Fig. 2.
Fig. 2. Processing of the chemokines CTAP-III, MCP-2, PF-4, RANTES, and GRO-α by activated neutrophil gelatinase B. / Different chemokines were incubated with activated gelatinase B and subsequently analyzed by SDS-PAGE and silver staining. (A) Recombinant human MCP-2 was not affected by treatment with gelatinase B. Natural human CTAP-III and PF-4 were slowly degraded by gelatinase B. Degradation of PF-4 was inhibited by EDTA and o-phenantrolin (PHEN) and was not observed after incubation with stromelysin-1 alone. (B) Recombinant RANTES was not affected by incubation with gelatinase B, whereas natural GRO-α was slowly degraded. Degradation of GRO-α was inhibited by EDTA and PHEN and was not observed after incubation with stromelysin-1. S indicates relative molecular mass standard; 0, no incubation; −, incubation with stromelysin-1 only; +, incubation with activated gelatinase B. Respective inhibitors are indicated at the top of each lane.

Processing of the chemokines CTAP-III, MCP-2, PF-4, RANTES, and GRO-α by activated neutrophil gelatinase B.

Different chemokines were incubated with activated gelatinase B and subsequently analyzed by SDS-PAGE and silver staining. (A) Recombinant human MCP-2 was not affected by treatment with gelatinase B. Natural human CTAP-III and PF-4 were slowly degraded by gelatinase B. Degradation of PF-4 was inhibited by EDTA and o-phenantrolin (PHEN) and was not observed after incubation with stromelysin-1 alone. (B) Recombinant RANTES was not affected by incubation with gelatinase B, whereas natural GRO-α was slowly degraded. Degradation of GRO-α was inhibited by EDTA and PHEN and was not observed after incubation with stromelysin-1. S indicates relative molecular mass standard; 0, no incubation; −, incubation with stromelysin-1 only; +, incubation with activated gelatinase B. Respective inhibitors are indicated at the top of each lane.

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