Zymographic analysis of extracellular, released and cell-associated proteases of rat interleukin 2-activated natural killer (A-NK) cells.
The biochemical properties of heretofore uncharacterized extracellular proteases of rat interleukin-2-activated natural killer (A-NK) cells were investigated. Following p-aminobenzamidine- and D-phenylalanine-agarose affinity chromatography both trypsin- and chymotrypsin-like protease activities were found. Zymography revealed "trypsin-like" activities, with apparent molecular weights of approximately 42 kDa to 20.5 kDa, and "chymotrypsin-like" activities of approximately 27 kDa, to 22 kDa. These proteases might contribute to diverse NK cell functions, and the characteristics of these proteolytic activities are compared with those of granzymes of lytic granules and the proteasome of A-NK cells.
Wasserman
K
K
Department of Radiation Oncology, University of Pittsburgh School of Medicine, PA 15213.
Kitson
R P
RP
Gabauer
M K
MK
Miller
C A
CA
Herberman
R B
RB
Goldfarb
R H
RH
D000818:Animals; D002478:Cells, Cultured; D002846:Chromatography, Affinity; D004591:Electrophoresis, Polyacrylamide Gel; D010450:Endopeptidases / Q000032:analysis / Q000302:isolation & purification / Q000378:metabolism*; D004792:Enzyme Precursors / Q000032:analysis / Q000302:isolation & purification / Q000378:metabolism*; D053804:Granzymes; D007376:Interleukin-2 / Q000494:pharmacology*; D007694:Killer Cells, Natural / Q000187:drug effects / Q000201:enzymology* / Q000276:immunology; D008213:Lymphocyte Activation / Q000187:drug effects / Q000502:physiology*; D008970:Molecular Weight; D051381:Rats; D012697:Serine Endopeptidases / Q000032:analysis / Q000302:isolation & purification / Q000378:metabolism; D013154:Spleen / Q000201:enzymology
D004792:Enzyme Precursors; D007376:Interleukin-2; D010450:Endopeptidases; D053804:Granzymes; D012697:Serine Endopeptidases