Linked Life Data

19780201

Source:http://linkedlifedata.com/resource/pubmed/id/19780201

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2009-12-16
pubmed:abstractText
Astrocytes play an active role in the central nervous system and are critically involved in astrogliosis, a homotypic response of these cells to disease, injury, and associated neuroinflammation. Among the numerous molecules involved in these processes are the matrix metalloproteinases (MMPs), a family of zinc-dependent endopeptidases, secreted or membrane-bound, that regulate by proteolytic cleavage the extracellular matrix, cytokines, chemokines, cell adhesion molecules, and plasma membrane receptors. MMP activity is tightly regulated by the tissue inhibitors of MMPs (TIMPs), a family of secreted multifunctional proteins. Astrogliosis in vivo and astrocyte reactivity induced in vitro by proinflammatory cues are associated with modulation of expression and/or activity of members of the MMP/TIMP system. However, nothing is known concerning the intracellular distribution and secretory pathways of MMPs and TIMPs in astrocytes. Using a combination of cell biology, biochemistry, fluorescence and electron microscopy approaches, we investigated in cultured reactive astrocytes the intracellular distribution, transport, and secretion of MMP-2, MMP-9, TIMP-1, and TIMP-2. MMP-2 and MMP-9 demonstrate nuclear localization, differential intracellular vesicular distribution relative to the myosin V and kinesin molecular motors, and LAMP-2-labeled lysosomal compartment, and we show vesicular secretion for MMP-2, MMP-9, and their inhibitors. Our results suggest that these proteinases and their inhibitors use different pathways for trafficking and secretion for distinct astrocytic functions.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
1098-1136
pubmed:author
pubmed:copyrightInfo
(c) 2009 Wiley-Liss, Inc.
pubmed:issnType
Electronic
pubmed:volume
58
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
344-66
pubmed:meshHeading
pubmed-meshheading:19780201-Active Transport, Cell Nucleus, pubmed-meshheading:19780201-Animals, pubmed-meshheading:19780201-Animals, Newborn, pubmed-meshheading:19780201-Astrocytes, pubmed-meshheading:19780201-Cell Compartmentation, pubmed-meshheading:19780201-Cells, Cultured, pubmed-meshheading:19780201-Encephalitis, pubmed-meshheading:19780201-Gliosis, pubmed-meshheading:19780201-Lysosomal-Associated Membrane Protein 2, pubmed-meshheading:19780201-Lysosomes, pubmed-meshheading:19780201-Matrix Metalloproteinase 2, pubmed-meshheading:19780201-Matrix Metalloproteinase 9, pubmed-meshheading:19780201-Mice, pubmed-meshheading:19780201-Molecular Motor Proteins, pubmed-meshheading:19780201-Protein Transport, pubmed-meshheading:19780201-Signal Transduction, pubmed-meshheading:19780201-Tissue Inhibitor of Metalloproteinase-1, pubmed-meshheading:19780201-Tissue Inhibitor of Metalloproteinase-2, pubmed-meshheading:19780201-Transport Vesicles
pubmed:year
2010
pubmed:articleTitle
Differential vesicular distribution and trafficking of MMP-2, MMP-9, and their inhibitors in astrocytes.
pubmed:affiliation
Neurobiologie des Interactions Cellulaires et Neurophysiopathologie, UMR 6184 CNRS--Université de la Méditerranée, Faculté de Médecine, 51 Boulevard Pierre Dramard, Marseille Cedex 15, France.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't