What question did this study set out to answer?

Identify and systematically map membrane proteins shed from the surface of human platelets following activation.

October 20, 2010BloodOpen Access

Deciphering the human platelet sheddome

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Authors

KFKaren P. FongUniversity of Pennsylvania CBColin G. BarryAlliance Pharmaceutical (United States)ATAnh Ngoc TranCan Tho University

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Implication

Proteomic profiling uncovers 69 membrane protein fragments released by activated human platelets, suggesting ADAM17 mediates substantial ectodomain shedding during activation.

Key Points

Identify and systematically map membrane proteins shed from the surface of human platelets following activation.
Analyzed supernatants of activated human platelets by mass spectrometry after removing plasma proteins and microparticles.
Characterized candidate protein semaphorin 7A expression, α-granule localization, and activation-dependent cleavage.
Tested the effects of a selective ADAM17 inhibitor on the shedding of identified candidate membrane proteins.
Identified 1,048 proteins in the platelet supernatant, including 69 membrane proteins of which 59 represent novel shed candidates.
Demonstrated novel platelet surface expression, α-granule association, and activation-induced cleavage of semaphorin 7A.
Demonstrated that chemical inhibition of ADAM17 substantially reduces the cleavage of semaphorin 7A and 12 additional membrane proteins.

Cite This Study

Fong et al. (2010) studied this question.

synapsesocial.com/papers/69ffa41ada5c1eb07f2d8194 https://doi.org/10.1182/blood-2010-05-283838

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Implication

Proteomic profiling uncovers 69 membrane protein fragments released by activated human platelets, suggesting ADAM17 mediates substantial ectodomain shedding during activation.

Deciphering the human platelet sheddome

Discussion

Member takes

Implication

Key Points

Cite This Study

Deciphering the human platelet sheddome

Discussion

Member takes

Implication

Key Points

Cite This Study

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