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. 2018 Mar 2;9:910. doi: 10.1038/s41467-018-03351-4

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© The Author(s) 2018

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 3 — The protease MT4-MMP can cleave the αM integrin chain (Itgam). a Percentage of circulating patrolling monocytes (CD45+Itgam+Ly6Clow, excluding granulocytes) and the normalized mean fluorescence intensity (MFI) of Itgam cell-surface levels in patrolling monocytes from Ldlr^–/– mice transplanted with MT4-MMP^+/+ or MT4-MMP^–/– BM cells and fed a HFD for 0, 1, or 8 weeks; n = 12, n = 6, and n = 6 mice in basal, 1 week and 8 weeks per genotype; four independent experiments in basal and two independent experiments at 1 and 8 weeks. b Design of lentiviral (LV) vector with SFFV-driven Mmp17 (MT4-MMP) expression and IRES-driven expression of green fluorescent protein (GFP). c LV encoding full-length mouse MT4-MMP (FL), the catalytic inactive mutant (E248A, EA), or GFP only (mock) were i.p. injected into MT4-MMP-null mice. Itgam cell surface levels were assessed by flow cytometry in the infected peritoneal macrophages (GFP+Itgam+F4/80+) 5 days after infection; n = 6 mice per condition in two independent experiments. d Depiction of human αMβ2 integrin domains, indicating the predicted cleavage site at position 977 in the Calf-2 domain of human αM integrin. e In silico model of human MT4-MMP dimer (gray) and αMβ2 integrin (αM chain, green; β2 chain, blue) showing the putative cleavage site between N977 and L978 (red) in the αM chain, and the catalytic active center in the MT4-MMP dimer (orange). f Representative extracted ion chromatogram of peptides obtained after incubation of the synthetic human αM integrin peptide RPQVTFSENLSSTCHTKER in the presence or absence of human recombinant MT4-MMP catalytic domain (hrMT4). g Quantification of the relative abundance of the intact RPQVTFSENLSSTCHTKER and N-terminal peptide fragments in each condition; n = 4 independent experiments. Data were tested by two-way ANOVA followed by Bonferroni’s post test in a, by one-way ANOVA followed by Bonferroni’s post test in c, and by two-tailed Student’s t-test in g. IRES, internal ribosome entry site; SFFV, spleen focus-forming virus. Results are expressed as mean ± SEM. *p < 0.05, **p < 0.01, and ***p < 0.001