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J. Cell Biol.,
Volume 144, Number 4, February 22, 1999 789-801
* University of Oxford, Molecular Immunology Group, Nuffield Department of Medicine and The extracellular matrix glycosaminoglycan
hyaluronan (HA) is an abundant component of skin
and mesenchymal tissues where it facilitates cell migration during wound healing, inflammation, and em-
bryonic morphogenesis. Both during normal tissue
homeostasis and particularly after tissue injury, HA is
mobilized from these sites through lymphatic vessels to
the lymph nodes where it is degraded before entering
the circulation for rapid uptake by the liver. Currently,
however, the identities of HA binding molecules which
control this pathway are unknown. Here we describe
the first such molecule, LYVE-1, which we have identified as a major receptor for HA on the lymph vessel
wall. The deduced amino acid sequence of LYVE-1
predicts a 322-residue type I integral membrane
polypeptide 41% similar to the CD44 HA receptor with
a 212-residue extracellular domain containing a single
Link module the prototypic HA binding domain of the
Link protein superfamily. Like CD44, the LYVE-1 molecule binds both soluble and immobilized HA.
However, unlike CD44, the LYVE-1 molecule colocalizes with HA on the luminal face of the lymph vessel
wall and is completely absent from blood vessels. Hence, LYVE-1 is the first lymph-specific HA receptor
to be characterized and is a uniquely powerful marker
for lymph vessels themselves.
Department of Cellular Science,
John Radcliffe Hospital, Headington, Oxford OX3 9DU, United Kingdom; § Department of Anatomy, University of Kuopio,
FIN-70211 Kuopio, Finland; and Human Genome Sciences, Inc., Rockville, Maryland 20850
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