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

Guest Editor
Dr. Frank S. Markland
Biochemistry and Molecular Biology, 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:
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. Radu Minea
Department of Biochemistry and Molecular Biology, University of Southern California, Keck School of Medicine, USA
E-Mail:

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:

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.

Frank S. Markland, Ph. D.
Steve Swenson, Ph. D.
Guest Editors

Submission

All manuscripts should be submitted to toxins@mdpi.org with a copy to the Guest Editor. Manuscripts can be submitted until the deadline. Papers will be published continuously (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are refereed through a peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Toxins is an international peer-reviewed Open Access monthly journal published by MDPI.

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