Arthropod venom Hyaluronidases: biochemical properties and potential applications in medicine and biotechnology
J. venom. anim. toxins incl. trop. dis
; 21: 1-12, 31/03/2015. ilus, tab
Article
in English
| LILACS, VETINDEX
| ID: biblio-1484615
Responsible library:
BR68.1
Localization: BR68.1
ABSTRACT
Hyaluronidases are enzymes that mainly degrade hyaluronan, the major glycosaminoglycan of the interstitial matrix. They are involved in several pathological and physiological activities including fertilization, wound healing, embryogenesis, angiogenesis, diffusion of toxins and drugs, metastasis, pneumonia, sepsis, bacteremia, meningitis, inflammation and allergy, among others. Hyaluronidases are widely distributed in nature and the enzymes from mammalian spermatozoa, lysosomes and animal venoms belong to the subclass EC 3.2.1.35. To date, only five three-dimensional structures for arthropod venom hyaluronidases (Apis mellifera and Vespula vulgaris) were determined. Additionally, there are four molecular models for hyaluronidases fromMesobuthus martensii, Polybia paulista and Tityus serrulatus venoms. These enzymes are employed as adjuvants to increase the absorption and dispersion of other drugs and have been used in various off-label clinical conditions to reduce tissue edema. Moreover, a PEGylated form of a recombinant human hyaluronidase is currently under clinical trials for the treatment of metastatic pancreatic cancer. This review focuses on the arthropod venom hyaluronidases and provides an overview of their biochemical properties, role in the envenoming, structure/activity relationship, and potential medical and biotechnological applications.
Full text:
Available
Health context:
SDG3 - Target 3.3 End transmission of communicable diseases
Health problem:
Meningitis
Database:
LILACS
/
VETINDEX
Main subject:
Arthropod Venoms
/
Hyaluronoglucosaminidase
/
Animals, Poisonous
Type of study:
Prognostic study
Limits:
Animals
Language:
English
Journal:
J. venom. anim. toxins incl. trop. dis
Year:
2015
Document type:
Article
/
Project document
Institution/Affiliation country:
University of São Paulo/BR