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Results from the gelatin zymography assay showed that GPNMB knockdown greatly down-regulated the levels of MMP-2 and MMP-9 in conditioned media of cultured SiHa and HeLa cells compared with the control (Figure 3B).
MMP-2 and MMP-9 activity levels in follicular fluid and seminal plasma: Zymography gel showed bands at 62 kDa and 82 kDa which were considered as MMP-2 and MMP-9, respectively.
[17] Test: serum of 15 PCa RT-PCR and patients with zymography metastasis and 10 without metastasis.
Caption: FIGURE 8: MMP-2 and MMP-9 expressions were detected by gelatin gel zymography. MMP-2 and MMP-9 expression in microencapsulated SGC7901 cells (a), macrophages (b), and microencapsulated SGC7901 cells cocultured with macrophages (c).
W146 promoted a robust downregulation of the enzyme expression (Figures 2(a) and 2(b)), associated with a reduction of the release of MMP-2 active form, as judged by zymography (Figure 2(c)), further underlying the role of S1PR1-mediated signalling in the control of ECM remodelling.
Caption: Figure 2: Peri-implant sulcular fluid (PISF) collected from 29 peri-implantitis and 32 periodontally healthy sites were tested for elevated aMMP-8 by ImplantSafe PoC/chair-side test (+/-), analysed for aMMP-8 (ng/ml) by immunofluorometric assay (IFMA), and by quantitated gelatin zymography for all molecular weight forms of gelatinase-B (MMP-9, zymographic densitometric units) (a).
(a) Image of gelatin zymography assay (GZ) using the medium of HTR8/SVneo cells disturbed by shRNA.
ProMMPs and their active forms (MMPs) were detected in the llama OF after incubation with or without 1mM APMA prior to zymography. OF samples without APMA incubation showed two gelatinolytic bands corresponding to 62 and 94 kDa, assumedly proMMP2 and proMMP9, respectively.
Purified trypsin showed a single band on both SDS and zymography (Figure 2a, b) suggesting their high purity and showing only one dominant isoform of trypsin in Dosidicus gigas hepatopancreas.
Measure of gelatinase activities, MMP-2 and MMP-9, was performed by zymography, a polyacrylamide gel electrophoresis (10%), with gelatin (1%, Sigma) in nonreduced conditions [47].
The enzyme activities of MMP-2 and MMP-9 were evaluated by zymography. Fifty micrograms of the supernatant protein were subjected to electrophoresis in a 10% SDS-PAGE gel copolymerized with gelatin (1 mg/mL).
Homogenates were screened for the presence of MMP species by substrate gelatin zymography [22, 23, 38, 39].