Recombinant Rat Pulmonary surfactant-associated protein D (Sftpd)

1. in acute lung injury, serum level increased from day 5, peaked on day 10, and then gradually decreased until day 28 PMID: 27541374
2. SPA binds dipalmitoyl-phosphatidylcholine, the major surfactant lipid component, but not phosphatidylinositol; SPD exhibits the opposite preference. Data suggest flexibility in a key surface loop supports distinctive lipid binding of SPA; quadruple mutant SPA (E171D/P175E/R197N/K203D) that introduces SPD-like loop-stabilizing Ca2+ binding site in carbohydrate recognition domain exhibits ligand-binding preferences of SPD. PMID: 28719181
3. In rat SP-D overexpressed mice, the lipopolysaccharide-induced levels of TNF-alpha and IL-10 in amniotic fluid and fetal serum and the expression of IL-10 in placenta and fetal membranes were significantly different from wild-type mice. PMID: 22892325
4. Surfactant protein D modulated subpollen particle uptake in a cell type specific way (e.g. greater number of macrophages and epithelial cells, which participated in allergen particle uptake) and led to a decreased secretion of pro-inflammatory cytokines. PMID: 22296755
5. Silica exposure causes dynamic changes of SP-D and CC16 protein expression in lung tissue and bronchoalveolar lavage fluid. PMID: 19080379
6. An extended binding site for influenza A virus; calcium-dependent antiviral activity involves residues flanking the primary carbohydrate binding site as well as more remote residues displayed on the carbohydrate recognition domain surface. PMID: 20601494
7. SP-D promotes attachment of allergen-containing subpollen particles to epithelial cells and may thus be involved in the inflammatory response to inhaled allergen. PMID: 20569420
8. analysis of myeloperoxidase-dependent inactivation of surfactant protein D in vitro and in vivo PMID: 20228064
9. Results suggest that SP-D-dependent processes regulating surfactant lipid homeostasis were disassociated from those mediating emphysema. PMID: 12163500
10. Heterogeneous allele expression of SP-D mRNA in large intestine and other tissues. PMID: 12464693
11. SP-A and SP-D are antimicrobial proteins that directly inhibit the proliferation of Gram-negative bacteria in a macrophage- and aggregation-independent manner by increasing the permeability of the microbial cell membrane PMID: 12750409
12. SP-A and SP-D are antimicrobial proteins that directly inhibit the growth of Histoplasma capsulatum by increasing permeability of the organism PMID: 12857753
13. SP-D interacts with chlamydial pathogens and enhance their phagocytosis into macrophages PMID: 15075250
14. Degradation of pulmonary surfactant protein D by Pseudomonas aeruginosa elastase abrogates innate immune function PMID: 15123664
15. SP-A and SP-D enhance mannose receptor-mediated phagocytosis of M. avium by macrophages PMID: 15187139
16. results indicated SP-A & SP-D have distinct functions in lung homeostasis & the function of the neck domain & carbohydrate recognition domain of SP-D is dependent on its own NH2-terminal & collagenous domains that cannot be complemented by those of SP-A PMID: 16500946
17. The ligand binding of homologous human, rat, and mouse trimeric trimeric neck plus carbohydrate recognition domain (neck+CRD) fusion proteins, each with identical N-terminal tags remote from the ligand-binding surface, was compared. PMID: 16514117
18. VEGF increased expression of SP-D mRNA in preterm rat lung. PMID: 17267143
19. Interactions with the side chain of inner core heptoses provide a potential mechanism for the recognition of diverse types of lipopolysaccharides by SP-D. PMID: 18092821
20. These results show that antiviral activities of surfactant protein-D can be reproduced without the N-terminal and collagen domains and that cross-linking of these domains is essential for anti-influenza A virus activity. PMID: 18302538
21. After OVA challenge alveolar epithelial cells Type II (AEII) show a significantly higher expression of SP-A and SP-D leading also to higher amounts of both SPs in BALF, and macrophages gather predominantly SP-A. PMID: 18802356
22. S-nitrosylation of SP-D causes quaternary structural alterations and a swtich to its inflammatory signaling role. PMID: 19007302
23. Multimerization of surfactant protein D, but not its collagen domain, is required for antiviral and opsonic activities related to influenza virus. PMID: 19017984

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KEGG: rno:25350

UniGene: Rn.11348