Tissue Localization and Extracellular Matrix Degradation by PI, PII and PIII Snake Venom Metalloproteinases: Clues on the Mechanisms of Venom-Induced Hemorrhage
artículo original
Fecha
2015-04-24Autor
Voisin, Mathieu-Benoit
Rucavado Romero, Alexandra
Morazán, Diego
Macêdo, Jéssica Kele A.
Calvete Chornet, Juan José
Sanz, Libia
Nourshargh, Sussan
Gutiérrez, José María
Fox, Jay W.
Herrera Arias, Cristina
Escalante Muñoz, Teresa
Metadatos
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Snake venom hemorrhagic metalloproteinases (SVMPs) of the PI, PII and PIII classes were
compared in terms of tissue localization and their ability to hydrolyze basement membrane
components in vivo, as well as by a proteomics analysis of exudates collected in tissue injected
with these enzymes. Immunohistochemical analyses of co-localization of these
SVMPs with type IV collagen revealed that PII and PIII enzymes co-localized with type IV
collagen in capillaries, arterioles and post-capillary venules to a higher extent than PI
SVMP, which showed a more widespread distribution in the tissue. The patterns of hydrolysis
by these three SVMPs of laminin, type VI collagen and nidogen in vivo greatly differ,
whereas the three enzymes showed a similar pattern of degradation of type IV collagen,
supporting the concept that hydrolysis of this component is critical for the destabilization of
microvessel structure leading to hemorrhage. Proteomic analysis of wound exudate revealed
similarities and differences between the action of the three SVMPs. Higher extent of
proteolysis was observed for the PI enzyme regarding several extracellular matrix components
and fibrinogen, whereas exudates from mice injected with PII and PIII SVMPs had
higher amounts of some intracellular proteins. Our results provide novel clues for understanding
the mechanisms by which SVMPs induce damage to the microvasculature and
generate hemorrhage.
External link to the item
10.1371/journal.pntd.0003731Colecciones
- Microbiología [1171]
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