Expression of prosalusin in human neuroblastoma cells

Nakayama, Chisato; Shichiri, Masayoshi; Sato, Kengo; Hirata, Yukio

doi:10.1016/j.peptides.2009.03.021

Cited by 29 publications

(13 citation statements)

References 15 publications

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“…The sera obtained were transferred to microcentrifuge tubes and stored at -80 • C until analysis. Some studies found an association between the locally reduced synthesis of salusin-␣ in circulation and vascular tissues and atherosclerosis [4].The development of atherosclerosis was accelerated by salusin-␤ and suppressed by salusin-␣ [2]. No.…”

mentioning

confidence: 99%

Serum salusin-α and salusin-β levels in patients with psoriasis

Erden

Uçak

Demir

et al. 2015

European Journal of Dermatology

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mentioning

confidence: 99%

Serum salusin-α and salusin-β levels in patients with psoriasis

Erden

Uçak

Demir

et al. 2015

European Journal of Dermatology

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“…We recently suggested the possible mechanisms responsible for decreased production of salusin- α in atherosclerotic lesions. Salusin- α expression may be inhibited by the activation of Jak-2 kinase, which is expected to be upregulated by angiotensin II, inflammatory cytokines, and growth factors in atherosclerotic and hypertensive diseases [48]. …”

Section: Linkage Of Salusins With Atherosclerotic Cardiovascular mentioning

confidence: 99%

Salusins: Potential Use as a Biomarker for Atherosclerotic Cardiovascular Diseases

Sato

Watanabe

Itoh

et al. 2013

International Journal of Hypertension

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Human salusin-α and salusin-β are related peptides produced from prosalusin. Bolus injection of salusin-β into rats induces more profound hypotension and bradycardia than salusin-α. Central administration of salusin-β increases blood pressure via release of norepinephrine and arginine-vasopressin. Circulating levels of salusin-α and salusin-β are lower in patients with essential hypertension. Salusin-β exerts more potent mitogenic effects on human vascular smooth muscle cells (VSMCs) and fibroblasts than salusin-α. Salusin-β accelerates inflammatory responses in human endothelial cells and monocyte-endothelial adhesion. Human macrophage foam cell formation is stimulated by salusin-β but suppressed by salusin-α. Chronic salusin-β infusion into apolipoprotein E-deficient mice enhances atherosclerotic lesions; salusin-α infusion reduces lesions. Salusin-β is expressed in proliferative neointimal lesions of porcine coronary arteries after stenting. Salusin-α and salusin-β immunoreactivity have been detected in human coronary atherosclerotic plaques, with dominance of salusin-β in macrophage foam cells, VSMCs, and fibroblasts. Circulating salusin-β levels increase and salusin-α levels decrease in patients with coronary artery disease. These findings suggest that salusin-β and salusin-α may contribute to proatherogenesis and antiatherogenesis, respectively. Increased salusin-β and/or decreased salusin-α levels in circulating blood and vascular tissue are closely linked with atherosclerosis. Salusin-α and salusin-β could be candidate biomarkers and therapeutic targets for atherosclerotic cardiovascular diseases.

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“…Both of these peptides are produced from the same precursor preprosalusin, which is a product of the torsion dystonia‐related gene (TOR2A) after alternative splicing (Shichiri et al, ). Salusins have been proven to be distributed widely in many humans and rat tissue types such as the cardiovascular system, central nervous system (CNS), lung, and kidney, as well as in human bodily fluids such as plasma and urine (Citil et al, ; Nakayama, Shichiri, Sato, & Hirata, ; Sahin & Aydin, ; Sato, Sato, Susumu, Koyama, & Shichiri, ; Suzuki et al, ; Suzuki, Shichiri, Tateno, Sato, & Hirata, ). Previous studies show that salusins exert multiple cardiovascular effects including hypotension, bradycardia (Izumiyama et al, ), inhibition of myocardial contraction (Izumiyama et al, ), reduction of cardiac ischemic injury (Masumura et al, ), promotion of cardiomyocyte hypertrophy (Yu et al, ) and proliferation of vascular smooth muscle cells (Xu et al, ).…”

Section: Introductionmentioning

confidence: 99%

The cardiovascular functions of salusin‐β mediated by muscarinic receptors, glutamate receptors or L‐type calcium channels within the rostral ventrolateral medulla of rats

Xie

Chai

Zhu

et al. 2017

Microscopy Res & Technique

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Salusin-α and salusin-β are newly identified bioactive peptides of 28 and 20 amino acids, respectively, that were initially predicted using in silico analyses and are widely distributed in the endocrine system, hematopoietic system, and central nervous system. The goal of our study was to investigate the cardiovascular effect of salusin-β microinjections into the rostral ventrolateral medulla (RVLM) in anesthetized rats and study their mechanism of action. Microinjection of the artificial cerebrospinal fluid (aCSF) into the RVLM did not affect the blood pressure (BP) or heart rate (HR) in anesthetized rats. Topical application of salusin-β into the RVLM produced a dose-dependently increase of BP in anesthetized rats. Microinjection of higher dose salusin-β produced significant tachycardia. Prior application of the L-NAME into the RVLM of rats did not alter the hypertension and tachycardia induced by intra-RVLM salusin-β. Notable, the cardiovascular functions elicited by intra-RVLM salusin-β were significantly decreased by pretreatment with Nic, KYN and atropine. In conclusion, the present study shows that the hypertension and tachycardia induced by intra-RVLM salusin-β might be partly mediated, at least in our opinion, by muscarinic receptors, glutamate receptors or L-type calcium channels.

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Expression of prosalusin in human neuroblastoma cells

Cited by 29 publications

References 15 publications

Serum salusin-α and salusin-β levels in patients with psoriasis

Serum salusin-α and salusin-β levels in patients with psoriasis

Salusins: Potential Use as a Biomarker for Atherosclerotic Cardiovascular Diseases

The cardiovascular functions of salusin‐β mediated by muscarinic receptors, glutamate receptors or L‐type calcium channels within the rostral ventrolateral medulla of rats

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