The snake venom toxin alboaggregin-A activates glycoprotein VI

Naoki Asazuma; Stuart J. Marshall; Oscar Berlanga; Daniel Snell; Alastair W. Poole; Michael C. Berndt; Robert K. Andrews; Steve P. Watson

doi:10.1182/blood.V97.12.3989

The snake venom toxin alboaggregin-A activates glycoprotein VI

Naoki Asazuma, Stuart J. Marshall, Oscar Berlanga, Daniel Snell, Alastair W. Poole, Michael C. Berndt, Robert K. Andrews, Steve P. Watson

Research output: Contribution to journal › Article › Research › peer-review

28 Citations (Scopus)

Abstract

The glycoprotein (GP)-lb-IX-V receptor complex has recently been reported to signal through a pathway similar to that used by the collagen receptor GPVI, with a critical role described for the Fc receptor γ-chain. The evidence for this was based in part on studies with the GPlbα-selective snake venom toxin, alboaggregin-A. In the present study, it is reported that alboaggregin-A has activity at the Collagen receptor GPVI in addition to GPlbα, and evidence is provided that this contributes to protein tyrosine phosphorylation, shape change, and GPlb-llla-dependent aggregation. This may explain why responses to alboaggregin-A are distinct from those to von Willebrand factor-ristocetin.

Original language	English
Pages (from-to)	3989-3991
Number of pages	3
Journal	Blood
Volume	97
Issue number	12
DOIs	https://doi.org/10.1182/blood.V97.12.3989
Publication status	Published - 15 Jun 2001
Externally published	Yes

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title = "The snake venom toxin alboaggregin-A activates glycoprotein VI",

abstract = "The glycoprotein (GP)-lb-IX-V receptor complex has recently been reported to signal through a pathway similar to that used by the collagen receptor GPVI, with a critical role described for the Fc receptor γ-chain. The evidence for this was based in part on studies with the GPlbα-selective snake venom toxin, alboaggregin-A. In the present study, it is reported that alboaggregin-A has activity at the Collagen receptor GPVI in addition to GPlbα, and evidence is provided that this contributes to protein tyrosine phosphorylation, shape change, and GPlb-llla-dependent aggregation. This may explain why responses to alboaggregin-A are distinct from those to von Willebrand factor-ristocetin.",

author = "Naoki Asazuma and Marshall, \{Stuart J.\} and Oscar Berlanga and Daniel Snell and Poole, \{Alastair W.\} and Berndt, \{Michael C.\} and Andrews, \{Robert K.\} and Watson, \{Steve P.\}",

year = "2001",

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doi = "10.1182/blood.V97.12.3989",

language = "English",

volume = "97",

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T1 - The snake venom toxin alboaggregin-A activates glycoprotein VI

AU - Asazuma, Naoki

AU - Marshall, Stuart J.

AU - Berlanga, Oscar

AU - Snell, Daniel

AU - Poole, Alastair W.

AU - Berndt, Michael C.

AU - Andrews, Robert K.

AU - Watson, Steve P.

PY - 2001/6/15

Y1 - 2001/6/15

N2 - The glycoprotein (GP)-lb-IX-V receptor complex has recently been reported to signal through a pathway similar to that used by the collagen receptor GPVI, with a critical role described for the Fc receptor γ-chain. The evidence for this was based in part on studies with the GPlbα-selective snake venom toxin, alboaggregin-A. In the present study, it is reported that alboaggregin-A has activity at the Collagen receptor GPVI in addition to GPlbα, and evidence is provided that this contributes to protein tyrosine phosphorylation, shape change, and GPlb-llla-dependent aggregation. This may explain why responses to alboaggregin-A are distinct from those to von Willebrand factor-ristocetin.

AB - The glycoprotein (GP)-lb-IX-V receptor complex has recently been reported to signal through a pathway similar to that used by the collagen receptor GPVI, with a critical role described for the Fc receptor γ-chain. The evidence for this was based in part on studies with the GPlbα-selective snake venom toxin, alboaggregin-A. In the present study, it is reported that alboaggregin-A has activity at the Collagen receptor GPVI in addition to GPlbα, and evidence is provided that this contributes to protein tyrosine phosphorylation, shape change, and GPlb-llla-dependent aggregation. This may explain why responses to alboaggregin-A are distinct from those to von Willebrand factor-ristocetin.

UR - https://www.scopus.com/pages/publications/0035877964

U2 - 10.1182/blood.V97.12.3989

DO - 10.1182/blood.V97.12.3989

M3 - Article

C2 - 11389045

AN - SCOPUS:0035877964

SN - 0006-4971

VL - 97

SP - 3989

EP - 3991

JO - Blood

JF - Blood

IS - 12

ER -

The snake venom toxin alboaggregin-A activates glycoprotein VI

Abstract

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