http://rdf.ncbi.nlm.nih.gov/pubchem/patent/KR-100533911-B1
Outgoing Links
| Predicate | Object |
|---|---|
| classificationCPCInventive | http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12N9-0022 http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12N9-0012 http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C07K14-705 |
| classificationIPCInventive | http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C07K14-47 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C07K14-435 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C07K14-705 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N1-21 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N1-19 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N1-15 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N15-09 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N9-06 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N5-10 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/G01N33-68 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12P21-02 |
| filingDate | 1998-05-22-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| grantDate | 2005-12-06-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| publicationDate | 2005-12-06-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| publicationNumber | KR-100533911-B1 |
| titleOfInvention | Vascular adhesion protein-1 having amine oxidase activity |
| abstract | The present invention relates to VAP-1, wherein VAP-1 is an endothelial sialoglycoprotein and its cell surface expression is induced under inflammatory conditions. It has already been shown to mediate binding of recycle lymphocytes to human peripheral lymph node vascular endothelial cells in L-selectin independent form. VAP-1 cDNA was purified to encode an 84.6 KD type II transmembrane protein with a single transmembrane region located at the N-terminal end of the molecule. VAP-1 is located in the region of the cell with three putative O-glycosylation sites in vivo, mainly six dimers of 170-180KD dimer. VAP-1 does not have much similarity with any currently known adhesion molecule but is very identical to the copper containing amine oxidase family. Enzyme evaluation defines VAP-1 as membrane bound amine oxidase. Therefore, VAP-1 is a novel type of adhesion molecule having a dual function. Accurate inflammation settings, along with appropriate glycosylation, allow VAP-1 expression on the enema endothelial cell surface, which is in a location that mediates lymphocyte adhesion, to act as an adhesion receptor involved in a novel mechanism of lymphocyte return. The basic function at other positions depends on its inherent amine oxidase activity. |
| priorityDate | 1997-05-23-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| type | http://data.epo.org/linked-data/def/patent/Publication |
Incoming Links
Total number of triples: 1263.