Development of the pulmonary surfactant system in two oviparous vertebrates

2000 ◽  
Vol 278 (2) ◽  
pp. R486-R493 ◽  
Author(s):  
Sonya D. Johnston ◽  
Sandra Orgeig ◽  
Olga V. Lopatko ◽  
Christopher B. Daniels
Keyword(s):  
Lung Tissue ◽  
Pulmonary Surfactant ◽  
Northern Blot Analysis ◽  
Total Phospholipid ◽  
Pulmonary Ventilation ◽  
Protein A ◽  
Surfactant Protein ◽  
Surfactant System ◽  
Bearded Dragon ◽  
Pogona Vitticeps

In birds and oviparous reptiles, hatching is often a lengthy and exhausting process, which commences with pipping followed by lung clearance and pulmonary ventilation. We examined the composition of pulmonary surfactant in the developing lungs of the chicken, Gallus gallus, and of the bearded dragon, Pogona vitticeps. Lung tissue was collected from chicken embryos at days 14, 16, 18 (prepipped), and 20(postpipped) of incubation and from 1 day and 3 wk posthatch and adult animals. In chickens, surfactant protein A mRNA was detected using Northern blot analysis in lung tissue at all stages sampled, appearing relatively earlier in development compared with placental mammals. Chickens were lavaged at days 16, 18, and 20 of incubation and 1 day posthatch, whereas bearded dragons were lavaged at day 55, days 57–60 (postpipped), and days 58–61 (posthatched). In both species, total phospholipid (PL) from the lavage increased throughout incubation. Disaturated PL (DSP) was not measurable before 16 days of incubation in the chick embryo nor before 55 days in bearded dragons. However, the percentage of DSP/PL increased markedly throughout late development in both species. Because cholesterol (Chol) remained unchanged, the Chol/PL and Chol/DSP ratios decreased in both species. Thus the Chol and PL components are differentially regulated. The lizard surfactant system develops and matures over a relatively shorter time than that of birds and mammals. This probably reflects the highly precocial nature of hatchling reptiles.

Inhaled nitric oxide injures the pulmonary surfactant system of lambs in vivo

1996 ◽  
Vol 270 (2) ◽  
pp. L273-L280 ◽  
Author(s):  
S. Matalon ◽  
V. DeMarco ◽  
I. Y. Haddad ◽  
C. Myles ◽  
J. W. Skimming ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Bronchoalveolar Lavage ◽  
Surface Properties ◽  
Pulmonary Surfactant ◽  
Protein A ◽  
Surfactant Protein ◽  
Surfactant System ◽  
Minimum Surface Tension

Nitric oxide (.NO) is a free radical, and as such may damage the pulmonary surfactant system. To determine the potential toxicity of .NO in vivo, we exposed 35 newborn lambs to 0, 20, 80 or 200 ppm .NO in either 21 or 60% O2 for 6 h. At the end of the exposure, lambs had normal values of arterial Po2, Pco2, and pH; total protein concentration in the bronchoalveolar lavage was also at normal levels. There were no differences in the surface properties of surfactant among the air or 60% O2 groups. Pulmonary surfactant samples, isolated from the bronchoalveolar lavage of lambs breathing air or 20 ppm .NO and reconstituted at a lipid concentration of 3 mg/ml, reached a low minimum surface tension (Tmin < 3 mN/m) in a pulsating bubble surfactometer. On the other hand, abnormal surface properties were observed in 36 and 60% of surfactant samples isolated from lungs of lambs that breathed 80 or 200 ppm .NO, respectively. These findings were confirmed using a captive bubble surfactometer. Surfactant protein A, isolated from the lungs of lambs that breathed 200 ppm .NO, exhibited decreased ability to aggregate lipids in vitro. These data are consistent with injury to the surfactant apoproteins during inhalation of either 80 or 200 ppm .NO for 6 h.

Surfactant metabolism in surfactant protein A-deficient mice

1997 ◽  
Vol 272 (3) ◽  
pp. L479-L485 ◽  
Author(s):  
M. Ikegami ◽  
T. R. Korfhagen ◽  
M. D. Bruno ◽  
J. A. Whitsett ◽  
A. H. Jobe
Keyword(s):  
Lung Tissue ◽  
Protein A ◽  
Surfactant Protein ◽  
Normal Lung ◽  
Tissue Slices ◽  
Normal Lung Function ◽  
Deficient Mice ◽  
Surfactant Metabolism

In the present study we asked if surfactant metabolism was altered in surfactant protein (SP) A-deficient mice in vivo. Although previous studies in vitro demonstrated that SP-A modulates surfactant secretion and reuptake by type II cells, mice made SP-A deficient by homologous recombination grow and reproduce normally and have normal lung function. Alveolar and lung tissue saturated phophatidylcholine (Sat PC) pools were 50 and 26% larger, respectively, in SP-A(-/-) mice than in SP-A(+/+) mice. Radiolabeled choline and palmitate incorporation into lung Sat PC was similar both in vivo and for lung tissue slices in vitro from SP-A(+/+) and SP-A(-/-) mice. Percent secretion of radiolabeled Sat PC was unchanged from 3 to 15 h, although SP-A(-/-) mice retained more labeled Sat PC in the alveolar lavages at 48 h (consistent with the increased surfactant pool sizes). Clearance of radiolabeled dipalmitoylphosphatidylcholine and SP-B from the air spaces after intratracheal injection was similar in SP-A(-/-) and SP-A(+/+) mice. Lack of SP-A had minimal effects on the overall metabolism of Sat PC or SP-B in mice.

