Neutrophils undergo fast migration dynamics onto endothelium or extracellular matrix using anterior protrusion together with posterior contraction and retraction. While these migrating cells tend to leave behind the long-lasting membranous trails with enriched integrins ripped down from cell body, it is still unclear how the trail formation is quantitatively correlated with cell migration and what the regulating factors are key in this process. Here a multi-layered mechanochemical model was integrated with a motor-clutch model to simulate numerically the chemotactic migration of a neutrophil on the substrate. Results indicated that, in response to those polarized distributions of sensing molecule P21-activated kinase 1 (PAK1) and the downstream molecules Ras-related C3 botulinum toxin substrate (Rac) and Ras homolog family member (RhoA), membrane-bound integrins tend to be accumulated at both the cell front and rear, promoting the increase of migrating velocity and trail number with time when actin-related protein2/3 complex (Arp2/3) and myosin are respectively accumulated at the front and rear. These predictions were in agreement with those typical experimental observations in integrin polarization and trail formation. Parametric analysis further proposed that, while the migrating velocity yields a biphasic dependence on substrate hardness and motor unloaded velocity, trail number increases monotonically with substrate hardness, on-rate of integrin-ligand bonds, motor unloaded velocity, motor stall force, and clutch number but decreases with chemokine concentration and off-rate of integrin-ligand bonds. This work provided an insight in elaborating the mechanochemical pathways in neutrophil migration and deciphering the key extracellular or intracellular factors in regulating the relevant trail formation of those migrating neutrophils.