These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Non-granular proteolytic enzymes of rat interleukin-2-activated natural killer cells. III. Enhancement of A-NKP 1, 2, and 3 proteolytic activities (cleaving after Arg, Phe and Pro) in response to interleukin-2.
    Author: Kitson RP, Miller CA, Goldfarb RH.
    Journal: Nat Immun; 1995 Sep; 14(5-6):286-94. PubMed ID: 8933822.
    Abstract:
    Rat IL-2-activated natural killer (A-NK) cells contain a number of cytosolic proteases (A-NKP 1-3), two of which (A-NKP 2 and A-NKP 3) have been implicated in cytolytic function. The 3.2.3 monoclonal antibody directed against the NKRP-1 signal transduction molecule, a selective marker of rat NK cells, was used to select a highly purified population of rat NK cells. When the 3.2.3-positive cells were cultured in the presence of IL-2, a time-dependent increase in the specific activity of A-NKP 1, A-NKP 2 and A-NKP 3 was observed which paralleled the observed increase in lytic activity against both NK-sensitive (YAC-1) and NK-resistant (P815) targets. A transient rise was observed in the specific activity of N alpha-benzyloxycarbonyl-L-lysine thiobenzyl esterase (BLT esterase, i.e. granzyme A). These results lend further support to the hypothesis that A-NKP 2, a component of the rat A-NK cell multicatalytic proteinase complex/proteasome, and A-NKP 3 contribute to the cytolytic function of A-NK cells. Moreover, these results further suggest that proteolytic enzymes that contribute to cell-mediated cytotoxicity are not restricted to the granzymes or localized only in the lytic granules of effector cells.
    [Abstract] [Full Text] [Related] [New Search]