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Paul Lyons, E. Benveniste (1998)
Cleavage of membrane‐associated ICAM‐1 from astrocytes: Involvement of a metalloproteaseGlia, 22
S. Nadanaka, C. Sato, K. Kitajima, K. Katagiri, S. Irie, T. Yamagata (2001)
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M. Mühlenhoff, A. Manegold, M. Windfuhr, Birgit Gotza, R. Gerardy-Schahn (2001)
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James Bloom, Melanie Madanat, M. Ray (1996)
Cell line and site specific comparative analysis of the N-linked oligosaccharides on human ICAM-1des454-532 by electrospray ionization mass spectrometry.Biochemistry, 35 6
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Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels.Analytical chemistry, 68 5
Yuting Yang, C. Jun, Jin‐huan Liu, Rong-guang Zhang, A. Joachimiak, T. Springer, Jia-huai Wang (2004)
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sICAM-1 and TNF-alpha
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HP-IEC, high-performance ion-exchange chromatography
AB, 2-aminobenzamide
P. Stanley, W. Chaney (1985)
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matrix-assisted laser desorption ionizationtime of flight
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Bernhard Kuster, Matthias Mann (1999)
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Karen Lee, Xiaoying Jin, Kate Zhang, Lorraine Copertino, L. Andrews, J. Baker-Malcolm, Laura Geagan, Huawei Qiu, K. Seiger, D. Barngrover, J. McPherson, T. Edmunds (2003)
A biochemical and pharmacological comparison of enzyme replacement therapies for the glycolipid storage disorder Fabry disease.Glycobiology, 13 4
A. Dell, H. Morris (2001)
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J. Millán, A. Ridley (2005)
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D. Jiménez, P. Roda-Navarro, T. Springer, J. Casasnovas (2005)
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Mac-1, macrophage antigen-1
Zenta Yasukawa, C. Sato, Kotone Sano, H. Ogawa, K. Kitajima (2006)
Identification of disialic acid-containing glycoproteins in mouse serum: a novel modification of immunoglobulin light chains, vitronectin, and plasminogen.Glycobiology, 16 7
Zenta Yasukawa, C. Sato, K. Kitajima (2005)
Inflammation-dependent changes in α2,3-, α2,6-, and α2,8-sialic acid glycotopes on serum glycoproteins in miceGlycobiology, 15
L. Klickstein, M. York, A. Fougerolles, T. Springer (1996)
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D. Meyer, Michael Dustin, C. Carron (1995)
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sICAM‐1 and TNF‐α induce MIP‐2 with distinct kinetics in astrocytes and brain microvascular endothelial cellsJournal of Neuroscience Research, 60
LFA-1, leukocyte functionassociated antigen-1
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Upregulation of ICAM‐1 and MCP‐1 but not of MIP‐2 and sensorimotor deficit in response to traumatic axonal injury in ratsJournal of Neuroscience Research, 63
IAA, iodoacetamide; ICAM-1, intercellular adhesion molecule-1
Michael Dustin, R. Rothlein, A. Bhan, C. Dinarello, T. Springer (1986)
Induction by IL 1 and interferon-gamma: tissue distribution, biochemistry, and function of a natural adherence molecule (ICAM-1).Journal of immunology, 137 1
J. Biol. Chem
Intercellular adhesion molecule-1 (ICAM-1) is a heavily N‐glycosylated transmembrane protein comprising five extracellular Ig-like domains. The soluble isoform of ICAM-1 (sICAM-1), consisting of its extracellular part, is elevated in the cerebrospinal fluid of patients with severe brain trauma. In mouse astrocytes, recombinant mouse sICAM-1 induces the production of the CXC chemokine macrophage inflammatory protein-2 (MIP-2). MIP-2 induction is glycosylation dependent, as it is strongly enhanced when sICAM-1 carries sialylated, complex-type N-glycans as synthesized by wild-type Chinese hamster ovary (CHO) cells. The present study was aimed at elucidating the N-glycosylation of mouse sICAM-1 expressed in wild-type CHO cells with regard to sialylation, N-glycan profile, and N-glycosylation sites. Ion-exchange chromatography and matrix-assisted laser desorption ionization time-of-flight (MALDI-TOF) mass spectrometry (MS) of the released N-glycans showed that sICAM-1 mostly carried di- and trisialylated complex-type N-glycans with or without one fucose. In some sialylated N-glycans, one N-acetylneuraminic acid was replaced by N-glycolylneuraminic acid, and ∼4% carried a higher number of sialic acid residues than of antennae. The N-glycosylation sites of mouse sICAM-1 were analyzed by MALDI-Fourier transform ion cyclotron resonance (FTICR)-MS and nanoLC-ESI-FTICR-MS of tryptic digests of mouse sICAM-1 expressed in the Lec1 mutant of CHO cells. All nine consensus sequences for N-glycosylation were found to be glycosylated. These results show that the N-glycans that enhance the MIP-2‐inducing activity of mouse sICAM-1 are mostly di- and trisialylated complex-type N-glycans including a small fraction carrying more sialic acid residues than antennae and that the nine N-glycosylation sites of mouse sICAM-1 are all glycosylated.
Glycobiology – Oxford University Press
Published: Nov 28, 2006
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