| dc.description | Snake venoms are complex mixtures of proteins,
which aVect the vital biologic systems of prey, as
well as humans. Envenomation leads to immobilization by
paralysis, cardiac, and circulatory failure. These same
venom proteins that cause havoc in the physiologic system
could be used as therapeutic agents. Disintegrins and disintegrin-
like proteins are molecules found in the venom of
four snake families (Atractaspididae, Elapidae, Viperidae,
and Colubridae). The disintegrins are non-enzymatic proteins
that inhibit cell–cell interactions, cell–matrix interactions,
and signal transduction. These proteins may have
potential in the treatment of strokes, heart attacks, cancers,
osteoporosis, and diabetes. The present study describes the
isolation and characterization of a disintegrin (colombistatin)
found in the venom of the Venezuelan snake mapanare
(Bothrops colombiensis). Colombistatin was puriWed by a
two-step high-performance liquid chromatography procedure,
which included reverse phase C18 and size exclusion
protein Pak 60. Colombistatin inhibited ADP-induced
platelet aggregation, human urinary (T24) and skin melanoma
(SK-Mel-28) cancer cell adhesion to Wbronectin, and
cell migration. Colombistatin contained 72 amino acids
with a mass of 7.778 kDa as determined by mass spectrometry.
Colombistatin could be used as a therapeutic tool in
the treatment of melanoma cancers and also thrombotic diseases. | |
