PMID- 8238531
OWN - NLM
STAT- MEDLINE
DCOM- 19931222
LR  - 20171213
IS  - 0002-9513 (Print)
IS  - 0002-9513 (Linking)
VI  - 265
IP  - 5 Pt 1
DP  - 1993 Nov
TI  - A 96-kDa gelatinase induced by TNF-alpha contributes to increased microvascular 
      endothelial permeability.
PG  - L438-47
AB  - Tumor necrosis factor-alpha (TNF-alpha) may increase vascular endothelial 
      permeability through alteration of the extracellular matrix (ECM). Incubation of 
      bovine pulmonary microvascular endothelial (BPMVE) cells grown to confluence on 
      microporous filters with 10(4) U/ml TNF-alpha for 24 h increased monolayer 
      permeability to 125I-labeled albumin two- to threefold. TNF-alpha treatment also 
      induced expression of a 96-kDa gelatinolytic metalloproteinase that was present 
      in the medium and bound to the ECM. The induced 96-kDa metalloproteinase was 
      purified from conditioned medium and found to cleave fibronectin, laminin, types 
      IV and V collagens, and gelatins from types I and III collagens, suggesting 
      identity as a type IV collagenase-gelatinase. Incubation of BPMVE cells with the 
      96-kDa gelatinase increased monolayer permeability, an effect prevented by 
      inclusion of either tissue inhibitor of metalloproteinase (TIMP) or 
      1,10-phenanthroline. When BPMVE cells were incubated with the 96-kDa gelatinase 
      or 10(4) U/ml TNF-alpha and then stripped from the filters, the remaining ECM 
      displayed increased permeability to 125I-albumin compared with matrix from 
      untreated BPMVE. The ECM extracts from both TNF-alpha- and enzyme-treated cells 
      were found to contain less fibronectin, whereas their total protein contents were 
      similar to those of untreated controls. These results suggest that the 96-kDa 
      metalloproteinase induced by TNF-alpha contributes to increased vascular 
      endothelial permeability through the degradation of specific extracellular matrix 
      components.
FAU - Partridge, C A
AU  - Partridge CA
AD  - Department of Physiology, Albany Medical College of Union University, New York 
      12208.
FAU - Jeffrey, J J
AU  - Jeffrey JJ
FAU - Malik, A B
AU  - Malik AB
LA  - eng
GR  - HL-27016/HL/NHLBI NIH HHS/United States
GR  - HL-32418/HL/NHLBI NIH HHS/United States
GR  - HL-45638/HL/NHLBI NIH HHS/United States
GR  - etc.
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Am J Physiol
JT  - The American journal of physiology
JID - 0370511
RN  - 0 (Caseins)
RN  - 0 (Fibronectins)
RN  - 0 (Glycoproteins)
RN  - 0 (Matrix Metalloproteinase Inhibitors)
RN  - 0 (Phenanthrolines)
RN  - 0 (Tissue Inhibitor of Metalloproteinases)
RN  - 0 (Tumor Necrosis Factor-alpha)
RN  - EC 3.4.24.- (Gelatinases)
RN  - W4X6ZO7939 (1,10-phenanthroline)
SB  - IM
MH  - Animals
MH  - Caseins/metabolism
MH  - Cattle
MH  - Cell Line
MH  - *Cell Membrane Permeability
MH  - Cells, Cultured
MH  - Electrophoresis, Polyacrylamide Gel
MH  - Endothelium, Vascular/drug effects/enzymology/*physiology
MH  - Fibronectins/metabolism
MH  - Gelatinases/*biosynthesis/isolation & purification
MH  - Glycoproteins/pharmacology
MH  - Humans
MH  - Matrix Metalloproteinase Inhibitors
MH  - Microcirculation
MH  - Molecular Weight
MH  - Phenanthrolines/pharmacology
MH  - *Pulmonary Circulation
MH  - Substrate Specificity
MH  - Tissue Inhibitor of Metalloproteinases
MH  - Tumor Cells, Cultured
MH  - Tumor Necrosis Factor-alpha/*pharmacology
EDAT- 1993/11/01 00:00
MHDA- 1993/11/01 00:01
CRDT- 1993/11/01 00:00
PHST- 1993/11/01 00:00 [pubmed]
PHST- 1993/11/01 00:01 [medline]
PHST- 1993/11/01 00:00 [entrez]
AID - 10.1152/ajplung.1993.265.5.L438 [doi]
PST - ppublish
SO  - Am J Physiol. 1993 Nov;265(5 Pt 1):L438-47. doi: 10.1152/ajplung.1993.265.5.L438.