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PSGL-1 function in immunity and steady state homeostasis.

Douglas A Carlow¹, Klaus Gossens, Silvia Naus

¹The Biomedical Research Centre, University of British Columbia, Vancouver, British Columbia, Canada.

Immunological Reviews

|July 15, 2009

Summary

P-selectin glycoprotein ligand 1 (PSGL-1) is crucial for leukocyte trafficking, with O-glycan modifications influencing its role in both inflammation and homeostasis. Understanding PSGL-1 glycosylation is key to its diverse functions in the immune system.

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Area of Science:

Immunology
Cell Biology
Glycobiology

Background:

P-selectin glycoprotein ligand 1 (PSGL-1) is vital for leukocyte trafficking, initially identified as a selectin ligand.
Its extracellular mucin domain, with branched O-glycan extensions, mediates leukocyte rolling via selectin interactions.
PSGL-1 supports leukocyte recruitment in both innate and adaptive immunity.

Purpose of the Study:

To review current knowledge and identify gaps in understanding PSGL-1 glycosylation in T cells.
To update the understanding of PSGL-1's functional scope beyond inflammation.
To elucidate the role of O-glycans in PSGL-1's dual functions in inflammatory and homeostatic settings.

Main Methods:

Literature review and synthesis of existing research on PSGL-1 structure, function, and glycosylation.
Analysis of PSGL-1's interaction with selectins and chemokines.
Comparison of PSGL-1 glycosylation patterns in different cell types (neutrophils vs. T cells).

Main Results:

PSGL-1's O-glycans are essential for selectin-mediated leukocyte rolling during inflammation.
PSGL-1 also binds homeostatic chemokines (CCL19, CCL21) for T-cell homing.
Inflammatory O-glycan modifications can hinder binding to homeostatic chemokines, impacting steady-state T-cell traffic.

Conclusions:

The O-glycosylation of PSGL-1 is a critical determinant of its function in both inflammatory and homeostatic cell trafficking.
While PSGL-1's role in inflammation is well-studied, its regulation and function in homeostasis, particularly in T cells, require further investigation.
Targeting PSGL-1 glycosylation may offer therapeutic potential for immune cell trafficking disorders.