As evidenced by ELISA, CTSL and CTSH alone had only small effects on COX2 and PGE2 syntheses.
Whereas CTSL had no effects on RANKL and OPG expressions (data not shown), CTSH caused a significant (P < 0.05) upregulation of the F.
 have detected an anti-inflammatory effect of CTSL and Nokhbehsaim et al.
For inhibition studies of CTLA-2[alpha], purification of recombinant mouse cathepsin L (CtsL) was performed according to the method described by Kramer et al.
For the inhibition assays towards CtsL, 30 [micro]L of the CTLA-2[alpha] fraction was added to the assay buffer (500 [micro]L) as described above.
CtsL and CTLA-2[alpha] were preincubated in 500 pL of preincubation buffer (1mM EDTA, 8mM cysteine, and 100 mM sodium acetate, pH 5.0) at 37[degrees]C.
pH Dependence of the Interaction between CTLA-2[alpha] and CtsL. CtsL was activated by preincubation in the buffer (1 mM EDTA, 8 mM cysteine, 0.1 M sodium acetate, pH 5.5) for 5 min at 37[degrees] C.
It was fully inhibitory against CtsL. By treating it with the strong reducing reagent, DTT, the dimeric form lost all its inhibitory activity and was completely converted to the monomeric form (Figure 3, lane 3).
CTLA-2[alpha] and/or CtsL were firstly preincubated for a short time in an acidic buffer (pH 5.0) containing cysteine to activate CtsL and allow the interaction between CTLA-2[alpha] and CtsL.
In previous research, Gonzalo's team showed that vitamin D inhibits CTSL-mediated degradation of 53BP1 in non-tumor cells, as efficiently as specific CTSL inhibitors.
In a final exceptionally useful discovery, Gonzalo and collaborators found that high levels of nuclear CTSL and low levels of 53BP1 and nuclear vitamin D receptor (VDR) are a clear marker that identifies certain triple-negative breast cancer patients, biomarkers that offer the potential to customize future breast cancer therapies.