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Identification and characterization of ligands for L‐selectin in the kidney. II. Expression of chondroitin sulfate and heparan sulfate proteoglycans reactive with L‐selectin
Author(s) -
Li Yong-Fei,
Kawashima Hiroto,
Watanabe Norifumi,
Miyasaka Masayuki
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)00046-0
Subject(s) - heparan sulfate , chondroitin sulfate , chemistry , biochemistry , l selectin , glycosaminoglycan , selectin , perlecan , chondroitin , cell adhesion molecule , divalent , adhesion , microbiology and biotechnology , biology , receptor , organic chemistry
Ligands for the leukocyte adhesion molecule L‐selectin are expressed not only in lymph node high endothelial venules (HEV) but also in the renal distal tubuli. Here we report that L‐selectin‐reactive molecules in the kidney are chondroitin sulfate and heparan sulfate proteoglycans of 500–1000 kDa, unlike those in HEV bearing sialyl Lewis X‐like carbohydrates. Binding of L‐selectin to these molecules was mediated by the lectin domain of L‐selectin and required divalent cations. Binding was inhibited by chondroitinase and/or heparitinase but not sialidase. Thus, L‐selectin can recognize chondroitin sulfate and heparan sulfate glycosaminoglycans structurally distinct from sialyl Lewis X‐like carbohydrates.