Metabolic Serum Profiles for Patients Receiving Allogeneic Stem
Cell Transplantation: The Pretransplant Profile Differs for
Patients with and without Posttransplant Capillary Leak Syndrome
Table 4
The importance of protein glycosylation for paracellular and transcellular transport across the endothelial cell layer.
Cellular structure and molecule
Glycosylation
References
Tight junctions
Claudin-1, -2, and -4
Two in silico studies suggest that claudins can be glycosylated, and there seems to be a functional interplay between glycosylation and phosphorylation. For claudin-1 it has been suggested that alternate phosphorylation/glycosylation on Ser192, Ser205, Ser206, and Thr191 may provide an on/off switch to regulate their assembly at tight junctions.
An in silico study suggests that human occludin can be O-β-glycosylated, and for Ser408 and Ser490 there may be a functional interplay between phosphorylation and glycosylation. The glycosylation can be altered by cellular stress.
Connexins show posttranscriptional modulations through glycosylation but also through phosphorylation, proteolysis, acetylation, nitrosylation, ubiquitination, lipidation, hydroxylation, methylation, and deamidation.
Connexin 43 is expressed by endothelium and is involved in regulation of permeability. Glycosylation of connexin 43 is important for the regulation of their biological functions; inhibition of glycosylation enhances both basal and cAMP induced junctional communication.
Modification of N-linked glycanes can affect their adhesive functions; glycosyltransferases are involved in this modulation, including acetylglucosaminyltransferases.
CD147 is an interaction partner of Caveolin-1; a significant biochemical property of CD147 is its high level of glycosylation. Glycosylation is important for its biological functions and glycosyltransferases involved in the biosynthesis of CD147 N-glycanes. Glycosylated extracellular matrix metalloproteinase inducer specifically associates with caveolin-1.
