pubmed-article:8590318 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:8590318 | lifeskim:mentions | umls-concept:C0020792 | lld:lifeskim |
pubmed-article:8590318 | lifeskim:mentions | umls-concept:C1524119 | lld:lifeskim |
pubmed-article:8590318 | lifeskim:mentions | umls-concept:C0077503 | lld:lifeskim |
pubmed-article:8590318 | lifeskim:mentions | umls-concept:C1749467 | lld:lifeskim |
pubmed-article:8590318 | lifeskim:mentions | umls-concept:C1420280 | lld:lifeskim |
pubmed-article:8590318 | lifeskim:mentions | umls-concept:C1419030 | lld:lifeskim |
pubmed-article:8590318 | lifeskim:mentions | umls-concept:C0376315 | lld:lifeskim |
pubmed-article:8590318 | pubmed:issue | 2 | lld:pubmed |
pubmed-article:8590318 | pubmed:dateCreated | 1996-3-25 | lld:pubmed |
pubmed-article:8590318 | 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. | lld:pubmed |
pubmed-article:8590318 | pubmed:language | eng | lld:pubmed |
pubmed-article:8590318 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8590318 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:8590318 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8590318 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8590318 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8590318 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8590318 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8590318 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8590318 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8590318 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8590318 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:8590318 | pubmed:month | Feb | lld:pubmed |
pubmed-article:8590318 | pubmed:issn | 1079-9907 | lld:pubmed |
pubmed-article:8590318 | pubmed:author | pubmed-author:CortiAA | lld:pubmed |
pubmed-article:8590318 | pubmed:author | pubmed-author:MariniGG | lld:pubmed |
pubmed-article:8590318 | pubmed:author | pubmed-author:CassaniGG | lld:pubmed |
pubmed-article:8590318 | pubmed:author | pubmed-author:MerliSS | lld:pubmed |
pubmed-article:8590318 | pubmed:author | pubmed-author:D'AmbrosioFF | lld:pubmed |
pubmed-article:8590318 | pubmed:author | pubmed-author:BagnascoLL | lld:pubmed |
pubmed-article:8590318 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:8590318 | pubmed:volume | 15 | lld:pubmed |
pubmed-article:8590318 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:8590318 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:8590318 | pubmed:pagination | 143-52 | lld:pubmed |
pubmed-article:8590318 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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pubmed-article:8590318 | pubmed:year | 1995 | lld:pubmed |
pubmed-article:8590318 | 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. | lld:pubmed |
pubmed-article:8590318 | pubmed:affiliation | Molecular Immunology and Biochemistry Unit, Tecnogen ScpA, Piana di Monte Verna, Italy. | lld:pubmed |
pubmed-article:8590318 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:8590318 | pubmed:publicationType | Comparative Study | lld:pubmed |
pubmed-article:8590318 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8590318 | lld:pubmed |