Yoshinori Ogasawara

TL;DR: Investigation of the cellular and subcellular distribution of surfactant protein D by immunogold labeling in lungs of adult rats that had been given bovine serum albumin coupled to 5-nm gold (BSAG) for 2 hr to visualize the endocytotic pathway found that both SP-A and SP-D were present in the same granules.

TL;DR: It is concluded that SP-D specifically binds to PI, the first report that demonstrates thatSP-D interacts with surfactant phospholipids.

TL;DR: The functional region in the carbohydrate recognition domain of rat SP-A and SP-D that is involved in binding lipids and interacting with alveolar type II cells by using chimeric proteins is investigated and it is concluded that theSP-A region of Glu195–Phe228 is required for lipid and type II cell interactions.

TL;DR: New ELISA with recombinant SP-D and F(ab')2 fragment of anti-SP-D monoclonal antibody gives a greater advantage for the accurate detection of SP- D in sera from patients with idiopathic pulmonary fibrosis, interstitial pneumonia with collagen disease and pulmonary alveolar proteinosis without interference of rheumatoid factor.

TL;DR: The CRD is essential for the SP-A functions of lipid binding, liposome aggregation, the inhibitory effect on lipid secretion, and the augmentation of lipid uptake by type II cells, and these activities are largely attributable to amino acid residues within the steric inhibitory footprint of 1D6.