Unexpected timely fracture union in matrix metalloproteinase 9 deficient mice
Immediately following a fracture, a fibrin laden hematoma is formed to prevent bleeding and infection. Subsequently, the organized removal of fibrin, via the protease plasmin, is essential to permit fracture repair through angiogenesis and ossification. Yet, when plasmin activity is lost, the deplet...
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| creator | Yuasa, Masato Saito, Masanori Molina, Cesar Moore-Lotridge, Stephanie N Benvenuti, Michael A Mignemi, Nicholas A Okawa, Atsushi Yoshii, Toshitaka Schwartz, Herbert S Nyman, Jeffry S Schoenecker, Jonathan G |
| description | Immediately following a fracture, a fibrin laden hematoma is formed to prevent bleeding and infection. Subsequently, the organized removal of fibrin, via the protease plasmin, is essential to permit fracture repair through angiogenesis and ossification. Yet, when plasmin activity is lost, the depletion of fibrin alone is insufficient to fully restore fracture repair, suggesting the existence of additional plasmin targets important for fracture repair. Previously, activated matrix metalloproteinase 9 (MMP-9) was demonstrated to function in fracture repair by promoting angiogenesis. Given that MMP-9 is a defined plasmin target, it was hypothesized that pro-MMP-9, following plasmin activation, promotes fracture repair. This hypothesis was tested in a fixed murine femur fracture model with serial assessment of fracture healing. Contrary to previous findings, a complete loss of MMP-9 failed to affect fracture healing and union through 28 days post injury. Therefore, these results demonstrated that MMP-9 is dispensable for timely fracture union and cartilage transition to bone in fixed femur fractures. Pro-MMP-9 is therefore not a significant target of plasmin in fracture repair and future studies assessing additional plasmin targets associated with angiogenesis are warranted. |
| doi_str_mv | 10.1371/journal.pone.0198088 |
| format | Article |
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Subsequently, the organized removal of fibrin, via the protease plasmin, is essential to permit fracture repair through angiogenesis and ossification. Yet, when plasmin activity is lost, the depletion of fibrin alone is insufficient to fully restore fracture repair, suggesting the existence of additional plasmin targets important for fracture repair. Previously, activated matrix metalloproteinase 9 (MMP-9) was demonstrated to function in fracture repair by promoting angiogenesis. Given that MMP-9 is a defined plasmin target, it was hypothesized that pro-MMP-9, following plasmin activation, promotes fracture repair. This hypothesis was tested in a fixed murine femur fracture model with serial assessment of fracture healing. Contrary to previous findings, a complete loss of MMP-9 failed to affect fracture healing and union through 28 days post injury. Therefore, these results demonstrated that MMP-9 is dispensable for timely fracture union and cartilage transition to bone in fixed femur fractures. Pro-MMP-9 is therefore not a significant target of plasmin in fracture repair and future studies assessing additional plasmin targets associated with angiogenesis are warranted.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0198088</identifier><identifier>PMID: 29851987</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Analysis ; Angiogenesis ; Animals ; Biology and Life Sciences ; Biomechanics ; Bleeding ; Bone healing ; Cartilage ; Femoral Fractures - enzymology ; Femoral Fractures - physiopathology ; Femoral Fractures - surgery ; Femur ; Fibrin ; Fracture Fixation, Internal ; Fracture Healing ; Fracture repair ; Fractures ; Gelatinase B ; Growth factors ; Healing ; Health aspects ; Hematoma ; Immunology ; Infection control ; Infections ; Matrix metalloproteinase ; Matrix Metalloproteinase 9 - deficiency ; Matrix metalloproteinase inhibitors ; Matrix metalloproteinases ; Medicine and Health Sciences ; Metalloproteinase ; Mice ; Mice, Inbred C57BL ; Ossification ; Plasmin ; Proteases ; Rehabilitation ; Repair ; Surgery ; Tomography ; Trauma</subject><ispartof>PloS one, 2018-05, Vol.13 (5), p.e0198088-e0198088</ispartof><rights>COPYRIGHT 2018 Public Library of Science</rights><rights>2018 Yuasa et al. This is an open access article distributed under the terms of the Creative Commons Attribution License: http://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. 