Tissue localization and extracellular matrix degradation by PI, PII and PIII snake venom metalloproteinases: clues on the mechanisms of venom-induced hemorrhage.
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. Immun...
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Public Library of Science (PLoS)
2015-04-01
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| Series: | PLoS Neglected Tropical Diseases |
| Online Access: | https://doi.org/10.1371/journal.pntd.0003731 |
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| author | Cristina Herrera Teresa Escalante Mathieu-Benoit Voisin Alexandra Rucavado Diego Morazán Jéssica Kele A Macêdo Juan J Calvete Libia Sanz Sussan Nourshargh José María Gutiérrez Jay W Fox |
| author_facet | Cristina Herrera Teresa Escalante Mathieu-Benoit Voisin Alexandra Rucavado Diego Morazán Jéssica Kele A Macêdo Juan J Calvete Libia Sanz Sussan Nourshargh José María Gutiérrez Jay W Fox |
| author_sort | Cristina Herrera |
| collection | DOAJ |
| description | 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. |
| format | Article |
| id | doaj-art-90ea38cdfae14a9db21ab4f409d0b9d3 |
| institution | OA Journals |
| issn | 1935-2727 1935-2735 |
| language | English |
| publishDate | 2015-04-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS Neglected Tropical Diseases |
| spelling | doaj-art-90ea38cdfae14a9db21ab4f409d0b9d32025-08-20T02:22:37ZengPublic Library of Science (PLoS)PLoS Neglected Tropical Diseases1935-27271935-27352015-04-0194e000373110.1371/journal.pntd.0003731Tissue localization and extracellular matrix degradation by PI, PII and PIII snake venom metalloproteinases: clues on the mechanisms of venom-induced hemorrhage.Cristina HerreraTeresa EscalanteMathieu-Benoit VoisinAlexandra RucavadoDiego MorazánJéssica Kele A MacêdoJuan J CalveteLibia SanzSussan NoursharghJosé María GutiérrezJay W FoxSnake 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.https://doi.org/10.1371/journal.pntd.0003731 |
| spellingShingle | Cristina Herrera Teresa Escalante Mathieu-Benoit Voisin Alexandra Rucavado Diego Morazán Jéssica Kele A Macêdo Juan J Calvete Libia Sanz Sussan Nourshargh José María Gutiérrez Jay W Fox Tissue localization and extracellular matrix degradation by PI, PII and PIII snake venom metalloproteinases: clues on the mechanisms of venom-induced hemorrhage. PLoS Neglected Tropical Diseases |
| title | Tissue localization and extracellular matrix degradation by PI, PII and PIII snake venom metalloproteinases: clues on the mechanisms of venom-induced hemorrhage. |
| title_full | Tissue localization and extracellular matrix degradation by PI, PII and PIII snake venom metalloproteinases: clues on the mechanisms of venom-induced hemorrhage. |
| title_fullStr | Tissue localization and extracellular matrix degradation by PI, PII and PIII snake venom metalloproteinases: clues on the mechanisms of venom-induced hemorrhage. |
| title_full_unstemmed | Tissue localization and extracellular matrix degradation by PI, PII and PIII snake venom metalloproteinases: clues on the mechanisms of venom-induced hemorrhage. |
| title_short | Tissue localization and extracellular matrix degradation by PI, PII and PIII snake venom metalloproteinases: clues on the mechanisms of venom-induced hemorrhage. |
| title_sort | tissue localization and extracellular matrix degradation by pi pii and piii snake venom metalloproteinases clues on the mechanisms of venom induced hemorrhage |
| url | https://doi.org/10.1371/journal.pntd.0003731 |
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