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  • GRP78 protects a disintegrin and metalloprotease 17 against protein-disulfide isomerase A6 catalyzed inactivation.

GRP78 protects a disintegrin and metalloprotease 17 against protein-disulfide isomerase A6 catalyzed inactivation.

FEBS letters (2017-09-28)
Miriam Schäfer, Daniela C Granato, Sebastian Krossa, Anne-Kathrin Bartels, Sami Yokoo, Stefan Düsterhöft, Tomas Koudelka, Axel J Scheidig, Andreas Tholey, Adriana F Paes Leme, Joachim Grötzinger, Inken Lorenzen
ZUSAMMENFASSUNG

The shedding of ectodomains is a crucial mechanism in many physiological and pathological events. A disintegrin and metalloprotease-17 (ADAM17) is a key sheddase involved in essential processes, such as development, regeneration, and immune defense. ADAM17 exists in two conformations which differ in their disulfide connection in the membrane-proximal domain (MPD). Protein-disulfide isomerases (PDIs) on the cell surface convert the open MPD into a rigid closed form, which corresponds to inactive ADAM17. ADAM17 is expressed in its open activatable form in the endoplasmic reticulum (ER) and consequently must be protected against ER-resident PDI activity. Here, we show that the chaperone 78-kDa glucose-regulated protein (GRP78) protects the MPD against PDI-dependent disulfide-bond isomerization by binding to this domain and, thereby, preventing ADAM17 inhibition.

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VER-155008, ≥98% (HPLC)
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Malachitgrünchlorid, analytical standard
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