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Cited by 24Nitric Oxide and Endothelin EffectsCardiovascular, Neuropeptides, and Oxidative Stress ResearchNeuropeptides and Animal Physiology

The DOI matches its Crossref record; 23 of the 23 references it cites were found in a registry or an index.

Novel properties of peptides derived from the sequence coded by exon 26A of human elastin

Ostuni, A, Lograno, M.D, Gasbarro, A.R, Bisaccia, F, Tamburro, A.M·2002·The International Journal of Biochemistry & Cell Biology

Abstract

The exon 26A is a rarely expressed human elastin exon that codes for a hydrophilic and charged amino acid sequence. The functional role of elastin containing this additional sequence is unknown. The present investigation was aimed to determine the effect of synthetic peptides derived from this exon on the vascular tone of rat thoracic aorta. On phenilephrine-preconstricted rat thoracic aortic rings the peptides LSPELREGD and REGD cause dose-dependent relaxation in the concentration range from 10(-9) to 10(-5) M. omega-nitro-L-arginine methyl ester, a known inhibitor of the NO synthase, highly inhibits, although to a different extent, the relaxation induced by these peptides. Removal of endothelium and blocking of ATP-sensitive potassium channels by glibenclamide significantly inhibited the vasorelaxant activity of LSPELREGD but not that of REGD, suggesting a different mechanism of action and possibly a different receptor.

Overview

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Crossref · 10.1016/s1357-2725(01)00115-7

Cites

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Research works printed but not linked: 1

  1. M.J. Liptay, M.D. Botney, R.P. Mecham, J. Rosenbloom, J.D. Cooper, L.R. Kaiser, Surgical Forum, vol. XLII, reprinted from American College of Surgeons, 1991, pp. 287–289.

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Metadata

Authors
Ostuni, A., Lograno, M. D., Gasbarro, A. R., Bisaccia, F., & Tamburro, A. M.
Affiliations
  • University of Basilicata (IT)
  • University of Bari Aldo Moro (IT)
Venue
The International Journal of Biochemistry & Cell Biology
Publisher
Elsevier BV
Published
2002-02
Volume
34
Issue
2
Pages
130-135
ISSN
1357-2725 (ISSN-L)
OpenAlex
W1967409427
Cited by
21
References
23
Citations by year
2021: 1 · 2019: 1 · 2016: 1 · 2014: 1 · 2012: 1
FWCI
1.20
Type
journal article
Language
en
Open access
closed
Licence
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations
  • The International Journal of Biochemistry & Cell Biology (publishedVersion)
  • PubMed (publishedVersion)
  • CINECA IRIS Institutional Research Information System (University of Basilicata) (submittedVersion)
Topics
  • Health Sciences › Medicine › Physiology (medical) › Nitric Oxide and Endothelin Effects
  • Health Sciences › Medicine › Surgery › Cardiovascular, Neuropeptides, and Oxidative Stress Research
  • Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuropeptides and Animal Physiology
Keywords
elastin peptides, vasorelaxation, thoracic aorta, nitric oxide, nitric oxide synthase inhibition, ATP-sensitive potassium channels, glibenclamide, endothelium, peptide receptors
MeSH terms
Animals, Aorta, Dose-Response Relationship, Drug, Elastin, Enzyme Inhibitors, Exons, Glyburide, Humans, Hypoglycemic Agents, Lactose, Male, Models, Biological, Muscle, Smooth, Vascular, Peptides, Virulence Factors, Bordetella, Phenylephrine, Tolbutamide, Vasoconstrictor Agents, 4-Aminopyridine, Rats, Wistar, Nitroarginine, Potassium Channel Blockers, Rats, In Vitro Techniques

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CoChat. (2026). Citation check: Novel properties of peptides derived from the sequence coded by exon 26A of human elastin. https://app.cochat.ai/papers/10.1016/s1357-2725(01)00115-7
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Ostuni, A., Lograno, M. D., Gasbarro, A. R., Bisaccia, F., & Tamburro, A. M. (2002). Novel properties of peptides derived from the sequence coded by exon 26A of human elastin. The International Journal of Biochemistry & Cell Biology. https://doi.org/10.1016/s1357-2725(01)00115-7

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.