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
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
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“When inserted into the final transcript, exon 26A produces an increase of 99 base pairs, which code for 33 amino acids (GADEGVRRSLSPELREGDPSSSQHLPSTPSSPR) in the tropoelastin protein sequence (Fig. 3) and alter its structural and biological properties [37, 64, 65].”
From Elastin structure and its involvement in skin photoageing (2017) · cites this paper as [65]
Citations
Cites
Furchgott, R. F., & Zawadzki, J. V. (1980) · Nature · doi:10.1038/288373a0 · Cited by 12,064
Senior, R. M., Griffin, G. L., Mecham, R. P., Wrenn, D. S., Prasad, K. U., & Urry, D. W. (1984) · The Journal of cell biology · doi:10.1083/jcb.99.3.870 · Cited by 408
Indik, Z., Yeh, H., Ornstein-Goldstein, N., Sheppard, P., Anderson, N., Rosenbloom, J. C., Peltonen, L., & Rosenbloom, J. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.16.5680 · Cited by 334
The Elastin Receptor: A Galactoside-Binding Protein
Hinek, A., Wrenn, D. S., Mecham, R. P., & Barondes, S. H. (1988) · Science · doi:10.1126/science.2832941 · Cited by 316
Elastin Fragments Attract Macrophage Precursors to Diseased Sites in Pulmonary Emphysema
Hunninghake, G. W., Davidson, J. M., Rennard, S. I., Szapiel, S. V., Gadek, J. E., & Crystal, R. G. (1981) · Science · doi:10.1126/science.7233186 · Cited by 215
cAMP-Independent Dilation of Coronary Arterioles to Adenosine
Hein, T. W., & Kuo, L. (1999) · Circulation Research · doi:10.1161/01.res.85.7.634 · Cited by 199
Elastin binds to a multifunctional 67-kilodalton peripheral membrane protein
Mecham, R. P., Hinek, A., Entwistle, R. L., Wrenn, D. S., Griffin, G. L., & Senior, R. M. (1989) · Biochemistry · doi:10.1021/bi00435a014 · Cited by 194
Regulation and Functional Consequences of Endothelial Nitric Oxide Formation
Busse, R., & Fleming, I. (1995) · Annals of Medicine · doi:10.3109/07853899509002586 · Cited by 166
Oxidation, cross-linking, and insolubilization of recombinant tropoelastin by purified lysyl oxidase
Bedell-Hogan, D., Trackman, P. C., Abrams, W. R., Rosenbloom, J., & Kagan, H. M. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)82207-4 · Cited by 152
Wu, W. J., Vrhovski, B., & Weiss, A. S. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.31.21719 · Cited by 150
Research works printed but not linked: 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.
Cited by
Elastin as a biomaterial for tissue engineering
Daamen, W. F., Veerkamp, J. H., van Hest, J. C. M., & van Kuppevelt, T. H. (2007) · Biomaterials · doi:10.1016/j.biomaterials.2007.06.025 · Cited by 528
Biomimetic Scaffolds for Tissue Engineering
Kim, T. G., Shin, H., & Lim, D. W. (2012) · Advanced Functional Materials · doi:10.1002/adfm.201103083 · Cited by 459
Holst, J., Watson, S., Lord, M. S., Eamegdool, S. S., Bax, D. V., Nivison-Smith, L. B., Kondyurin, A., Ma, L., Oberhauser, A. F., Weiss, A. S., et al. (2010) · Nature Biotechnology · doi:10.1038/nbt.1687 · Cited by 273
Duca, L., Floquet, N., Alix, A. J. P., Haye, B., & Debelle, L. (2004) · Critical Reviews in Oncology/Hematology · doi:10.1016/j.critrevonc.2003.09.007 · Cited by 245
Mithieux, S. M., Rasko, J. E. J., & Weiss, A. S. (2004) · Biomaterials · doi:10.1016/j.biomaterials.2004.01.055 · Cited by 244
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)
- ORCID
- 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
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
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.
