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Review
. 2003 May;111(10):1453-5.
doi: 10.1172/JCI18650.

Pulmonary surfactant: a front line of lung host defense

Affiliations
Review

Pulmonary surfactant: a front line of lung host defense

Jo Rae Wright. J Clin Invest. 2003 May.
No abstract available

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Figures

Figure 1
Figure 1
SP-A and SP-D are members of the collectin family of oligomeric proteins, which have collagen-like N-terminal regions and C-type carbohydrate recognition domains (CRDs). The CRDs bind carbohydrates such as those found on pathogen surfaces. SP-A consists of 6 structural units, which are assembled into a “flower bouquet” formation. SP-D consists of the tetrameric structural units assembled into an X-like structure. Figure adapted from an online article by N. Kawasaki that appears on Glycoforum(http://www.glycoforum.gr.jp/science/word/lectin/LEA06E.html).
Figure 2
Figure 2
SP-A and SP-D enhance bacterial clearance and inhibit bacterial growth. SP-A and SP-D are oligomeric proteins synthesized by type II pulmonary epithelial cells and secreted in the liquid that covers the lung epithelium. Both SP-A and SP-D opsonize pathogens and enhance their phagocytosis by innate immune cells such as alveolar macrophages and neutrophils. In this issue of the JCI, Wu and coworkers provide compelling evidence that SP-A and SP-D also are directly bactericidal (1); they damage the bacterial cell membrane and inhibit bacterial growth. Thus, SP-A and SP-D enhance bacterial clearance via enhancing phagocytosis and via direct antimicrobial effects on bacteria. Images are not to scale.

Comment on

References

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    1. Wright JR. Immunomodulatory functions of surfactant. Physiol. Rev. 1997;77:931–962. - PubMed
    1. Crouch E, Wright JR. Surfactant proteins A and D and pulmonary host defense. Annu. Rev. Physiol. 2001;63:521–554. - PubMed

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