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Comment
. 1999 Oct;155(4):1013-20.
doi: 10.1016/S0002-9440(10)65201-7.

Endothelial ligands for L-selectin: from lymphocyte recirculation to allograft rejection

Comment

Endothelial ligands for L-selectin: from lymphocyte recirculation to allograft rejection

S D Rosen. Am J Pathol. 1999 Oct.
No abstract available

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Figures

Figure 1.
Figure 1.
Model of lymph node HEV ligands for L-selectin. Four sialomucins are shown. GlyCAM-1, CD34, and Sgp200 have been identified in mouse lymph node. CD34, podocalyxin, and Sgp200 have been identified in human tonsils. All of these components are recognized by MECA-79. The complex, defined by purification with MECA-79, is referred as the peripheral node addressin (PNAd). The cDNA encoding Sgp200 (sulfated glycoprotein of 200 kd) has not been cloned as yet. The white circles denote the posttranslational modifications of these ligands including sialylation, fucosylation, and sulfation. CD34 and podocalyxin share the same overall structural organization, each having an amino-terminal mucin domain, a presumed globular domain with cysteines, a transmembrane domain, and a cytoplasmic tail. There is significant sequence homology in the cytoplasmic tails.
Figure 2.
Figure 2.
Sulfated O-linked chains of GlyCAM-1. Oligosaccharides bearing the 6′-sulfo sLex and 6-sulfo sLex tetrasaccharide capping groups (Table 2) ▶ are shown. They extend from the core 2 branch, indicated by a box. The monosulfated heptasaccharide structures, which occur in equal amounts, represent <25% of the O-linked chains in GlyCAM-1. The other structures, which have not been defined, are more complex. Some of these are larger than heptasaccharides and at least half contain more than one sulfate modification per chain. Among the more complex chains, the 6′,6-disulfo sLex capping group is a candidate structure but has not yet been demonstrated.

Comment on

References

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