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Identification of novel short peptides derived from the alpha 4, alpha 5, and alpha 6 fibrils of type IV collagen with anti-angiogenic properties.
Biochem Biophys Res Commun. 2007 Mar 09; 354(2):434-9.BB

Abstract

Angiogenesis, or neovascularization, is tightly controlled by positive and negative regulators, many of which reside in the extracellular matrix. We have now identified eight novel 19- to 20-residue peptides derived from the alpha4, alpha5, and alpha6 fibrils of type IV collagen, which we have designated tetrastatins, pentastatins, and hexastatins, respectively. We have shown that these endogenous peptides suppress the proliferation and migration of HUVECs in vitro. By performing clustering analyses of the sequences using sequence similarity criteria and of the experimental results using a hierarchical algorithm, we report that the clusters identified by the experimental results coincide with the sequence-based clusters, indicating a tight relationship between peptide sequence and anti-angiogenic potency. These peptides may have potential as anti-angiogenic therapeutic agents.

Authors+Show Affiliations

Department of Biomedical Engineering, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA. ekaragi1@jhmi.eduNo affiliation info available

Pub Type(s)

Journal Article
Research Support, N.I.H., Extramural

Language

eng

PubMed ID

17239819

Citation

Karagiannis, Emmanouil D., and Aleksander S. Popel. "Identification of Novel Short Peptides Derived From the Alpha 4, Alpha 5, and Alpha 6 Fibrils of Type IV Collagen With Anti-angiogenic Properties." Biochemical and Biophysical Research Communications, vol. 354, no. 2, 2007, pp. 434-9.
Karagiannis ED, Popel AS. Identification of novel short peptides derived from the alpha 4, alpha 5, and alpha 6 fibrils of type IV collagen with anti-angiogenic properties. Biochem Biophys Res Commun. 2007;354(2):434-9.
Karagiannis, E. D., & Popel, A. S. (2007). Identification of novel short peptides derived from the alpha 4, alpha 5, and alpha 6 fibrils of type IV collagen with anti-angiogenic properties. Biochemical and Biophysical Research Communications, 354(2), 434-9.
Karagiannis ED, Popel AS. Identification of Novel Short Peptides Derived From the Alpha 4, Alpha 5, and Alpha 6 Fibrils of Type IV Collagen With Anti-angiogenic Properties. Biochem Biophys Res Commun. 2007 Mar 9;354(2):434-9. PubMed PMID: 17239819.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Identification of novel short peptides derived from the alpha 4, alpha 5, and alpha 6 fibrils of type IV collagen with anti-angiogenic properties. AU - Karagiannis,Emmanouil D, AU - Popel,Aleksander S, Y1 - 2007/01/16/ PY - 2006/12/26/received PY - 2006/12/29/accepted PY - 2007/1/24/pubmed PY - 2007/4/11/medline PY - 2007/1/24/entrez SP - 434 EP - 9 JF - Biochemical and biophysical research communications JO - Biochem Biophys Res Commun VL - 354 IS - 2 N2 - Angiogenesis, or neovascularization, is tightly controlled by positive and negative regulators, many of which reside in the extracellular matrix. We have now identified eight novel 19- to 20-residue peptides derived from the alpha4, alpha5, and alpha6 fibrils of type IV collagen, which we have designated tetrastatins, pentastatins, and hexastatins, respectively. We have shown that these endogenous peptides suppress the proliferation and migration of HUVECs in vitro. By performing clustering analyses of the sequences using sequence similarity criteria and of the experimental results using a hierarchical algorithm, we report that the clusters identified by the experimental results coincide with the sequence-based clusters, indicating a tight relationship between peptide sequence and anti-angiogenic potency. These peptides may have potential as anti-angiogenic therapeutic agents. SN - 0006-291X UR - https://www.unboundmedicine.com/medline/citation/17239819/ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0006-291X(06)02889-0 DB - PRIME DP - Unbound Medicine ER -