Disease relevance of SP-D

• Interactions of influenza A virus with sialic acids present on porcine surfactant protein D [1].
• We report a new bleeding disease--storage pool deficiency (SPD) of platelets--in pigs from the Mayo swine colony of homozygous von Willebrand's disease (vWD) and of heterozygous carriers of vWD [2].

High impact information on SP-D

• Platelet aggregation in response to collagen was reduced in most SPD pigs [2].
• While the initial uptake of 14C-labeled serotonin into platelets was similar in SPD and normal pigs, retention of serotonin was reduced in platelets of SPD pigs [2].
• The difference in mass is due to the presence of an Asparagine-linked glycosylation in the carbohydrate recognition domain of porcine SP-D, which is absent in SP-D of other species investigated so far [3].
• Our present aim was to establish the sites of SP-A and SP-D expression within the epithelium of the ET in vivo [4].
• Recently, we described the expression of SP-A and SP-D in the ET, suggesting their role in middle ear host defense [5].

Biological context of SP-D

• Surfactant protein D (SP-D) is a collectin believed to play an important role in innate immunity [6].
• Assignment of surfactant protein A (SFTPA) and surfactant protein D (SFTPD) to pig chromosome band 14q25-->q26 by in situ hybridization [7].

Anatomical context of SP-D

• SP-D immunoreactivity was intracellular in dendritic cells [8].
• Surfactant protein D (SP-D) is a pattern-recognition molecule of the innate immune system that recognizes various microbial surface-specific carbohydrate and lipid patterns [8].

Other interactions of SP-D

• In lavage, only SP-D, alpha (2)-macroglobulin and fibronectin were detected [9].

Analytical, diagnostic and therapeutic context of SP-D

• This report documents the isolation and characterization of SP-D purified from porcine lung lavage using mannan affinity chromatography and gel filtration [3].
• With in situ hybridization, electron microscopy, and immunoelectron microscopy, the cells responsible for SP-A and SP-D expression and storage were identified [4].
• The SP-A and SP-D immunoreactivities in ET lavage fluid, as shown by Western blot analyses, were similar to those in bronchoalveolar lavage fluid [4].
• Porcine SP-D was purified from porcine bronchoalveolar lavage (BAL) by maltose-agarose and immunoglobulin M affinity chromatography [6].
• Transmission electron microscopy showed a large decrease of dense bodies in the platelets of SPD pigs [2].

References