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Vol. 13, Issue 8, 2853-2868, August 2002
Department of Biochemistry and Molecular Biology, University of
Oklahoma Health Sciences Center, Oklahoma City, Oklahoma 73190
We recently purified the rat liver hyaluronan receptor for
endocytosis (HARE) and found abundant expression of 175- and ~300-kDa HARE species in sinusoidal endothelial cells of the liver,
spleen, and lymph nodes. We report herein the first cloning and
functional expression of the rat 175-kDa HARE. Peptide sequences were
obtained from the purified 175-kDa HARE, and degenerate oligonucleotide primers were designed for reverse transcription-polymerase chain reaction and cDNA cloning. Results of 5'-rapid amplification of cDNA
ends, Northern analysis, N-terminal sequence, and antibody reactivity
analyses indicated the absence of mRNA directly encoding the 175-kDa
HARE. This protein is most likely derived from a larger precursor.
Accordingly, we constructed an artificial 4.7-kb cDNA encoding the 1431 amino acid 175-kDa HARE. The predicted type I membrane protein has a
mass of 156,393 Da and a pI of 7.86. The 175-kDa HARE cDNA, fused to
the N-terminal leader sequence of the Ig 
-chain, was transfected
transiently into COS-7 cells and stably into SK-Hep-1 cells,
respectively, to assess hyaluronan or hyaluronic acid (HA)-binding
activity and endocytosis. In both cases, HARE expression and HA-binding
activity were detected. Furthermore, stable SK-175HARE cells
demonstrated specific endocytosis of 125I-HA and receptor
recycling. Fluorescence-activated cell sorting analysis confirmed that
recombinant HARE was expressed on the cell surface and that fluorescent
HA uptake was inhibited by a specific blocking monoclonal antibody
against HARE. Additionally, HARE was substantially colocalized with
clathrin, but not with internalized HA that was delivered to lysosomes.
The results confirm that recombinant 175-kDa HARE is an authentic
endocytic receptor for HA and that this receptor can function
independently of the ~300-kDa HARE. HARE is the first functionally
identified member of a protein family that shares a similar
organization of Fasciclin, epidermal growth factor-like, Xlink, and
transmembrane domains.
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