Rat Pulmonary Surfactant-associated protein D (SP-D) ELISA kit

Contributes to the lung's defense against inhaled microorganisms, organic antigens and toxins. Interacts with compounds such as bacterial lipopolysaccharides, oligosaccharides and fatty acids and modulates leukocyte action in immune response. May participate in the extracellular reorganization or turnover of pulmonary surfactant. Binds strongly maltose residues and to a lesser extent other alpha-glucosyl moieties.

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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Secreted, extracellular space, extracellular matrix. Secreted, extracellular space, surface film.

SFTPD family

KEGG: rno:25350

UniGene: Rn.11348