Soluble defense collagens: Sweeping up immune threats.

• Soluble defense collagens are secreted proteins containing short collagen domains. • High-order oligomerization is integral to the biological functions of these proteins. • They are involved in clearing the extracellular space of dying cells and pathogens. • They modulate macrophages toward an anti-inflammatory resolving phenotype. • They are key factors for macrophage-driven repair programs that restore homeostasis. Soluble defense collagens form a group of secreted proteins that are primarily involved in host defense. All defense collagens contain a globular recognition domain contiguous to a collagen-like triple helical domain. They are oligomeric proteins, assembled in multiples of three subunits due to their collagen domains. Members of this group include collectins such as surfactant protein A and D (SP-A, SP-D), and mannan-binding lectin; C1q, the first component of the complement system; adiponectin; and ficolins. All are secreted to tissue cavities or serum. Soluble defense collagens are specialized to respond to infection, triggering the initiation of the complement cascade and/or enhancing phagocytosis of pathogens by macrophages. However, once inflammation is established, C1q, collectins, ficolins, or adiponectin can influence macrophage responses, thereby contributing to resolve the inflammation. In addition, some members of this group of proteins (SP-A, C1q, and adiponectin) modulate tissue-repair functions of macrophages. This review will focus on the molecular mechanisms by which these proteins efficiently defend against immune threats and contribute to tissue repair. [ABSTRACT FROM AUTHOR]