Screening and Identification of Aptamers Against Pulmonary Surfactant Protein A

2013 ◽  
Vol 41 (11) ◽  
pp. 1659-1663 ◽  
Author(s):  
Li-Juan LIU ◽  
Yi CHEN ◽  
Wei WANG ◽  
Chao CHEN ◽  
Ming-Hao GAO ◽  
...  
Keyword(s):  
Pulmonary Surfactant ◽  
Protein A ◽  
Surfactant Protein ◽  
Surfactant Protein A ◽  
Screening And Identification ◽  
Pulmonary Surfactant Protein

Introduction of Mannose Binding Protein-Type Phosphatidylinositol Recognition into Pulmonary Surfactant Protein A†

Biochemistry ◽  
1999 ◽  
Vol 38 (22) ◽  
pp. 7321-7331 ◽  
Author(s):  
Hirofumi Chiba ◽  
Hitomi Sano ◽  
Masaki Saitoh ◽  
Hitoshi Sohma ◽  
Dennis R. Voelker ◽  
...  
Keyword(s):  
Pulmonary Surfactant ◽  
Binding Protein ◽  
Protein A ◽  
Surfactant Protein ◽  
Surfactant Protein A ◽  
Mannose Binding Protein ◽  
Mannose Binding ◽  
Pulmonary Surfactant Protein

scholarly journals Enhanced clearance of surfactant protein D during LPS-induced acute inflammation in rat lung

2001 ◽  
Vol 281 (1) ◽  
pp. L268-L277 ◽  
Author(s):  
Joel F. Herbein ◽  
Jo Rae Wright
Keyword(s):  
Host Defense ◽  
Lung Tissue ◽  
Pulmonary Surfactant ◽  
Acute Inflammation ◽  
Surfactant Protein ◽  
Enzymatic Digestion ◽  
Time Dependent ◽  
Surfactant Protein D ◽  
Rat Lung ◽  
Secretion Clearance

Pulmonary surfactant participates in the regulation of alveolar compliance and lung host defense. Surfactant homeostasis is regulated through a combination of synthesis, secretion, clearance, recycling, and degradation of surfactant components. The extracellular pool size of surfactant protein (SP) D fluctuates significantly during acute inflammation. We hypothesized that changes in SP-D levels are due, in part, to altered clearance of SP-D. Clearance pathways in rats were assessed with fluorescently labeled SP-D that was instilled into control lungs or lungs that had been treated with lipopolysaccharide (LPS) 16 h earlier. SP-D clearance from lavage into lung tissue was time dependent from 5 min to 1 h and 1.7-fold greater in LPS-treated lungs than in control lungs. Analysis of cells isolated by enzymatic digestion of lung tissue revealed differences in the SP-D-positive cell population between groups. LPS-treated lungs had 28.1-fold more SP-D-positive tissue-associated neutrophils and 193.6-fold greater SP-D association with those neutrophils compared with control lungs. These data suggest that clearance of SP-D into lung tissue is increased during inflammation and that tissue-associated neutrophils significantly contribute to this process.

Pulmonary surfactant protein A-mediated uptake of phosphatidylcholine by alveolar type II cells

1993 ◽  
Vol 265 (2) ◽  
pp. L193-L199 ◽  
Author(s):  
A. Tsuzuki ◽  
Y. Kuroki ◽  
T. Akino
Keyword(s):  
Pulmonary Surfactant ◽  
Protein A ◽  
Lamellar Body ◽  
Surfactant Protein ◽  
Surfactant Protein A ◽  
Alveolar Type ◽  
Type Ii Cells ◽  
Type Ii ◽  
Lamellar Bodies ◽  
Pulmonary Surfactant Protein

Pulmonary surfactant protein A (SP-A)-mediated uptake of phosphatidylcholine (PC) by alveolar type II cells was investigated. SP-A enhanced the uptake of liposomes containing dipalmitoylphosphatidylcholine (DPPC), 1-palmitoyl-2-linoleoyl phosphatidylcholine (PLPC), or 1,2-dihexadecyl-sn-glycero-3-phosphocholine (DPPC-ether), a diether analogue of DPPC, but about twice as much DPPC was taken up by type II cells as PLPC or DPPC-ether. When subcellular distribution was analyzed, 51.3 +/- 2.9% (mean +/- SD, n = 3) of cell-associated radiolabeled DPPC was recovered in the lamellar body-rich fraction in the presence of SP-A, whereas only 19.3 +/- 1.9% (mean +/- SD, n = 3) was found to this fraction in the absence of SP-A. When type II cells were incubated either with DPPC at 0 degree C or with DPPC-ether at 37 degrees C, or no cells were included, low proportions of the cell-associated lipids were present in the fractions corresponding to lamellar bodies even in the presence of SP-A. Anti-SP-A antibody significantly reduced the radioactivity incorporated into the lamellar body fraction. Phosphatidylcholine that had been incorporated into lamellar bodies remained largely intact when SP-A was present. Subcellular fractionations of type II cells with radiolabeled SP-A and DPPC revealed that the sedimentation characteristics of cell-associated SP-A are different from those of DPPC, although a small broad peak of radiolabeled SP-A was found in the lamellar body fraction.(ABSTRACT TRUNCATED AT 250 WORDS)

scholarly journals Pulmonary Surfactant Protein A Protects Lung Epithelium from Cytotoxicity of Human β-Defensin 3

2012 ◽  
Vol 287 (18) ◽  
pp. 15034-15043 ◽  
Author(s):  
Atsushi Saito ◽  
Shigeru Ariki ◽  
Hitoshi Sohma ◽  
Chiaki Nishitani ◽  
Kanako Inoue ◽  
...  
Keyword(s):  
Pulmonary Surfactant ◽  
Protein A ◽  
Surfactant Protein ◽  
Surfactant Protein A ◽  
Lung Epithelium ◽  
Pulmonary Surfactant Protein
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