| http://purl.uniprot.org/citations/11724793 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/11724793 | http://www.w3.org/2000/01/rdf-schema#comment | "The interaction of lymphocytes with other cells is critical for normal immune surveillance and response. MDC-L (ADAM 28), a member of the ADAM (a disintegrin and metalloprotease) protein family, is expressed on the surface of human lymphocytes. ADAMs possess a disintegrin-like domain similar in sequence to small non-enzymatic snake venom peptides that act as integrin antagonists. We report here that the disintegrin domain of MDC-L is recognized by the leukocyte integrin alpha(4)beta(1). Recombinant Fc fusion proteins possessing the disintegrin domain of MDC-L supported adhesion of the T-lymphoma cell line, Jurkat, in a concentration- and divalent cation-dependent manner. Adhesion of Jurkat cells to the disintegrin domain of MDC-L was inhibited by an anti-MDC-L monoclonal antibody (mAb), Dis1-1. The epitope for mAb Dis1-1 was localized within 59 residues of the disintegrin domain. Recombinant expression of this 59-residue fragment of the disintegrin domain also supported cell adhesion. Adhesion of Jurkat cells to the MDC-L disintegrin domain was specifically inhibited by anti-alpha(4) and anti-beta(1) function-blocking mAbs. Furthermore, adhesion of various cell lines to MDC-L correlated with expression of the integrin alpha(4)-subunit. Transfected K562 cells expressing alpha(4)beta(1) adhered to the disintegrin domain in contrast to non-transfected K562 cells. We further investigated the binding of recombinant MDC-L disintegrin domain (rDis-Fc) in solution. The rDis-Fc was found to bind to Jurkat cells in solution in a concentration-dependent and saturable manner. Both adhesion and solution binding of rDis-Fc was inhibited by the alpha(4)beta(1) ligand mimetic CS-1 peptide. Additionally, recognition of the MDC-L disintegrin domain required "activation" of lymphocyte beta(1) integrins. The interaction of MDC-L with alpha(4)beta(1) may potentially regulate metalloprotease function by targeting or sequestering the active protease on the cell surface. These results suggest a potential role for the lymphocyte ADAM, MDC-L, in the interaction of lymphocytes with alpha(4)beta(1)-expressing leukocytes."xsd:string |
| http://purl.uniprot.org/citations/11724793 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m109538200"xsd:string |
| http://purl.uniprot.org/citations/11724793 | http://purl.uniprot.org/core/author | "Bowditch R.D."xsd:string |
| http://purl.uniprot.org/citations/11724793 | http://purl.uniprot.org/core/author | "Bridges L.C."xsd:string |
| http://purl.uniprot.org/citations/11724793 | http://purl.uniprot.org/core/author | "Roberts C.M."xsd:string |
| http://purl.uniprot.org/citations/11724793 | http://purl.uniprot.org/core/author | "Tani P.H."xsd:string |
| http://purl.uniprot.org/citations/11724793 | http://purl.uniprot.org/core/author | "Hanson K.R."xsd:string |
| http://purl.uniprot.org/citations/11724793 | http://purl.uniprot.org/core/author | "Judkins M.B."xsd:string |
| http://purl.uniprot.org/citations/11724793 | http://purl.uniprot.org/core/date | "2002"xsd:gYear |
| http://purl.uniprot.org/citations/11724793 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/11724793 | http://purl.uniprot.org/core/pages | "3784-3792"xsd:string |
| http://purl.uniprot.org/citations/11724793 | http://purl.uniprot.org/core/title | "The lymphocyte metalloprotease MDC-L (ADAM 28) is a ligand for the integrin alpha4beta1."xsd:string |
| http://purl.uniprot.org/citations/11724793 | http://purl.uniprot.org/core/volume | "277"xsd:string |
| http://purl.uniprot.org/citations/11724793 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/11724793 |
| http://purl.uniprot.org/citations/11724793 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/11724793 |
| http://purl.uniprot.org/uniprot/#_A0A2R8VHR5-mappedCitation-11724793 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/11724793 |
| http://purl.uniprot.org/uniprot/#_Q60619-mappedCitation-11724793 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/11724793 |
| http://purl.uniprot.org/uniprot/#_Q71U12-mappedCitation-11724793 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/11724793 |
| http://purl.uniprot.org/uniprot/#_Q9JLN6-mappedCitation-11724793 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/11724793 |
| http://purl.uniprot.org/uniprot/#_Q8C4L9-mappedCitation-11724793 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/11724793 |
| http://purl.uniprot.org/uniprot/A0A2R8VHR5 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/11724793 |
| http://purl.uniprot.org/uniprot/Q71U12 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/11724793 |
| http://purl.uniprot.org/uniprot/Q8C4L9 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/11724793 |
| http://purl.uniprot.org/uniprot/Q60619 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/11724793 |