Next Article in Journal
High Solid Fluorescence of a Pyrazoline Derivative through Hydrogen Bonding
Previous Article in Journal
Upregulation of Melanogenesis and Tyrosinase Activity: Potential Agents for Vitiligo
Article Menu
Issue 8 (August) cover image

Export Article

Open AccessReview
Molecules 2017, 22(8), 1305; doi:10.3390/molecules22081305

Structures and Functions of Snake Venom Metalloproteinases (SVMP) from Protobothrops venom Collected in Japan

Department of Hygienic Chemistry, Meiji Pharmaceutical University, 2-522-1 Noshio, Kiyose-shi, Tokyo 204-8588, Japan
Emeritus Professor.
*
Author to whom correspondence should be addressed.
Received: 26 June 2017 / Accepted: 31 July 2017 / Published: 4 August 2017
(This article belongs to the Section Bioorganic Chemistry)
View Full-Text   |   Download PDF [1422 KB, uploaded 7 August 2017]   |  

Abstract

Snake venom metalloproteinases (SVMP) are widely distributed among the venoms of Crotalinae and Viperidae, and are organized into three classes (P-I, P-II and P-III) according to their size and domain structure. P-I SVMP are the smallest SVMP, as they only have a metalloproteinase (M) domain. P-II SVMP contain a disintegrin-like (D) domain, which is connected by a short spacer region to the carboxyl terminus of the M domain. P-III SVMP contain a cysteine-rich (C) domain, which is attached to the carboxyl terminus of the D domain. Some SVMP exhibit hemorrhagic activity, whereas others do not. In addition, SVMP display fibrinolytic/fibrinogenolytic (FL) activity, and the physiological functions of SVMP are controlled by their structures. Furthermore, these proteinases also demonstrate fibrinogenolytic and proteolytic activity against synthetic substrates for matrix metalloproteinases and ADAM (a disintegrin and metalloproteinase). This article describes the structures and FL, hemorrhagic, and platelet aggregation-inhibiting activity of SVMP derived from Protobothrops snake venom that was collected in Japan. View Full-Text
Keywords: snake venom metalloproteinase; fibrinolytic/fibrinogenolytic activity; hemorrhagic activity; inhibitior of platelet aggregation snake venom metalloproteinase; fibrinolytic/fibrinogenolytic activity; hemorrhagic activity; inhibitior of platelet aggregation
Figures

Figure 1

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

Scifeed alert for new publications

Never miss any articles matching your research from any publisher
  • Get alerts for new papers matching your research
  • Find out the new papers from selected authors
  • Updated daily for 49'000+ journals and 6000+ publishers
  • Define your Scifeed now

SciFeed Share & Cite This Article

MDPI and ACS Style

Oyama, E.; Takahashi, H. Structures and Functions of Snake Venom Metalloproteinases (SVMP) from Protobothrops venom Collected in Japan. Molecules 2017, 22, 1305.

Show more citation formats Show less citations formats

Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Related Articles

Article Metrics

Article Access Statistics

1

Comments

[Return to top]

Molecules EISSN 1420-3049 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top