title: Substrate-specific proteases (BLT-esterase) are localized predominantly in the natural killer cells of unprimed mice.
abstract: In leukocytes isolated from unprimed mice, the levels of extractable N alpha-Cbz-Lys-thiobenzylesteresterase (BLT-esterase) closely correlated with the number of natural killer (NK) cells. The spleens of mice that exhibit severe combined immunodeficiency (SCID) contained much higher levels of this enzyme than other mouse strains. Treatments that resulted in a local accumulation of NK cells (as assessed by lytic activity) produced a concomitant increase in BLT-esterase activity. However, short-term in vitro treatment of spleen cells with interferon (IFN)-alpha/beta indicated that BLT-esterase levels correlated more closely with absolute numbers of NK cells than with their lytic capacity. There was a very good correlation between the numbers of cells bearing the NK phenotype (NK-1.1+) and BLT-esterase levels. Cells positively sorted using the NK-specific antibodies NK-1.1 and LGL-1 had high enzymatic activity. The BLT-esterase levels were high in both the NK-1.1+/LGL-1- and NK-1.1+/LGL-1+ subsets. Highly purified CD4+ and CD8+ T cells and sIg+ B cells demonstrated negligible enzyme, as did populations of cells highly enriched for macrophages or neutrophils. However, it should be stressed that the inbred mice used on this study have been maintained in a pathogen-free facility. It would be anticipated that mice maintained under less stringent conditions could exhibit appreciable levels of BLT-esterase activity in their T cells. Nonetheless, BLT-esterase is present at high levels in NK cells and cannot be regarded as a T cell-specific enzyme.
authors: Biological Carcinogenesis Development Program, PRI/DynCorp, NCI-FCRDC, Frederick, Maryland 21702-1201.
authors: T J
authors: TJ
authors: Sayers
authors: L H
authors: LH
authors: Mason
authors: A
authors: A
authors: Pilaro
authors: T A
authors: TA
authors: Wiltrout
authors: K
authors: K
authors: Komschlies
authors: W L
authors: WL
authors: Munger
authors: R H
authors: RH
authors: Wiltrout
mesh_terms: D000818:Animals; D002266:Carboxymethylcellulose Sodium / Q000494:pharmacology / Q000031:analogs & derivatives; D005434:Flow Cytometry; D053804:Granzymes; D007369:Interferon Inducers / Q000494:pharmacology; D007370:Interferon Type I / Q000494:pharmacology; D007371:Interferon-gamma / Q000494:pharmacology; D007694:Killer Cells, Natural / Q000187:drug effects / Q000201:enzymology* / Q000276:immunology; D007700:Kinetics; D008099:Liver / Q000187:drug effects / Q000201:enzymology; D008198:Lymph Nodes / Q000187:drug effects / Q000201:enzymology; D008297:Male; D051379:Mice; D008807:Mice, Inbred BALB C; D008810:Mice, Inbred C57BL; D008819:Mice, Nude; D016513:Mice, SCID; D011070:Poly I-C / Q000494:pharmacology; D011107:Polylysine / Q000494:pharmacology / Q000031:analogs & derivatives; D011994:Recombinant Proteins; D012697:Serine Endopeptidases / Q000378:metabolism*; D013154:Spleen / Q000276:immunology; D013379:Substrate Specificity; D016176:T-Lymphocyte Subsets / Q000276:immunology
chemical_list: D007369:Interferon Inducers; D007370:Interferon Type I; D011994:Recombinant Proteins; D011107:Polylysine; C019531:poly ICLC; D007371:Interferon-gamma; D053804:Granzymes; D012697:Serine Endopeptidases; D002266:Carboxymethylcellulose Sodium; D011070:Poly I-C