dc.contributor.author |
Selman, M |
|
dc.contributor.author |
Ruiz, V |
|
dc.contributor.author |
Cabrera, S |
|
dc.contributor.author |
Segura-Valdez, ML |
|
dc.contributor.author |
Ramirez, R |
|
dc.contributor.author |
BarRíos, R |
|
dc.contributor.author |
Pardo-Cemo, Annie |
|
dc.date.accessioned |
2011-01-22T10:27:33Z |
|
dc.date.available |
2011-01-22T10:27:33Z |
|
dc.date.issued |
2000 |
|
dc.identifier.issn |
10400605 |
|
dc.identifier.uri |
http://hdl.handle.net/11154/3277 |
|
dc.description.abstract |
Fibroblast proliferation and extracellular matrix accumulation characterize idiopathic pulmonary fibrosis (IPF). We evaluated the presence of tissue inhibitor of metalloproteinase (TIMP)-1, -2, -3, and -4 |
en_US |
dc.description.abstract |
collagenase-1, -2, and -3 |
en_US |
dc.description.abstract |
gelatinases A and B |
en_US |
dc.description.abstract |
and membrane type 1 matrix metalloproteinase (MMP) in 12 IPF and 6 control lungs. TIMP-1 was found in interstitial macrophages and TIMP-2 in fibroblast foci. TIMP-3 revealed an intense staining mainly decorating the elastic lamina in vessels. TIMP-4 was expressed in IPF lungs by epithelial and plasma cells. TIMP-2 colocalized with Ki67 in fibroblasts, whereas TIMP-3 colocalized with p27 in inflammatory and epithelial cells. Collagenase-1 was localized in macrophages and alveolar epithelial cells, collagenase-2 was localized in a few neutrophils, and collagenase-3 was not detected. MMP-9 was found in neutrophils and subepithelial myofibroblasts. Myofibroblast expression of MMP-9 was corroborated in vitro by RT-PCR. MMP-2 was noticed in myofibroblasts, some of them close to areas of basement membrane disruption, and membrane type 1 MMP was noticed in interstitial macrophages. These findings suggest that in IPF there is higher expression of TIMPs compared with collagenases, supporting the hypothesis that a nondegrading fibrillar collagen microenvironment is prevailing. |
en_US |
dc.language.iso |
en |
en_US |
dc.title |
TIMP-1,-2,-3, and-4 in idiopathic pulmonary fibrosis. A prevailing nondegradative lung microenvironment? |
|
dc.type |
Artículo de investigación |
en_US |
dc.identifier.idprometeo |
2476 |
|
dc.source.novolpages |
279(3) |
|
dc.subject.wos |
Physiology |
|
dc.subject.wos |
Respiratory System |
|
dc.description.index |
WoS: SCI, SSCI o AHCI |
|
dc.subject.keywords |
tissue inhibitor of metalloproteinases |
|
dc.subject.keywords |
gelatinases |
|
dc.subject.keywords |
collagenase |
|
dc.subject.keywords |
fibrosis |
|
dc.relation.journal |
American Journal of Physiology-Lung Cellular and Molecular Physiology |
|
dc.description.Departamento |
Departamento de Biología Comparada |
|