What question did this study set out to answer?

Summarize the molecular mechanisms and physiological importance of beta3 tyrosine phosphorylation in alphaIIbbeta3 outside-in integrin signaling during platelet activation.

January 1, 2001Thrombosis and Haemostasis

β3 Tyrosine Phosphorylation in αIIbβ3 (Platelet Membrane GP IIb-IIIa) Outside-in Integrin Signaling

View Full Paper

Ask AI

Bookmark

Authors

LNLisa Nannizzi‐Alaimo KPK. S. Srinivasa Prasad DPDavid R. Phillips

Discussion

Member takes

Overview

Narrative review reveals impaired clot stability and rebleeding from defective beta3 phosphorylation in mutant mice, indicating its essential role in integrin outside-in signaling.

Key Points

Summarize the molecular mechanisms and physiological importance of beta3 tyrosine phosphorylation in alphaIIbbeta3 outside-in integrin signaling during platelet activation.
Reviewed biochemical pathways governing tyrosine phosphorylation within the beta3 integrin cytoplasmic tyrosine (ICY) domain upon platelet aggregation and adhesion to immobilized fibrinogen.
Evaluated functional phenotypes from the diYF mouse model harboring tyrosine-to-phenylalanine mutations at the two beta3 ICY phosphorylation sites.
Tyrosine phosphorylation of the beta3 ICY domain specifically recruits the cytoskeletal protein myosin to mediate clot retraction and the adapter protein Shc to mediate downstream platelet stimulation.
diYF mutant mice exhibit selective impairment in outside-in signaling, displaying defective in vitro aggregation and clot retraction alongside an in vivo bleeding phenotype marked by frequent rebleeding.

Cite This Study

Nannizzi‐Alaimo et al. (2001) studied this question.

synapsesocial.com/papers/6a6f6c01f44fa9f079dcdc19 https://doi.org/10.1055/s-0037-1616222

View Full Paper

Ask AI

Bookmark

January 1, 2001Thrombosis and Haemostasis

β3 Tyrosine Phosphorylation in αIIbβ3 (Platelet Membrane GP IIb-IIIa) Outside-in Integrin Signaling

View Full Paper

Ask AI

Bookmark

Authors

LNLisa Nannizzi‐Alaimo KPK. S. Srinivasa Prasad DPDavid R. Phillips

Discussion

Member takes

Overview

Narrative review reveals impaired clot stability and rebleeding from defective beta3 phosphorylation in mutant mice, indicating its essential role in integrin outside-in signaling.

Key Points

Summarize the molecular mechanisms and physiological importance of beta3 tyrosine phosphorylation in alphaIIbbeta3 outside-in integrin signaling during platelet activation.
Reviewed biochemical pathways governing tyrosine phosphorylation within the beta3 integrin cytoplasmic tyrosine (ICY) domain upon platelet aggregation and adhesion to immobilized fibrinogen.
Evaluated functional phenotypes from the diYF mouse model harboring tyrosine-to-phenylalanine mutations at the two beta3 ICY phosphorylation sites.
Tyrosine phosphorylation of the beta3 ICY domain specifically recruits the cytoskeletal protein myosin to mediate clot retraction and the adapter protein Shc to mediate downstream platelet stimulation.
diYF mutant mice exhibit selective impairment in outside-in signaling, displaying defective in vitro aggregation and clot retraction alongside an in vivo bleeding phenotype marked by frequent rebleeding.

Cite This Study

Nannizzi‐Alaimo et al. (2001) studied this question.

synapsesocial.com/papers/6a6f6c01f44fa9f079dcdc19 https://doi.org/10.1055/s-0037-1616222

Also Consider

Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context:

View Full Paper

Ask AI

Bookmark