrine release 47 and a contraction of the coronary vascular bed.…”

Section: Effects Of Npy In the Isolated Heart And Cultured Atrial Cellsmentioning

confidence: 99%

Cardiovascular Effects of Neuropeptide Y

Waeber

Aubert

Corder

et al. 1988

American Journal of Hypertension

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Neuropeptide Y (NPY) is present in the brain, the adrenal medulla, and peripheral sympathetic nerves. This peptide is released together with catecholamines during sympathoadrenal activation. It possesses direct vasoconstrictor properties that are not dependent on simultaneous adrenergic activation. Moreover, it potentiates the vascular effect of several stimulatory substances and may contribute to the modulation of blood pressure responsiveness under a number of circumstances. NPY may alsoN europeptide Y (NPY) is a 36 amino acid peptide first isolated from porcine brain.1,2 It has been found to be widely distributed throughout the central and peripheral nervous system of a variety of mammals including man (for review see references 3-6). This peptide is co-stored with norepinephrine in perivascular nerve fibers. It has also been localized to the adrenal medulla. NPY has been shown to induce vasoconstriction through a direct effect. In addition, it has been recognized to potentiate the contractile response evoked by stimulation of aadrenoceptors.The vasoactive properties of NPY have been extensively studied during the last few years. In the present work, we intend to focus on the evidence suggesting a role for this newly discovered peptide in the regulation of vascular tone. be indirectly involved in the control of blood pressure through regulating the release of hormones with well-established actions on the cardiovascular system. Am J Hypertens 1988;1:193-199 KEY WORDS: Neuropeptide Y, sympathetic nervous system, catecholamines, renin-angiotensin system, blood pressure taining neurons located in areas physiologically involved in the regulation of the cardiovascular system, particularly at the level of the nucleus tractus solitarius. CARDIOVASCULAR EFFECTS OF NPY7 ' 8 One group of investigators has shown that intraventricular administration of NPY causes in conscious as well as in anesthetized rats a hypotension accompanied by a bradycardia. 9,10 This type of hemodynamic response corresponds to what is expected to occur after central injection of a 2 -adrenergic agonists. It is therefore of interest that brain o^-adrenergic binding sites have been reported to increase in the presence of NPY.11 It has been suggested that NPY stimulates presynaptic receptors on norepinephrine and/or epinephrine nerve terminals, which may enhance the presynaptic û^-adrenoceptor function to inhibit norepinephrine release.12 The hypotension and bradycardia induced by intracisternal and intraventricular administration of NPY has however not been observed by all investigators. 1314NPY may even be responsible in rats for a dose-dependent pressor response and a tachycardia.14 Such effects could be prevented by pretreating intravenously with a-and /^-adrenoceptor blocking agents, suggesting that the cardiovascular response to centrally administered NPY is mediated by an activation of the sympathetic nervous system. Microinjection of NPY at a large dose into the nucleus tractus solitarius of rats decreases blood pressure and heart rate,...

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Section: Effects Of Npy In the Isolated Heart And Cultured Atrial Cellsmentioning

confidence: 99%

Cardiovascular Effects of Neuropeptide Y

Waeber

Aubert

Corder

et al. 1988

American Journal of Hypertension

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“…Central administration has implicated NPY in the control of feeding (9,10) and in secretion of gonadotrophin-releasing hormone secretion (11). Peripheral administration of NPY induces vasoconstriction in many vascular beds (12)(13)(14) and potentiates catecholamine-induced vascular smooth muscle contraction in vitro (15). NPY may play a role in degenerative diseases such as Alzheimer's disease (16).…”

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confidence: 99%

Molecular structure of mammalian neuropeptide Y: analysis by molecular cloning and computer-aided comparison with crystal structure of avian homologue.

Allen¹,

Novotný²,

Martin³

et al. 1987

Proc. Natl. Acad. Sci. U.S.A.

