Cell and Tissue Research

, Volume 371, Issue 3, pp 455–471 | Cite as

Armed for destruction: formation, function and trafficking of neutrophil granules

  • Charles Yin
  • Bryan HeitEmail author


Neutrophils respond nearly instantly to infection, rapidly deploying a potent enzymatic and chemical arsenal immediately upon entering an infected site. This capacity for rapid and potent responses is endowed by stores of antimicrobial proteins contained in readily mobilizable granules. These granules contain the proteins necessary to mediate the recruitment, chemotaxis, antimicrobial function and NET formation of neutrophils. Four granule types exist, and are sequentially deployed as neutrophils enter infected sites. Secretory vesicles are released first, enabling recruitment of neutrophils out of the blood. Next, specific and gelatinase granules are released to enable neutrophil migration and begin the formation of an antimicrobial environment. Finally, azurophilic granules release potent antimicrobial proteins at the site of infection and into phagosomes. The step-wise mobilization of these granules is regulated by calcium signaling, while specific trafficking regulators and membrane fusion complexes ensure the delivery of granules to the correct subcellular site. In this review, we describe neutrophil granules from their formation through to their deployment at the site of infection, focusing on recent developments in our understanding of the signaling pathways and vesicular trafficking mechanisms which mediate neutrophil degranulation.


Neutrophil Degranulation Granulopoiesis Calcium GTPase Vesicular traffic 



Adaptor protein


Chédiak–Higashi syndrome


Complement receptor 3




Dedicator of cytokinesis protein 2


Endoplasmic reticulum


Fc receptor




GTPase activating protein


Guanine exchange factor


G protein-coupled receptor




Immunoreceptor tyrosine-based activation motif




Neutrophil extracellular trap


Phosphatidic acid




Src-family kinase


Specific granule deficiency


Synaptosomal-associated protein


Store-operated channel


Secretory vesicle


Vesicle-associated membrane protein.



The work in B.H.’s laboratory is supported by an operating grant from the Canadian Institutes for Health Research (MOP-123419), discovery grant #418194 from the Natural Sciences and Engineering Council of Canada, and an Ontario Ministry of Research and Innovation Early Researcher Award. C.Y. is a Vanier Scholar and holds a Canadian Institutes for Health Research MD/PhD Studentship.

Compliance with ethical standards

Conflict of interest

The authors declare that they have no conflict of interest.


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© Springer-Verlag GmbH Germany, part of Springer Nature 2017

Authors and Affiliations

  1. 1.Department of Microbiology and Immunology and the Center for Human ImmunologyThe University of Western OntarioLondonCanada

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