| Autor: |
Chuliá-Peris L; Department of Physiology, Faculty of Pharmacy, University of Valencia, 46100 Burjassot, Spain., Carreres-Rey C; Department of Physiology, Faculty of Pharmacy, University of Valencia, 46100 Burjassot, Spain., Gabasa M; Unit of Biophysics and Bioengineering, Department of Biomedicine, School of Medicine and Health Sciences, University of Barcelona, 08036 Barcelona, Spain., Alcaraz J; Unit of Biophysics and Bioengineering, Department of Biomedicine, School of Medicine and Health Sciences, University of Barcelona, 08036 Barcelona, Spain.; Thoracic Oncology Unit, Hospital Clinic Barcelona, 08036 Barcelona, Spain.; Institute for Bioengineering of Catalonia (IBEC), The Barcelona Institute for Science and Technology (BIST), 08028 Barcelona, Spain., Carretero J; Department of Physiology, Faculty of Pharmacy, University of Valencia, 46100 Burjassot, Spain., Pereda J; Department of Physiology, Faculty of Pharmacy, University of Valencia, 46100 Burjassot, Spain. |
| Abstrakt: |
Pulmonary fibrosis (PF) is characterized by aberrant extracellular matrix (ECM) deposition, activation of fibroblasts to myofibroblasts and parenchymal disorganization, which have an impact on the biomechanical traits of the lung. In this context, the balance between matrix metalloproteinases (MMPs) and their tissue inhibitors of metalloproteinases (TIMPs) is lost. Interestingly, several MMPs are overexpressed during PF and exhibit a clear profibrotic role (MMP-2, -3, -8, -11, -12 and -28), but a few are antifibrotic (MMP-19), have both profibrotic and antifibrotic capacity (MMP7), or execute an unclear (MMP-1, -9, -10, -13, -14) or unknown function. TIMPs are also overexpressed in PF; hence, the modulation and function of MMPs and TIMP are more complex than expected. EMMPRIN/CD147 (also known as basigin) is a transmembrane glycoprotein from the immunoglobulin superfamily (IgSF) that was first described to induce MMP activity in fibroblasts. It also interacts with other molecules to execute non-related MMP aactions well-described in cancer progression, migration, and invasion. Emerging evidence strongly suggests that CD147 plays a key role in PF not only by MMP induction but also by stimulating fibroblast myofibroblast transition. In this review, we study the structure and function of MMPs, TIMPs and CD147 in PF and their complex crosstalk between them. |
