Essential neutrophil integrins are influenced by SEMA7A. Human PMNs were incubated with NaCl, 10 ng/mL TNF-α, or 2 μg/mL recSEMA7A for 15 minutes before proteomics analysis. The acquired raw data were analyzed after normalization. To analyze the samples, a 1-Factorial linear model was fitted with LIMMA, resulting in a 2-sided t test or F test based on moderated statistics. All presented P values were adjusted for multiple analyses by controlling the false discovery rate according to Benjamini and Hochberg. Proteins were defined as differential when |logFC| >.5 and an adjusted P value <.05 from triplicate experiments. (A) Expression of neutrophil surface lectin proteins and membrane integrin proteins from harvested samples. (B) Expression of intracellular neutrophil Rho/Ras GTPases, mitogen-associated kinases, adapter proteins, and detoxifying enzymes. (C) PMN surface expression of CD11b after 15 minutes of incubation with recSEMA7A or TNF-α. Measurement was performed by FACS, and the MFI (PE) was normalized to the highest measured value. (D) PMN surface expression of PSGL-1 after 15 minutes of incubation with recSEMA7A or TNF-α. (E) PMN surface expression of CD11a after 15 minutes of incubation with recSEMA7A or TNF-α. (F) PMN surface expression of CD62L after 15 minutes of incubation with recSEMA7A or TNF-α. Measurement was performed by FACS, and the MFI (BV510) was normalized to the highest measured value. Multiple cells were analyzed from independently performed experiments in triplicate. Group comparisons were performed by unpaired 2-tailed Student t tests (the data are the mean ± SD). ∗P < .05; ∗∗P < .01; ∗∗∗P < .001 as indicated. MFI, Mean Fluorescence Intensity; PE, Phycoerythrin.