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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
2
|
| pubmed:dateCreated |
1996-3-25
|
| pubmed:abstractText |
The structure and the activity of urinary soluble TNF receptor type 1 (sTNF-R1), isolated from the urine of normal individuals, has been characterized and compared with that of recombinant sTNF-R1 expressed in CHO cells and with that of a nonglycosylated form expressed in Escherichia coli. Urinary sTNF-R1 was resolved in a major band of 31-33 kD and in a 48 kD band (less than 5% of total) by reducing SDS-PAGE; CHO sTNF-R1 was resolved in two bands of 29 and 31 kD. All bands were recognized by various anti-sTNF-R1 antibodies as well as by TNF-alpha in western and ligand blotting assays. No cross-reaction was observed with anti-TNF-R2 antibodies. N- and O-glycosylation studies indicated that (1) the 29-31 kD recombinant form as well as the 31-33 kD urinary form are N-glycosylated; (2) the differences between the 29-31 and 31-33 kD recombinant and natural products are mainly related to differences in the N-linked sugar content; and (3) the 48 kD sTNF-R1 isolated from urine also contains O-linked sugars. The urinary sTNF-R1 antigen mixture was able to inhibit TNF-alpha cytotoxicity with a potency comparable to that of nonglycosylated E. coli sTNF-R1. At variance, urinary sTNF-R1 was able to inhibit TNF-beta sevenfold more efficiently than E. coli sTNF-R1. In conclusion, two subtypes of sTNF-R1 have been isolated from urine: a main N-glycosylated form of 31-33 kD and a N- and O-glycosylated form of 48 kD that appears to be a minor constituent of the urinary sTNF-R1 antigen.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD,
http://linkedlifedata.com/resource/pubmed/chemical/Lymphotoxin-alpha,
http://linkedlifedata.com/resource/pubmed/chemical/Nitrogen,
http://linkedlifedata.com/resource/pubmed/chemical/Oxygen,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Tumor Necrosis Factor,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Tumor Necrosis Factor...,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Tumor Necrosis Factor-alpha
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Feb
|
| pubmed:issn |
1079-9907
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
15
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
143-52
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:8590318-Animals,
pubmed-meshheading:8590318-Antigens, CD,
pubmed-meshheading:8590318-Blotting, Western,
pubmed-meshheading:8590318-CHO Cells,
pubmed-meshheading:8590318-Cells, Cultured,
pubmed-meshheading:8590318-Cricetinae,
pubmed-meshheading:8590318-Cytotoxicity Tests, Immunologic,
pubmed-meshheading:8590318-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:8590318-Escherichia coli,
pubmed-meshheading:8590318-Glycosylation,
pubmed-meshheading:8590318-Humans,
pubmed-meshheading:8590318-Lymphotoxin-alpha,
pubmed-meshheading:8590318-Mice,
pubmed-meshheading:8590318-Nitrogen,
pubmed-meshheading:8590318-Oxygen,
pubmed-meshheading:8590318-Receptors, Tumor Necrosis Factor,
pubmed-meshheading:8590318-Receptors, Tumor Necrosis Factor, Type I,
pubmed-meshheading:8590318-Recombinant Proteins,
pubmed-meshheading:8590318-Tumor Necrosis Factor-alpha,
pubmed-meshheading:8590318-Urine
|
| pubmed:year |
1995
|
| pubmed:articleTitle |
Identification of two forms (31-33 and 48 kD) of the urinary soluble p55 tumor necrosis factor receptor that are differentially N- and O-glycosylated.
|
| pubmed:affiliation |
Molecular Immunology and Biochemistry Unit, Tecnogen ScpA, Piana di Monte Verna, Italy.
|
| pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
|