PMID- 10025398
OWN - NLM
STAT- MEDLINE
DCOM- 19990303
LR  - 20190705
IS  - 0092-8674 (Print)
IS  - 0092-8674 (Linking)
VI  - 96
IP  - 3
DP  - 1999 Feb 5
TI  - The integrin alpha v beta 6 binds and activates latent TGF beta 1: a mechanism
      for regulating pulmonary inflammation and fibrosis.
PG  - 319-28
AB  - Transforming growth factor beta (TGF beta) family members are secreted in
      inactive complexes with a latency-associated peptide (LAP), a protein derived
      from the N-terminal region of the TGF beta gene product. Extracellular activation
      of these complexes is a critical but incompletely understood step in regulation
      of TGF beta function in vivo. We show that TGF beta 1 LAP is a ligand for the
      integrin alpha v beta 6 and that alpha v beta 6-expressing cells induce spatially
      restricted activation of TGF beta 1. This finding explains why mice lacking this 
      integrin develop exaggerated inflammation and, as we show, are protected from
      pulmonary fibrosis. These data identify a novel mechanism for locally regulating 
      TGF beta 1 function in vivo by regulating expression of the alpha v beta 6
      integrin.
FAU - Munger, J S
AU  - Munger JS
AD  - Department of Medicine, and Kaplan Cancer Center, New York University School of
      Medicine, New York 10016-6402, USA.
FAU - Huang, X
AU  - Huang X
FAU - Kawakatsu, H
AU  - Kawakatsu H
FAU - Griffiths, M J
AU  - Griffiths MJ
FAU - Dalton, S L
AU  - Dalton SL
FAU - Wu, J
AU  - Wu J
FAU - Pittet, J F
AU  - Pittet JF
FAU - Kaminski, N
AU  - Kaminski N
FAU - Garat, C
AU  - Garat C
FAU - Matthay, M A
AU  - Matthay MA
FAU - Rifkin, D B
AU  - Rifkin DB
FAU - Sheppard, D
AU  - Sheppard D
LA  - eng
GR  - HL47412/HL/NHLBI NIH HHS/United States
GR  - HL53949/HL/NHLBI NIH HHS/United States
GR  - HL56385/HL/NHLBI NIH HHS/United States
GR  - etc.
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Cell
JT  - Cell
JID - 0413066
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Integrins)
RN  - 0 (Ligands)
RN  - 0 (Peptide Fragments)
RN  - 0 (Protein Precursors)
RN  - 0 (Proteins)
RN  - 0 (Transforming Growth Factor beta)
RN  - 0 (Transforming Growth Factor beta1)
RN  - 0 (integrin alphavbeta6)
RN  - 11056-06-7 (Bleomycin)
SB  - IM
MH  - 3T3 Cells
MH  - Animals
MH  - *Antigens, Neoplasm
MH  - Bleomycin/pharmacology
MH  - CHO Cells
MH  - Cricetinae
MH  - Epithelial Cells/physiology
MH  - Esophagus/pathology
MH  - Humans
MH  - Integrins/biosynthesis/*metabolism/physiology
MH  - Keratinocytes/physiology
MH  - Ligands
MH  - Mice
MH  - Mice, Knockout
MH  - *Peptide Fragments
MH  - Protein Binding
MH  - *Protein Precursors
MH  - Proteins/metabolism
MH  - Pulmonary Fibrosis/chemically induced/*metabolism/pathology/prevention & control
MH  - Transforming Growth Factor beta/*metabolism/physiology
MH  - Transforming Growth Factor beta1
MH  - Tumor Cells, Cultured
EDAT- 1999/02/20 00:00
MHDA- 1999/02/20 00:01
CRDT- 1999/02/20 00:00
PHST- 1999/02/20 00:00 [pubmed]
PHST- 1999/02/20 00:01 [medline]
PHST- 1999/02/20 00:00 [entrez]
AID - S0092-8674(00)80545-0 [pii]
AID - 10.1016/s0092-8674(00)80545-0 [doi]
PST - ppublish
SO  - Cell. 1999 Feb 5;96(3):319-28. doi: 10.1016/s0092-8674(00)80545-0.