Document Detail


Terminal sialic acid residues on human glycophorin A are recognized by porcine kupffer cells.
MedLine Citation:
PMID:  16082330     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
BACKGROUND: 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. METHODS: Human erythrocytes were tested for ABO and MN specificity and used as targets in a 51Chromium quantitative erythrocyte rosette assay. Monosaccharides present on human glycophorin A, neuraminyl lactoses, bovine and porcine submaxillary mucins (BSM and PSM), and hyaluronic acid as well as proteoglycan N-linked glycosidase F(PNGaseF)- and sialidase A-treated human erythrocyte glycoproteins (hEGP) and human erythrocytes were all tested for inhibitory potential in the rosetting assay. RESULTS: Porcine Kupffer-cell recognition of human erythrocytes was insensitive to differences in blood groups A, B, O, or MN. At 30 mM, the monosaccharide, N-acetylneuraminic acid, and the trisaccharide mixture, neuraminyl lactoses, disrupted human erythrocyte recognition by 25% and 30%, respectively. A dilution of BSM but not PSM inhibited the rosetting assay by 17% (.2 mg/mL), 33% (1 mg/mL), and 53% (2 mg/mL). The same dilution of hyaluronic acid had no effect on rosetting. Removal of N-linked oligosaccharides from hEGP with PNGaseF did not impair its ability to inhibit the rosetting assay. In contrast, removal of sialic acid completely abrogated its inhibitory ability. Treatment of whole human erythrocytes with sialidase A likewise prevented recognition by porcine Kupffer cells. CONCLUSIONS: Terminal sialic acid on human erythrocytes is a target recognized by porcine Kupffer cells, suggesting a role for a sialic-acid receptor in innate cellular recognition of xenogeneic epitopes. Inasmuch as this work reveals a carbohydrate-recognition mechanism for cellular rejection, we shed light on a potential new boundary that will need to be overcome within xenotransplantation.
Authors:
Christopher Burlak; Lisa M Twining; Michael A Rees
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Transplantation     Volume:  80     ISSN:  0041-1337     ISO Abbreviation:  Transplantation     Publication Date:  2005 Aug 
Date Detail:
Created Date:  2005-08-05     Completed Date:  2005-08-31     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0132144     Medline TA:  Transplantation     Country:  United States    
Other Details:
Languages:  eng     Pagination:  344-52     Citation Subset:  IM    
Affiliation:
Department of Urology, Medical College of Ohio, Toledo, OH, USA. Cburlak@niaid.nih.gov
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MeSH Terms
Descriptor/Qualifier:
ABO Blood-Group System
Animals
Carbohydrates / chemistry
Cattle
Dose-Response Relationship, Drug
Erythrocytes / metabolism
Glycophorin / chemistry*
Glycoproteins / chemistry
Graft Rejection
Humans
Hyaluronic Acid / chemistry
Kupffer Cells / cytology,  metabolism*
Lactose / chemistry
Monosaccharides / chemistry
Mucins / chemistry
N-Acetylneuraminic Acid / chemistry*,  metabolism
Neuraminidase / chemistry
Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase / chemistry
Protein Binding
Species Specificity
Swine
Transplantation, Heterologous / methods*
Chemical
Reg. No./Substance:
0/ABO Blood-Group System; 0/Carbohydrates; 0/Glycophorin; 0/Glycoproteins; 0/Monosaccharides; 0/Mucins; 131-48-6/N-Acetylneuraminic Acid; 63-42-3/Lactose; 9004-61-9/Hyaluronic Acid; EC 3.2.1.18/Neuraminidase; EC 3.5.1.52/Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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