A Mechanism for Regulating Pulmonary Inflammation and Fibrosis: The Integrin αvβ6 Binds and Activates Latent TGF β1

نویسندگان

  • John S Munger
  • Xiaozhu Huang
  • Hisaaki Kawakatsu
  • Mark J.D Griffiths
  • Stephen L Dalton
  • Jianfeng Wu
  • Jean-François Pittet
  • Naftali Kaminski
  • Chrystelle Garat
  • Michael A Matthay
  • Daniel B Rifkin
  • Dean Sheppard
چکیده

ated, and in this configuration TGFb is unable to bind University of California, San Francisco to its receptors; that is, TGFb is latent. In most cases, San Francisco, California 94143-0854 the complex of LAP and TGFb (the small latent complex 5 Department of Medicine SLC) is joined by latent TGFb binding protein 1 (LTBP1), 6 Cell Biology and Kaplan Cancer Center a matrix protein with sequence similarity to the fibrillins, New York University School of Medicine and the complex of all three proteins is called the large New York, New York 10016-6402 latent complex (LLC). Latent TGFb can be linked by

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Atypical interactions of integrin αVβ8 with pro-TGF-β1.

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The Single-Molecule Mechanics of the Latent TGF-β1 Complex

BACKGROUND TGF-β1 controls many pathophysiological processes including tissue homeostasis, fibrosis, and cancer progression. Together with its latency-associated peptide (LAP), TGF-β1 binds to the latent TGF-β1-binding protein-1 (LTBP-1), which is part of the extracellular matrix (ECM). Transmission of cell force via integrins is one major mechanism to activate latent TGF-β1 from ECM stores. La...

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عنوان ژورنال:
  • Cell

دوره 96  شماره 

صفحات  -

تاریخ انتشار 1999