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Protein Modifications in the RER

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Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
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Structure and Function of Platelets

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Regulation of the Unfolded Protein Response

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The Unfolded Protein Response

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The ER is the hub of protein synthesis in a cell. It has robust systems to quality control protein folding and also for degradation of terminally misfolded proteins. Under normal conditions, a small proportion of misfolded proteins that cannot be salvaged need to be transported to the cytoplasm by the ER-associated degradation or ERAD pathways. However, if the ERAD cannot handle the misfolded proteins, the cell activates the unfolded protein response or UPR to adjust the protein folding...

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Related Experiment Video

Updated: May 26, 2026

Procoagulant Platelet Characterization by Measuring Phosphatidylserine Exposure and Microvesicle Release from Human Purified Platelets

Procoagulant Platelet Characterization by Measuring Phosphatidylserine Exposure and Microvesicle Release from Human Purified Platelets

Published on: November 29, 2024

The platelet-surface thiol isomerase enzyme ERp57 modulates platelet function.

L-M Holbrook¹, P Sasikumar, R G Stanley

¹Institute for Cardiovascular and Metabolic Research, School of Biological Sciences, University of Reading, Berkshire, UK. lisa.holbrook@path.ox.ac.uk

Journal of Thrombosis and Haemostasis : JTH

|December 16, 2011

Summary

This summary is machine-generated.

ERp57, a cell surface thiol isomerase, is crucial for platelet function, including aggregation and thrombus formation. Its inhibition significantly reduces arterial thrombus development in mice.

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Last Updated: May 26, 2026

Procoagulant Platelet Characterization by Measuring Phosphatidylserine Exposure and Microvesicle Release from Human Purified Platelets

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Published on: November 29, 2024

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Assessing Cellular Target Engagement by SHP2 (PTPN11) Phosphatase Inhibitors

Assessing Cellular Target Engagement by SHP2 (PTPN11) Phosphatase Inhibitors

Published on: July 17, 2020

Area of Science:

Biochemistry
Hematology
Cell Biology

Background:

Thiol isomerases are endoplasmic reticulum enzymes regulating protein disulfide bonds.
Previous research highlighted PDI and ERp5 roles in platelet function.

Purpose of the Study:

Investigate the role of ERp57, a newly identified platelet surface thiol isomerase, in regulating platelet function.

Main Methods:

Utilized enzyme activity-blocking antibodies to assess ERp57 function.
Observed effects on platelet aggregation, secretion, fibrinogen binding, and calcium mobilization.
Studied ERp57 in vivo using a murine model of arterial thrombosis induced by laser injury.

Main Results:

ERp57 inhibition impaired platelet aggregation, dense granule secretion, fibrinogen binding, and calcium mobilization.
ERp57 was detected in developing thrombi in vivo.
Inhibition of ERp57 reduced arterial thrombus formation in a mouse model.

Conclusions:

ERp57 plays a significant role in normal platelet function.
Cell surface thiol isomerases may broadly regulate hemostasis and thrombosis.