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Subsequently, the organized removal of fibrin, via the protease plasmin, is essential to permit fracture repair through angiogenesis and ossification. Yet, when plasmin activity is lost, the depletion of fibrin alone is insufficient to fully restore fracture repair, suggesting the existence of additional plasmin targets important for fracture repair. Previously, activated matrix metalloproteinase 9 (MMP-9) was demonstrated to function in fracture repair by promoting angiogenesis. Given that MMP-9 is a defined plasmin target, it was hypothesized that pro-MMP-9, following plasmin activation, promotes fracture repair. This hypothesis was tested in a fixed murine femur fracture model with serial assessment of fracture healing. Contrary to previous findings, a complete loss of MMP-9 failed to affect fracture healing and union through 28 days post injury. Therefore, these results demonstrated that MMP-9 is dispensable for timely fracture union and cartilage transition to bone in fixed femur fractures. Pro-MMP-9 is therefore not a significant target of plasmin in fracture repair and future studies assessing additional plasmin targets associated with angiogenesis are warranted.</description><subject>Analysis</subject><subject>Angiogenesis</subject><subject>Animals</subject><subject>Biology and Life Sciences</subject><subject>Biomechanics</subject><subject>Bleeding</subject><subject>Bone healing</subject><subject>Cartilage</subject><subject>Femoral Fractures - enzymology</subject><subject>Femoral Fractures - physiopathology</subject><subject>Femoral Fractures - surgery</subject><subject>Femur</subject><subject>Fibrin</subject><subject>Fracture Fixation, Internal</subject><subject>Fracture Healing</subject><subject>Fracture repair</subject><subject>Fractures</subject><subject>Gelatinase B</subject><subject>Growth factors</subject><subject>Healing</subject><subject>Health aspects</subject><subject>Hematoma</subject><subject>Immunology</subject><subject>Infection control</subject><subject>Infections</subject><subject>Matrix metalloproteinase</subject><subject>Matrix Metalloproteinase 9 - 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Subsequently, the organized removal of fibrin, via the protease plasmin, is essential to permit fracture repair through angiogenesis and ossification. Yet, when plasmin activity is lost, the depletion of fibrin alone is insufficient to fully restore fracture repair, suggesting the existence of additional plasmin targets important for fracture repair. Previously, activated matrix metalloproteinase 9 (MMP-9) was demonstrated to function in fracture repair by promoting angiogenesis. Given that MMP-9 is a defined plasmin target, it was hypothesized that pro-MMP-9, following plasmin activation, promotes fracture repair. This hypothesis was tested in a fixed murine femur fracture model with serial assessment of fracture healing. Contrary to previous findings, a complete loss of MMP-9 failed to affect fracture healing and union through 28 days post injury. Therefore, these results demonstrated that MMP-9 is dispensable for timely fracture union and cartilage transition to bone in fixed femur fractures. Pro-MMP-9 is therefore not a significant target of plasmin in fracture repair and future studies assessing additional plasmin targets associated with angiogenesis are warranted.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>29851987</pmid><doi>10.1371/journal.pone.0198088</doi><tpages>e0198088</tpages><orcidid>https://orcid.org/0000-0002-3097-5496</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | Analysis Angiogenesis Animals Biology and Life Sciences Biomechanics Bleeding Bone healing Cartilage Femoral Fractures - enzymology Femoral Fractures - physiopathology Femoral Fractures - surgery Femur Fibrin Fracture Fixation, Internal Fracture Healing Fracture repair Fractures Gelatinase B Growth factors Healing Health aspects Hematoma Immunology Infection control Infections Matrix metalloproteinase Matrix Metalloproteinase 9 - deficiency Matrix metalloproteinase inhibitors Matrix metalloproteinases Medicine and Health Sciences Metalloproteinase Mice Mice, Inbred C57BL Ossification Plasmin Proteases Rehabilitation Repair Surgery Tomography Trauma |
| title | Unexpected timely fracture union in matrix metalloproteinase 9 deficient mice |
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