The protective effect of different airway humidification liquids to lung after tracheotomy in traumatic brain injury: The role of pulmonary surfactant protein-A (SP-A)

Gene ◽  
2016 ◽  
Vol 577 (1) ◽  
pp. 89-95 ◽  
Author(s):  
Xinyang Su ◽  
Zefu Li ◽  
Meilin Wang ◽  
Zhenzhu Li ◽  
Qingbo Wang ◽  
...  
Keyword(s):  
Traumatic Brain Injury ◽  
Brain Injury ◽  
Protective Effect ◽  
Pulmonary Surfactant ◽  
Protein A ◽  
Surfactant Protein ◽  
Surfactant Protein A ◽  
Airway Humidification ◽  
Pulmonary Surfactant Protein

scholarly journals Lipid-restricted recognition of mycobacterial lipoglycans by human pulmonary surfactant protein A: a surface-plasmon-resonance study

2002 ◽  
Vol 365 (1) ◽  
pp. 89-97 ◽  
Author(s):  
Stéphane SIDOBRE ◽  
Germain PUZO ◽  
Michel RIVIÈRE
Keyword(s):  
Surface Plasmon Resonance ◽  
Surface Plasmon ◽  
Plasmon Resonance ◽  
Pulmonary Surfactant ◽  
Protein A ◽  
Surfactant Protein ◽  
Surfactant Protein A ◽  
Mycobacterial Cell Wall ◽  
Pulmonary Surfactant Protein

The human pulmonary surfactant protein A (hSP-A), a member of the mammalian collectin family, is thought to play a key defensive role against airborne invading pulmonary pathogens, among which is Mycobacterium tuberculosis, the aetiologic agent of tuberculosis. hSP-A has been shown to promote the uptake and the phagocytosis of pathogenic bacilli through the recognition and the binding of carbohydrate motifs on the invading pathogen surface. Recently we identified lipomannan and mannosylated lipoarabinomannan (ManLAM), two major mycobacterial cell-wall lipoglycans, as potential ligands for binding of hSP-A. We demonstrated that both the terminal mannose residues and the fatty acids are critical for binding, whereas the inner arabinosyl and mannosyl domains do not participate. In the present study we developed a surface-plasmon-resonance assay to analyse the molecular basis for the recognition of ManLAM by hSP-A and to try to define further the role of the lipidic aglycone moiety. Binding of ManLAM to immobilized hSP-A was consistent with the simplest one-to-one interaction model involving a single class of carbohydrate-binding site. This observation strongly suggests that the lipid moiety of ManLAM does not directly interact with hSP-A, but is rather responsible for the macromolecular organization of the lipoglycan, which may be necessary for efficient recognition of the terminal mannosyl epitopes. The indirect, structural role of the lipoglycan lipidic component is further supported by the complete lack of interaction with hSP-A in the presence of a low concentration of mild detergent.

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

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

Characterization of the rat pulmonary surfactant protein A promoter

1992 ◽  
Vol 206 (3) ◽  
pp. 613-623 ◽  
Author(s):  
Thierry LACAZE-MASMONTEIL ◽  
Caroline FRASLON ◽  
Jacques BOURBON ◽  
Michel RAYMONDJEAN ◽  
Axel KAHN
Keyword(s):  
Pulmonary Surfactant ◽  
Protein A ◽  
Surfactant Protein ◽  
Surfactant Protein A ◽  
Pulmonary Surfactant Protein
Sign in / Sign up

Export Citation Format

Share Document