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Disulphide-isomerase-enabled shedding of tumour-associated NKG2D ligands

Author

Listed:
  • Brett K. Kaiser

    (Fred Hutchinson Cancer Research Center, 1100 Fairview Avenue North, Seattle, Washington 98109, USA)

  • Daesong Yim

    (Fred Hutchinson Cancer Research Center, 1100 Fairview Avenue North, Seattle, Washington 98109, USA)

  • I-Ting Chow

    (Fred Hutchinson Cancer Research Center, 1100 Fairview Avenue North, Seattle, Washington 98109, USA)

  • Segundo Gonzalez

    (Fred Hutchinson Cancer Research Center, 1100 Fairview Avenue North, Seattle, Washington 98109, USA
    Present address: Biologia Funcional, Universidad de Oviedo, IUOPA, Oviedo, Asturias 33006, Spain.)

  • Zhenpeng Dai

    (Fred Hutchinson Cancer Research Center, 1100 Fairview Avenue North, Seattle, Washington 98109, USA)

  • Henning H. Mann

    (Fred Hutchinson Cancer Research Center, 1100 Fairview Avenue North, Seattle, Washington 98109, USA)

  • Roland K. Strong

    (Fred Hutchinson Cancer Research Center, 1100 Fairview Avenue North, Seattle, Washington 98109, USA)

  • Veronika Groh

    (Fred Hutchinson Cancer Research Center, 1100 Fairview Avenue North, Seattle, Washington 98109, USA)

  • Thomas Spies

    (Fred Hutchinson Cancer Research Center, 1100 Fairview Avenue North, Seattle, Washington 98109, USA)

Abstract

Evasive tumours A number of advanced tumours appear to evade immune recognition by natural killer cells by shedding the soluble major histocompatibility complex class I-related ligand MICA, which inactivates the NKG2D receptor. New work in tumour cell cultures shows that the mechanism of this shedding process involves ERp5, a protein isomerase associated with the endoplasmic reticulum. This identifies surface ERp5 as a strategic target for therapeutic intervention to block tumour immune evasion.

Suggested Citation

  • Brett K. Kaiser & Daesong Yim & I-Ting Chow & Segundo Gonzalez & Zhenpeng Dai & Henning H. Mann & Roland K. Strong & Veronika Groh & Thomas Spies, 2007. "Disulphide-isomerase-enabled shedding of tumour-associated NKG2D ligands," Nature, Nature, vol. 447(7143), pages 482-486, May.
    • Handle: RePEc:nat:nature:v:447:y:2007:i:7143:d:10.1038_nature05768
    DOI: 10.1038/nature05768
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