hTRPC1-associated alpha-actinin, and not hTRPC1 itself, is tyrosine phosphorylated during human platelet activation

P C Redondo; A G S Harper; M T Harper; S L Brownlow; J A Rosado; S O Sage

doi:10.1111/j.1538-7836.2007.02773.x

hTRPC1-associated alpha-actinin, and not hTRPC1 itself, is tyrosine phosphorylated during human platelet activation

P C Redondo
, A G S Harper
, M T Harper
, S L Brownlow
, J A Rosado
, S O Sage

School of Physiology, Pharmacology & Neuroscience

Research output: Contribution to journal › Article (Academic Journal) › peer-review

7 Citations (Scopus)

Abstract

Canonical transient receptor potential channels (TRPCs), which are regulated by several processes, including tyrosine phosphorylation, are candidates for the conduction of store-operated Ca(2+) entry (SOCE).

Original language	English
Pages (from-to)	2476-83
Number of pages	8
Journal	Journal of Thrombosis and Haemostasis
Volume	5
Issue number	12
DOIs	https://doi.org/10.1111/j.1538-7836.2007.02773.x
Publication status	Published - Dec 2007

Keywords

Thrombin
Phosphotyrosine
Humans
Actinin
Immunoprecipitation
Tyrosine
Protein-Tyrosine Kinases
Platelet Activation
Enzyme Inhibitors
Membrane Proteins
Blood Platelets
Blotting, Western
Neoplasm Proteins
Multiprotein Complexes
Phosphorylation
TRPC Cation Channels
Quinolines
Time Factors
Protein Tyrosine Phosphatase, Non-Receptor Type 6
Calcium Signaling

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@article{8df2cb833d6a4a1fba756f7f83960a19,

title = "hTRPC1-associated alpha-actinin, and not hTRPC1 itself, is tyrosine phosphorylated during human platelet activation",

abstract = "Canonical transient receptor potential channels (TRPCs), which are regulated by several processes, including tyrosine phosphorylation, are candidates for the conduction of store-operated Ca(2+) entry (SOCE).",

keywords = "Thrombin, Phosphotyrosine, Humans, Actinin, Immunoprecipitation, Tyrosine, Protein-Tyrosine Kinases, Platelet Activation, Enzyme Inhibitors, Membrane Proteins, Blood Platelets, Blotting, Western, Neoplasm Proteins, Multiprotein Complexes, Phosphorylation, TRPC Cation Channels, Quinolines, Time Factors, Protein Tyrosine Phosphatase, Non-Receptor Type 6, Calcium Signaling",

author = "Redondo, \{P C\} and Harper, \{A G S\} and Harper, \{M T\} and Brownlow, \{S L\} and Rosado, \{J A\} and Sage, \{S O\}",

year = "2007",

month = dec,

doi = "10.1111/j.1538-7836.2007.02773.x",

language = "English",

volume = "5",

pages = "2476--83",

journal = "Journal of Thrombosis and Haemostasis",

issn = "1538-7933",

publisher = "Elsevier B.V.",

number = "12",

}

TY - JOUR

T1 - hTRPC1-associated alpha-actinin, and not hTRPC1 itself, is tyrosine phosphorylated during human platelet activation

AU - Redondo, P C

AU - Harper, A G S

AU - Harper, M T

AU - Brownlow, S L

AU - Rosado, J A

AU - Sage, S O

PY - 2007/12

Y1 - 2007/12

N2 - Canonical transient receptor potential channels (TRPCs), which are regulated by several processes, including tyrosine phosphorylation, are candidates for the conduction of store-operated Ca(2+) entry (SOCE).

AB - Canonical transient receptor potential channels (TRPCs), which are regulated by several processes, including tyrosine phosphorylation, are candidates for the conduction of store-operated Ca(2+) entry (SOCE).

KW - Thrombin

KW - Phosphotyrosine

KW - Humans

KW - Actinin

KW - Immunoprecipitation

KW - Tyrosine

KW - Protein-Tyrosine Kinases

KW - Platelet Activation

KW - Enzyme Inhibitors

KW - Membrane Proteins

KW - Blood Platelets

KW - Blotting, Western

KW - Neoplasm Proteins

KW - Multiprotein Complexes

KW - Phosphorylation

KW - TRPC Cation Channels

KW - Quinolines

KW - Time Factors

KW - Protein Tyrosine Phosphatase, Non-Receptor Type 6

KW - Calcium Signaling

U2 - 10.1111/j.1538-7836.2007.02773.x

DO - 10.1111/j.1538-7836.2007.02773.x

M3 - Article (Academic Journal)

C2 - 17892531

SN - 1538-7933

VL - 5

SP - 2476

EP - 2483

JO - Journal of Thrombosis and Haemostasis

JF - Journal of Thrombosis and Haemostasis

IS - 12

ER -

hTRPC1-associated alpha-actinin, and not hTRPC1 itself, is tyrosine phosphorylated during human platelet activation

Abstract

Keywords

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