Ectodomain Shedding by ADAM17: Its Role in Neutrophil Recruitment and the Impairment of This Process during Sepsis

Hemant K Mishra, Jing Ma, Bruce Walcheck, Hemant K Mishra, Jing Ma, Bruce Walcheck

Abstract

Neutrophils are specialized at killing bacteria and are recruited from the blood in a rapid and robust manner during infection. A cascade of adhesion events direct their attachment to the vascular endothelium and migration into the underlying tissue. A disintegrin and metalloproteinase 17 (ADAM17) functions in the cell membrane of neutrophils and endothelial cells by cleaving its substrates, typically in a cis manner, at an extracellular site proximal to the cell membrane. This process is referred to as ectodomain shedding and it results in the downregulation of various adhesion molecules and receptors, and the release of immune regulating factors. ADAM17 sheddase activity is induced upon cell activation and rapidly modulates intravascular adhesion events in response to diverse environmental stimuli. During sepsis, an excessive systemic inflammatory response against infection, neutrophil migration becomes severely impaired. This involves ADAM17 as indicated by increased levels of its cleaved substrates in the blood of septic patients, and that ADAM17 inactivation improves neutrophil recruitment and bacterial clearance in animal models of sepsis. Excessive ADAM17 sheddase activity during sepsis thus appears to undermine in a direct and indirect manner the necessary balance between intravascular adhesion and de-adhesion events that regulate neutrophil migration into sites of infection. This review provides an overview of ADAM17 function and regulation and its potential contribution to neutrophil dysfunction during sepsis.

Keywords: adhesion; bacteria; infection; inflammation; leukocyte.

Figures

Figure 1
Figure 1
(A) Circulating neutrophils attach to and transmigrate through the vascular endothelium in a step-wise process. Neutrophils accumulate on the vascular endothelium by direct (1°) and indirect (2°) manners, roll and scan the endothelial cells for chemokines, which promotes stable tethers and eventual transmigration into the underlying tissue. Various neutrophil and endothelial cell adhesion molecules and receptors directly involved in this process (represented by black dots) are listed in the figure, and those that are ADAM17 substrates are indicated in red. (B) Over-activation of ADAM17 by inflammatory stimuli during sepsis may result in excessive ectodomain shedding by neutrophils and endothelial cells that in turn impairs neutrophil recruitment and bacterial (green rods) clearance.
Figure 2
Figure 2
Illustration of the domain structure of the human ADAM family members. Each domain is indicated by a letter. Metalloproteinase (M), disintegrin-like (D), cysteine-rich (C), and epidermal growth factor (E). Additional regions of functional relevance discussed in the text are indicated in the key.

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