Special Issue "Disintegrins: Structure-Function and Translational Potential"

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A special issue of Toxins (ISSN 2072-6651).

Deadline for manuscript submissions: closed (31 August 2011)

Special Issue Editors

Guest Editor
Dr. Frank S. Markland
Department of Biochemistry and Molecular Biology and Comprehensive Cancer, Center, University of Southern California, Keck School of Medicine, Cancer Research Laboratory #106, 1303 N. Mission Road, Los Angeles, CA 90033, USA
Website: http://www.usc.edu/schools/medicine/util/directories/faculty/profile.php?PersonIs_ID=735
E-Mail: markland@usc.edu
Phone: +1 323 224 7981
Fax: +1 323 224 7679
Interests: protein chemistry and structure/ function interrelationships; snake venom components with procoagulant and anticoagulant activities; snake venom platelet aggregation inhibitors (disintegrins); disintegrins as anti-angiogenic agents; disintegrins and wound healing; novel fibrinolytic agents (structure and modeling); thrombolytic therapy

Guest Editor
Dr. Steve Swenson
University of Southern California, Keck School of Medicine, Cancer Research Laboratory, 1303 N. Mission Road, Los Angeles, CA 90033, USA
Website: http://www.usc.edu/schools/medicine/util/directories/faculty/profile.php?PersonIs_ID=3152
E-Mail: sswenson@usc.edu
Phone: +1 323 224-5124
Fax: +1 323 224 7679

Guest Editor
Dr. Radu Minea
Department of Biochemistry and Molecular Biology, University of Southern California, Keck School of Medicine, USA
E-Mail: minea@usc.edu

Special Issue Information

Dear Colleagues,

Disintegrins are interesting molecules isolated as soluble proteins from snake venom. They are isolated from venom of different species in a variety of forms varying from short to medium to long polypeptide chains of approximately 49, 67 and 84 amino acids, respectively. Additionally, they are also found as homodimers or heterodimers with two identical or dissimilar chains, respectively, held together by two disulfide bonds. The structure of several disintegrins has been determined by solution NMR or X-ray crystallography. Interestingly, structural determination of one homodimeric disintegrin revealed that the two Arg-Gly-Asp (RGD) motifs on the individual chains are separated by 69Ǻ. In the monomeric and dimeric disintegrins the RGD motif is exposed in a 13 amino acid flexible loop that enables the disintegrins to bind with high affinity to integrins.

Disintegrins have interesting antagonist/agonist activity towards integrins and this has been taken advantage of in developing anti-tumor and anti-angiogenic strategies for the use of disintegrins. In animal models of breast, ovarian and prostate cancer and glioma, disintegrins have shown portent anti-tumor activity and studies are also underway to use disintegrins as imaging agents for cancer diagnostic purposes as well.

Another class of disintegrin-containing proteins is the ADAM (A Disintegrin And Metalloproteinase) family. These proteins, which represent the only mammalian proteins known to contain a disintegrin domain, are transmembrane proteins. The extracellular disintegrin domain may bind to integrins to facilitate metalloproteinase catalyzed events.

Dr. Frank S. Markland
Dr. Radu Minea
Dr. Steve Swenson
Guest Editors

Keywords

  • cancer
  • angiogenesis
  • snake venom
  • ADAM
  • integrin
  • disintegrin
  • signal transduction pathways
  • clinical translation

Published Papers (3 papers)

by ,  and
Toxins 2012, 4(5), 296-322; doi:10.3390/toxins4050296
Received: 23 February 2012; in revised form: 12 April 2012 / Accepted: 13 April 2012 / Published: 26 April 2012
Show/Hide Abstract | Cited by 2 | PDF Full-text (2578 KB) | HTML Full-text | XML Full-text | Supplementary Files

by , ,  and
Toxins 2010, 2(11), 2606-2621; doi:10.3390/toxins2112606
Received: 24 August 2010; in revised form: 15 October 2010 / Accepted: 18 October 2010 / Published: 29 October 2010
Show/Hide Abstract | Cited by 5 | PDF Full-text (282 KB) | HTML Full-text | XML Full-text

by , ,  and
Toxins 2010, 2(10), 2411-2427; doi:10.3390/toxins2102411
Received: 30 August 2010; in revised form: 13 October 2010 / Accepted: 18 October 2010 / Published: 19 October 2010
Show/Hide Abstract | Cited by 1 | PDF Full-text (827 KB) | HTML Full-text | XML Full-text

Last update: 5 March 2014

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