Disease relevance of Sftpd

• Wild-type B. pertussis and B. bronchiseptica were both resistant to SP-D; however, LPS mutants of either strain lacking the terminal trisaccharide were aggregated and permeabilized by SP-D [1].
• We conclude that the terminal trisaccharide protects Bordetella species from the bactericidal functions of SP-A and SP-D [1].
• We hypothesized that SP-A and SP-D would respond to an acute stress, such as lung inflammation, in the same manner as does mannose-binding protein, with increased messenger ribonucleic acid (mRNA) and protein production [2].
• We also found that the relative content of SP-D was significantly higher in PCP (24,249 +/- 4780 grey values) than that in the negative control (13,384 +/- 2887 grey values, P < 0.001) and that in bacterial pneumonia (11,989 +/- 2750 grey values, P < 0.001) [3].
• Twenty-one hours after ischemia, axonal damage was reduced by 45% (P = 0.006) in the SPD 502-treated group compared with the vehicle [4].

Psychiatry related information on Sftpd

• The REM (rapid eye movement) sleep stage was significantly shortened without a marked change of the Non-REM sleep from the 24th to the 32nd hr following injection of 40 microgram of SPD [5].

High impact information on Sftpd

• Lastly, we show that SP-D augments binding of P. carinii to alveolar macrophages, but does not significantly enhance macrophage phagocytosis of the organism [6].
• Accordingly, we evaluated the extent and localization of SP-D in the lower respiratory tract during Pneumocystis pneumonia in an immunosuppressed rat model and examined its role in modulating interaction of P. carinii with macrophages [6].
• We report that SP-D is a major component of the alveolar exudates that typify P. carinii pneumonia and is present bound to the surface of P. carinii organisms in vivo [6].
• The interaction of SP-D with gpA represents an additional important component of the host-parasite relationship during P. carinii pneumonia [6].
• Surfactant protein D (SP-D) is a recently described component of the airspace lining material that possesses a calcium-dependent lectin domain capable of interacting with glycoconjugates present on microorganisms and leukocytes [6].

Chemical compound and disease context of Sftpd

• CONCLUSION: SP-D accumulation is increased in this model of allergen-induced eosinophilia, both in upper and lower airways [7].
• They also confirmed the results of other studies that demonstrated the safety of the introduced protein, a bacterial 5-enolpyruvyl-shikimate-3-phosphate synthase from Agrobacterium sp. strain CP4 [8].

Biological context of Sftpd

• SP-D gene expression is tissue specific in the 14 tissues studied [9].
• Surfactant protein D (SP-D) (CP4) is a collagenous surfactant-associated carbohydrate binding protein that is synthesized and secreted by alveolar epithelial cells [10].
• From these results, we conclude that 1) the SP-A region of Glu195-Phe228 is required for lipid and type II cell interactions, 2) the SP-D region of Cys261-Phe355 is required for optimal lipid interactions, and 3) the structural requirement for the binding of SP-D to PI is different from that for GlcCer [11].
• SP-D binds to phosphatidylinositol (PI) and glucosylceramide (GlcCer), and its role in alveolar lipid metabolism remains to be clarified [12].
• In contrast, SP-D did not mediate phagocytosis [13].

Anatomical context of Sftpd

• Heterogeneous allele expression of pulmonary SP-D gene in rat large intestine and other tissues [9].
• Immunoperoxidase localization of SP-D studies at 2 weeks after silica instillation showed intense staining of intra-alveolar exudates, and cytoplasmic staining of hypertrophic type II cells [10].
• Immunoelectron microscopy showed that airspace SP-D was specifically associated with granular material, but not tubular myelin or other membranous structures [10].
• Surfactant proteins A (SP-A) and D (SP-D) are lung collectins that are constituents of the innate immune system of the lung [14].
• The opsonic activities of SP-A and SP-D for bacteria with different types of LPS and alveolar macrophages were investigated [13].

Associations of Sftpd with chemical compounds

• SP-D decreased CD14 binding to both smooth and rough LPS, whereas SP-A enhanced CD14 binding to rough LPS and inhibited binding to smooth LPS [14].
• Chimera A1A2D3D4 competed with iodinated SP-D in the solid phase binding assay to both PI and GlcCer [12].
• Mannose and EDTA inhibited SP-D binding to CD14 but did not decrease SP-A binding [14].
• Both proteins are composed of four characteristic domains which are: 1) an NH2-terminal domain involved in interchain disulfide formation (denoted A1 domain for SP-A or D1 for SP-D); 2) a collagenous domain (denoted A2 or D2); 3) a neck domain (denoted A3 or D3); and 4) a carbohydrate recognition domain (denoted A4 or D4) [12].
• Here we report that newborn rats, which can adapt to even higher levels of hyperoxia (100% O(2)) than do adult rats, manifest changes in the lung surfactant proteins (SP), especially SP-A and SP-D [15].

Other interactions of Sftpd

• In situ hybridization studies demonstrated increases in SP-D, and to a lesser extent in SP-A, in peripheral lung tissues from oxygen-exposed newborns [15].
• This pattern of SP-D mRNA expression was compared with the expression of the other surfactant proteins and found to be most similar to that of SP-B [16].
• By contrast, SP-C and SP-D mRNAs were maximally increased relative to values in simultaneously air-exposed control rats after 4 d of exposure [15].
• We investigated the cellular and subcellular distribution of surfactant protein D (SP-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 [17].

Analytical, diagnostic and therapeutic context of Sftpd

• Within 2 weeks after silica instillation, there was a greater than 45-fold increase in lavage SP-D per lung compared with saline controls, including an almost ten-fold increase in the insoluble or surfactant-associated protein [10].
• SP-D was quantified in bronchoalveolar lavage by immunoassay using antibodies specific for SP-D, and by reversephase HPLC after affinity purification of SP-D on maltosyl-agarose [10].
• These studies indicate that the extracellular accumulation of SP-D is markedly increased in silica-induced lipoproteinosis, and that SP-D is associated with amorphous components identified by electron microscopy [10].
• The authors examined the accumulation of SP-D using this animal model of alveolar proteinosis [10].
• SP-D mRNA expression was evaluated by Northern blot analysis [16].

References