Aspects of secondary and quaternary structure of surfactant protein A from canine lung

King, Richard J.; Simon, Dexter; Horowitz, Paul M.

doi:10.1016/0005-2760(89)90114-8

Cited by 79 publications

(68 citation statements)

References 20 publications

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“…The mechanism by which serum SP-A and SP-D levels are elevated in patients with interstitial lung disease has been thought to be that alveolar type II cells cause hyperplasia from stimulation, such as through inflammation, and generate the creation of biomarkers; in addition, the destruction of alveolar epithelium and endothelium might cause hyperlucent into blood (14,21). Furthermore, the molecular weight of a completed unit of SP-A and SP-D is estimated to be 650 kd and 540 kd, respectively, so SP-D is a slightly smaller than SP-A (22,23). Considering these mechanism, these differences between BALF and serum levels of SP-A and SP-D in AEP patients might be due to the grade of damage to bronchiolar epithelia.…”

Section: Discussionmentioning

confidence: 99%

KL-6 and Surfactant Proteins A and D in Serum and Bronchoalveolar Lavage Fluid in Patients with Acute Eosinophilic Pneumonia

et al. 2005

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Section: Discussionmentioning

confidence: 99%

KL-6 and Surfactant Proteins A and D in Serum and Bronchoalveolar Lavage Fluid in Patients with Acute Eosinophilic Pneumonia

et al. 2005

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“…This monomer trimerizes by the folding of the collagen-like domains into triple helices (8,51). Six SP-A trimers form an octadecamer through covalent and noncovalent interactions between the N-terminal segment and the first half of the collagen-like domain (8,51).…”

Section: Discussionmentioning

confidence: 99%

Pulmonary Surfactant Protein A Up-Regulates Activity of the Mannose Receptor, a Pattern Recognition Receptor Expressed on Human Macrophages

Beharka

Gaynor

Kang

et al. 2002

The Journal of Immunology

135

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Inhaled particulates and microbes are continually cleared by a complex array of lung innate immune determinants, including alveolar macrophages (AMs). AMs are unique cells with an enhanced capacity for phagocytosis that is due, in part, to increased activity of the macrophage mannose receptor (MR), a pattern recognition receptor for various microorganisms. The local factors that “shape” AM function are not well understood. Surfactant protein A (SP-A), a major component of lung surfactant, participates in the innate immune response and can enhance phagocytosis. Here we show that SP-A selectively enhances MR expression on human monocyte-derived macrophages, a process involving both the attached sugars and collagen-like domain of SP-A. The newly expressed MR is functional. Monocyte-derived macrophages on an SP-A substrate demonstrated enhanced pinocytosis of mannose BSA and phagocytosis of Mycobacterium tuberculosis lipoarabinomannan-coated microspheres. The newly expressed MR likely came from intracellular pools because: 1) up-regulation of the MR by SP-A occurred by 1 h, 2) new protein synthesis was not necessary for MR up-regulation, and 3) pinocytosis of mannose BSA via MR recycling was increased. AMs from SP-A−/− mice have reduced MR expression relative to SP-A+/+. SP-A up-regulation of MR activity provides a mechanism for enhanced phagocytosis of microbes by AMs, thereby enhancing lung host defense against extracellular pathogens or, paradoxically, enhancing the potential for intracellular pathogens to enter their intracellular niche. SP-A contributes to the alternative activation state of the AM in the lung.

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“…This modification, presumably important for stabilizing the collagenlike triple helix into which the amino-terminal one-third of SP-A is assembled (24) appears to be a prerequisite for passage of SP-A through the secretory apparatus of the cell (25). Human SP-A is also glycosylated close to the carboxy terminus with a sialylated oligosaccharide chain, but the role of this modification is not known.…”

Section: Heterogeneity Ofpulmonary Surfactantmentioning

confidence: 99%

Pulmonary surfactant and its apoproteins.

Hawgood¹,

Clements²

1990

J. Clin. Invest.

168

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Aspects of secondary and quaternary structure of surfactant protein A from canine lung

Cited by 79 publications

References 20 publications

KL-6 and Surfactant Proteins A and D in Serum and Bronchoalveolar Lavage Fluid in Patients with Acute Eosinophilic Pneumonia

KL-6 and Surfactant Proteins A and D in Serum and Bronchoalveolar Lavage Fluid in Patients with Acute Eosinophilic Pneumonia

Pulmonary Surfactant Protein A Up-Regulates Activity of the Mannose Receptor, a Pattern Recognition Receptor Expressed on Human Macrophages

Pulmonary surfactant and its apoproteins.

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