Open AccessTerminal Sialic Acid Residues on Human Glycophorin A Are Recognized by Porcine Kupffer Cells
Author(s) -
Christopher Burlak,
Lisa M. Twining,
Michael Rees
Publication year - 2005
Publication title -
transplantation
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.45
H-Index - 204
eISSN - 1534-6080
pISSN - 0041-1337
DOI - 10.1097/01.tp.0000162974.94890.9f
Subject(s) - glycophorin , sialic acid , sialidase , biochemistry , monosaccharide , microbiology and biotechnology , glycoprotein , chemistry , red blood cell , neuraminic acid , hyaluronic acid , neuraminidase , biology , enzyme , genetics , membrane
We have previously shown that recognition of human erythrocytes by porcine Kupffer cells is mediated by a carbohydrate-dependent mechanism. The present study explores the possible ligands existing on human glycophorin A and tests their ability to inhibit erythrocyte rosette formation.