title: Matrix metalloproteinases of human NK cells.
abstract: We have previously reported that MMP-2 and MMP-9 are present in rat A-NK cells, and have recently documented that additional MMPs are present in rodent A-NK cells. To our knowledge only proMMP-9 has previously been reported for human NK and A-NK cells. Herein, we report for the first time the presence of MMP-2 and MT1-MMP in human NK cells. The importance of these enzymes for the migration of A-NK cells into tumor metastases is of great potential relevance. MMPs may be rate limiting in A-NK cells, following their adoptive transfer, to traverse basement membrane and accumulate within established cancer metastases, a likely pre-requisite to their cytolytic function. Human NK cells express and produce MMP-2, MMP-9, MT1-MMP and the inhibitor TIMP-1. Moreover, human A-NK cells degrade the extracellular matrix equivalent (Matrigel) in a seemingly IL-2 dependent manner. It is therefore likely that A-NK cell MMPs play crucial roles in contributing to A-NK cell localisation and positioning the cells in vivo to allow for triggering their cytolytic potential.
authors.affiliation: Department of Anatomy and Cell Biology, University of Göteborg, Sweden.
authors.forename: P
authors.initials: P
authors.lastname: Albertsson
authors.forename: M H
authors.initials: MH
authors.lastname: Kim
authors.forename: L E
authors.initials: LE
authors.lastname: Jonges
authors.forename: R P
authors.initials: RP
authors.lastname: Kitson
authors.forename: P J
authors.initials: PJ
authors.lastname: Kuppen
authors.forename: B R
authors.initials: BR
authors.lastname: Johansson
authors.forename: U
authors.initials: U
authors.lastname: Nannmark
authors.forename: R H
authors.initials: RH
authors.lastname: Goldfarb
mesh_terms: D015153:Blotting, Western; D002460:Cell Line; D002465:Cell Movement / Q000187:drug effects; D003094:Collagen; D004338:Drug Combinations; D005434:Flow Cytometry; D015971:Gene Expression Regulation, Enzymologic; D006801:Humans; D007376:Interleukin-2 / Q000494:pharmacology; D007694:Killer Cells, Natural / Q000166:cytology / Q000201:enzymology*; D007797:Laminin; D020778:Matrix Metalloproteinase 2 / Q000235:genetics / Q000378:metabolism*; D020780:Matrix Metalloproteinase 9 / Q000235:genetics / Q000378:metabolism; D061965:Matrix Metalloproteinase Inhibitors; D053504:Matrix Metalloproteinases, Membrane-Associated; D008666:Metalloendopeptidases / Q000037:antagonists & inhibitors / Q000235:genetics / Q000378:metabolism*; D010649:Phenylalanine / Q000031:analogs & derivatives / Q000494:pharmacology; D011480:Protease Inhibitors / Q000494:pharmacology; D011509:Proteoglycans; D012333:RNA, Messenger / Q000235:genetics; D013876:Thiophenes / Q000494:pharmacology; D019715:Tissue Inhibitor of Metalloproteinase-1 / Q000235:genetics / Q000378:metabolism; D014407:Tumor Cells, Cultured
chemical_list: D004338:Drug Combinations; D007376:Interleukin-2; D007797:Laminin; D061965:Matrix Metalloproteinase Inhibitors; D011480:Protease Inhibitors; D011509:Proteoglycans; D012333:RNA, Messenger; D013876:Thiophenes; D019715:Tissue Inhibitor of Metalloproteinase-1; C059485:matrigel; D010649:Phenylalanine; D003094:Collagen; C080985:batimastat; D053504:Matrix Metalloproteinases, Membrane-Associated; D008666:Metalloendopeptidases; D020778:Matrix Metalloproteinase 2; D020780:Matrix Metalloproteinase 9