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Defective N-sulfation of heparan sulfate proteoglycans limits PDGF-BB binding and pericyte recruitment in vascular development.

Abstract：

:During vascular development, endothelial platelet-derived growth factor B (PDGF-B) is critical for pericyte recruitment. Deletion of the conserved C-terminal heparin-binding motif impairs PDGF-BB retention and pericyte recruitment in vivo, suggesting a potential role for heparan sulfate (HS) in PDGF-BB function during vascular development. We studied the participation of HS chains in pericyte recruitment using two mouse models with altered HS biosynthesis. Reduction of N-sulfation due to deficiency in N-deacetylase/N-sulfotransferase-1 attenuated PDGF-BB binding in vitro, and led to pericyte detachment and delayed pericyte migration in vivo. Reduced N-sulfation also impaired PDGF-BB signaling and directed cell migration, but not proliferation. In contrast, HS from glucuronyl C5-epimerase mutants, which is extensively N- and 6-O-sulfated, but lacks 2-O-sulfated L-iduronic acid residues, retained PDGF-BB in vitro, and pericyte recruitment in vivo was only transiently delayed. These observations were supported by in vitro characterization of the structural features in HS important for PDGF-BB binding. We conclude that pericyte recruitment requires HS with sufficiently extended and appropriately spaced N-sulfated domains to retain PDGF-BB and activate PDGF receptor beta (PDGFRbeta) signaling, whereas the detailed sequence of monosaccharide and sulfate residues does not appear to be important for this interaction.

journal_name

Genes Dev

journal_title

Genes & development

authors

Abramsson A,Kurup S,Busse M,Yamada S,Lindblom P,Schallmeiner E,Stenzel D,Sauvaget D,Ledin J,Ringvall M,Landegren U,Kjellén L,Bondjers G,Li JP,Lindahl U,Spillmann D,Betsholtz C,Gerhardt H

doi

10.1101/gad.398207

subject

Has Abstract

pub_date

2007-02-01 00:00:00

pages

316-31

issue

3

eissn

0890-9369

issn

1549-5477

pii

21/3/316

journal_volume

21

pub_type

杂志文章

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