The pulmonary collectins, SP-A and SP-D, orchestrate innate immunity in the lung

McCormack, Francis X.; Whitsett, Jeffrey A.

doi:10.1172/jci15293

Cited by 167 publications

(144 citation statements)

References 42 publications

(16 reference statements)

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“…The lung collectins, SP-A and SP-D, potentially contribute to the biophysical (alveolar stability) as well as the immunomodulatory (alveolar sterility) surfactant functions (Crouch and Wright, 2001;Hawgood and Poulain, 2001;McCormack and Whitsett, 2002). The present design-based stereological analysis characterizes parenchymal, alveolar type II cell, and alveolar macrophage alterations and thus provides quantitative data reflecting that chronic deficiency of SP-A and SP-D in mice leads to parenchymal remodeling, type II cell hyperplasia and hypertrophy, accumulation of enlarged alveolar macrophages, and disturbed type II cell surfactant metabolism.…”

Section: Discussionmentioning

confidence: 99%

“…The surfactant proteins A (SP-A) and D (SP-D) are members of the collectin protein family, and they have comparable potential to interact with cells and microorganisms (Crouch and Wright, 2001;Hawgood and Poulain, 2001). The lung collectins, SP-A and SP-D, are part of the pulmonary innate immune system (Crouch and Wright, 2001;McCormack and Whitsett, 2002;Wu et al, 2003;Wright, 2004) and influence inflammatory processes (Chabot et al, 2003;Gardai et al, 2003). Within the alveolar lumen, SP-A is associated with tubular myelin, whereas SP-D exists mainly free in the hypophase (Wright, 1997;McCormack and Whitsett, 2002).…”

mentioning

confidence: 99%

“…The lung collectins, SP-A and SP-D, are part of the pulmonary innate immune system (Crouch and Wright, 2001;McCormack and Whitsett, 2002;Wu et al, 2003;Wright, 2004) and influence inflammatory processes (Chabot et al, 2003;Gardai et al, 2003). Within the alveolar lumen, SP-A is associated with tubular myelin, whereas SP-D exists mainly free in the hypophase (Wright, 1997;McCormack and Whitsett, 2002). The distribution in different intra-alveolar microdomains may possibly lead to distinct functions.…”

mentioning

confidence: 99%

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Design‐based stereological analysis of the lung parenchymal architecture and alveolar type II cells in surfactant protein A and D double deficient mice

et al. 2005

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Alveolar epithelial type II cells synthesize and secrete surfactant. The surfactant-associated proteins A and D (SP-A and SP-D), members of the collectin protein family, participate in pulmonary immune defense, modulation of inflammation, and surfactant metabolism. Both proteins are known to have overlapping as well as distinct functions. The present study provides a design-based stereological analysis of adult mice deficient in both SP-A and SP-D (A Ϫ D Ϫ ) with special emphasis on parameters characterizing alveolar architecture and surfactant-producing type II cells. Compared to wild-type, A Ϫ D Ϫ mice have fewer and larger alveoli, an increase in the number and size of type II cells, as well as more numerous and larger alveolar macrophages. More surfactant-storing lamellar bodies are seen in type II cells, leading to a threefold increase in the total volume of lamellar bodies per lung, but the mean volume of a single lamellar body remains constant. These results demonstrate that chronic deficiency of SP-A and SP-D in mice leads to parenchymal remodeling, type II cell hyperplasia and hypertrophy, and disturbed intracellular surfactant metabolism. The design-based stereological approach presented here provides a framework for the quantitative lung structure analysis in gene-manipulated mice as well as in human lung disease.

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Section: Discussionmentioning

confidence: 99%

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confidence: 99%

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confidence: 99%

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Design‐based stereological analysis of the lung parenchymal architecture and alveolar type II cells in surfactant protein A and D double deficient mice

et al. 2005

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“…SP-D связывается с грамотрицательными бактериями, такими как Pseudomonas aeruginosa, Klebsiella pneumoniae, Escherichia coli и Haemophilus influenzaе, способствуя их агглютинации и стимуляции хемотак-сиса нейтрофилов, макрофагов и эозинофилов к месту инвазии патогена [25][26][27]. SP-D также может связываться с грамположи-тельными бактериями, такими как Streptococcus pneumoniae и Stafylococcus aureus, а также с микобактериями [28,29], респира-торно-синцитиальным вирусом, вирусом гриппа [30], грибами Pneumocystis carinii, Aspergillus fumigatus, Cryptococcus neoformans, Candida albicans [31].…”

Section: терапевтический архив 1 2015unclassified

Significance of surfactant proteins in the diagnosis of therapeutic diseases

et al. 2015

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“…In addition to the interaction with the surfactant lipids and alveolar type II cells [3,4], SP-A plays an important role in the innate immune system of the lung. SP-A has been reported to bind to various spectra of microorganisms and enhance phagocytosis by alveolar macrophages [5,6]. SP-A also modulates the cellular responses to microorganisms via its direct interactions with the pattern recognition receptors [7][8][9].…”

Section: Introductionmentioning

confidence: 99%

Lactoferrin and surfactant protein A exhibit distinct binding specificity to F protein and differently modulate respiratory syncytial virus infection

et al. 2003

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Surfactant protein A (SP-A) and lactoferrin (LF) play important roles in innate immune systems in the respiratory mucous membranes. We investigated how SP-A and LF act against respiratory syncytial virus (RSV) infection. The present study indicated that RSV-induced IL-8 secretion from HEp-2 cells was up-regulated by SP-A (170% of control) but downregulated by LF (23% of control). RSV infectivity determined by viral titers and the uptake of FITC-labeled RSV were also increased by SP-A, but decreased by LF. To clarify the mechanism of these opposite effects, we examined the interactions of SP-A and LF with RSV F protein, the most important surface glycoprotein for viral penetration. RSV F protein was found to be the ligand for both SP-A and LF, but the manners of binding were different. LF directly interacted with the F 1 subunit, which involved antigenic sites of F protein. Contrarily, SP-A associated with the F 2 subunit, which was highly glycosylated. SP-A but not LF failed to interact with deglycosylated F protein. Moreover, SP-A initiated the hemolyzing fusion activity of F protein. These results suggest that SP-A and LF modulate RSV infection by different binding specificity to F protein.

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The pulmonary collectins, SP-A and SP-D, orchestrate innate immunity in the lung

Cited by 167 publications

References 42 publications

Design‐based stereological analysis of the lung parenchymal architecture and alveolar type II cells in surfactant protein A and D double deficient mice

Design‐based stereological analysis of the lung parenchymal architecture and alveolar type II cells in surfactant protein A and D double deficient mice

Significance of surfactant proteins in the diagnosis of therapeutic diseases

Lactoferrin and surfactant protein A exhibit distinct binding specificity to F protein and differently modulate respiratory syncytial virus infection

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