163

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Identification and characterization of the cDNA encoding rat neuropeptide Y revealed the nucleotide sequence coding for a 98-amino acid precursor. The deduced amino acid sequence for rat neuropeptide Y is identical to the human peptide and is highly homologous to avian pancreatic polypeptide. The tertiary structure of avian pancreatic polypeptide has been previously derived from crystallographic data by Blundell and coworkers. The homology between neuropeptide Y and avian pancreatic polypeptide preserves all of the residues essential for the maintenance of the tertiary structure. Thus, it has been possible to compute a three-dimensional model of the mammalian neuropeptide, neuropeptide Y, based on the known structure of the avian homologue. This model suggests that neuropeptide preserves a compact tertiary structure characterized by extensive hydrophobic interactions between an N-terminal polyproline-II-like helix and a C-terminal a-helix. The model has been used to identify amino acids residing in key positions within this structure and, thereby, to direct future analysis of neuropeptide Y structure-function relationships.Neurons produce a variety of peptides that are secreted from axons and dendrites and are collectively known as neuropeptides. These peptides arise from larger precursors that are processed enzymatically to yield the mature neuropeptides (1). Neuropeptides are believed to serve as neurotransmitters and neuromodulators (2) by their interaction with specific cell membrane receptors after secretion and have been implicated in the control of behavior and autonomic and motor functions.Understanding the synthesis and secretion of neuropeptides and their mechanism of action requires detailed knowledge of the molecular structure of neuropeptides and neuropeptide precursors. To gain such knowledge, we have combined the methods of molecular cloning of cDNAs complementary to specific mRNAs with computer-aided molecular modeling to deduce both the primary and tertiary structures of the mammalian neuropeptide "neuropeptide Y" (NPY). This neuropeptide was originally identified by chemical means and subsequently purified from porcine brain (3, 4). NPY is widely distributed throughout the mammalian central (5, 6) and peripheral nervous systems (7,8). Central administration has implicated NPY in the control of feeding (9, 10) and in secretion of gonadotrophin-releasing hormone secretion (11). Peripheral administration of NPY induces vasoconstriction in many vascular beds (12-14) and potentiates catecholamine-induced vascular smooth muscle contraction in vitro (15). NPY may play a role in degenerative diseases such as Alzheimer's disease (16). The structure of the precursor of human NPY was recently determined by molecular cloning methods (17).NPY is a member of a larger family that includes the pancreatic polypeptide (18) and peptide YY (19) ( Table 1). In particular, NPY is highly homologous in amino acid sequence to avian pancreatic polypeptide (APP), these two having 19 of the total 36 amino acids in...

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“…The vasoconstrictor action of NPY is resistance to adrenoceptor blocking agents in vivo and in vitro. The prolonged vasoconstrictor action of NPY is associated with a reduction in the force of cardiac contraction [24], and these responses could not be dissociated.…”

Section: Neuropeptide Ymentioning

confidence: 99%

Distribution of Calcitonin Gene-Related Peptide, Atrial Natriuretic Peptide and Neuropeptide Y in the Rat Heart

Onuoha

Ritchie²,

Nicholls³

1998

Cardiology

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Calcitonin gene-related peptide (CGRP) is a novel neuropeptide, predicted on the basis of structural analysis of the rat calcitonin gene. It is a neurotransmitter which has been suggested to take part in sensory transmission. In this study, we have examined the distribution of this peptide, α-atrial natriuretic peptide immunoreactivity (irANP) and neuropeptide Y (NPY) within different regions of the rat heart. Attempts were also made to compare the distributions of these peptides in the regions examined, through different methods of immunocytochemistry and further comparing these results with those obtained through radioimmunoassay. The distributions of the peptides in the atria were similar to results obtained with radioimmunoassay, but there were no myocytes containing irANP in the ventricles with immunocytochemistry as opposed to radioimmunoassay. While the staining obtained for irANP in the atrium was more intense in the right, CGRP and NPY nerve fibres were two to three times more abundant in the left atrium. The high local concentration of a vasoconstrictor peptide in the region of coronary vessels may suggest that it is involved in the control of vascular smooth muscle tone. The method of choice with the immunocytochemical studies was that of the susa wax technique for irANP. Caution should therefore be observed when interpreting results based only on a single staining technique.

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Neuropeptide Y (NPY) reduces myocardial perfusion and inhibits the force of contraction of the isolated perfused rabbit heart

Cited by 170 publications

References 7 publications

Cardiovascular Effects of Neuropeptide Y

Cardiovascular Effects of Neuropeptide Y

Molecular structure of mammalian neuropeptide Y: analysis by molecular cloning and computer-aided comparison with crystal structure of avian homologue.

Distribution of Calcitonin Gene-Related Peptide, Atrial Natriuretic Peptide and Neuropeptide Y in the Rat Heart

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