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. 2001 Jan;11(1):65-73.
doi: 10.1093/glycob/11.1.65.

Human homologs of the Xenopus oocyte cortical granule lectin XL35

J K Lee  1 , J Schnee, M Pang, M Wolfert, L G Baum, K W Moremen, M Pierce
Affiliations

Human homologs of the Xenopus oocyte cortical granule lectin XL35

J K Lee et al. Glycobiology. 2001 Jan.

Abstract

The cDNAs encoding two human homologs of the Xenopus oocyte lectin, XL35, were isolated from a small intestine cDNA library and termed HL-1 and HL-2. The deduced amino acid sequence of each homolog is about 60% identical and 80% similar to that of XL35, and none of these sequences contains the C-type lectin motif, although it is known that XL35 requires calcium for ligand binding. By Northern analysis, HL-1 transcripts are present at relatively high levels in heart, small intestine, colon, thymus, ovary, and testis. HL-2 transcripts, by contrast, are expressed only in small intestine. Immunocytochemistry using a polyclonal antibody produced against XL35 shows HL-1 protein to be localized exclusively in endothelial cells in colon, thymus, liver, and other tissues. Primary cultures of human aortic endothelial cells are positive for HL-1 expression by immunoblotting and by PCR analysis, but several other human cell types are not. HL-1 and -2 are both encoded at chromosome 1q23, the same locus that encodes the selectins. XL35, HL-1 and -2, and another mouse homolog are members of a new family of proteins whose members most likely perform diverse functions.

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