TL;DR: In vitro transcription-translation experiments suggest that co-translational modifications of two primary translation products account for many of the isoforms observed by two-dimensional gel electrophoresis in the precursors of 35,000-dalton sialoglycoproteins.
TL;DR: All common and rare variants of the surfactant protein A2, SP-A2, in both A549 cells and in primary type II alveolar epithelial cells are analyzed and it is shown that the mechanism of disease does not involve an overt lack of secretedSP-A but instead involves an increase in ER stress of resident type IIAlveolarhelial cells.
TL;DR: The occurrence of irregular disulfide links between individual oligomericSP-A molecules composed of alpha 3-chains together with the demonstrated presence of both gene products in natural human SP-A suggest that the subunits of SP-B are heterotrimers of one alpha 2- and two alpha 3 -chains.
Abstract: The pulmonary surfactant-associated protein SP-A is encoded by presumably two different genes, resulting in slightly different amino acid sequences. Both gene products were expressed in Chinese hamster ovary cells. Their macromolecular structure differed significantly. SP-Aα3 exhibited a much higher amount of tetrameric to hexameric structures than SP-Aα2, for which dimeric structures predominate. These differences may be caused by the higher expression rates of SP-Aα3 presumably due to the presence of introns in the sequence. The occurrence of irregular disulfide links between individual oligomeric SP-A molecules composed of α3-chains together with the demonstrated presence of both gene products in natural human SP-A suggest that the subunits of SP-A are heterotrimers of one α2- and two α3-chains.
TL;DR: A second human SP-A gene is isolated and characterized, which appears to code for the mRNA corresponding to the previously described MPSAP-1A cDNA, and significant divergence in the two genes is observed throughout.
Abstract: Pulmonary surfactant is a lipid-protein complex involved in maintaining alveolar stability SP-A is the major surfactant-associated protein of 26 to 38 kD A human SP-A gene (SP-A I) and two distinct SP-A cDNAs, MPSAP 1A and MPSAP 6A, have been reported previously We have isolated and characterized a second human SP-A gene (SP-A II), which appears to code for the mRNA corresponding to the previously described MPSAP-1A cDNA Both genes consist of five exons, a consensus recognition sequence for initiation, TATAAA, and a polyadenylation signal sequence Significant divergence in the two genes is observed throughout The divergence is highest in the upstream region, intron I, exon III, and noncoding portion of exon V The coding regions of all other exons and the introns show much lower divergence Transcripts from both genes were found in adult human lung, using gene-specific oligonucleotide probes in Northern blot analysis
TL;DR: The evidence gathered thus far indicates that SP-A, possibly by interacting with other surfactant components, may play a role in the development of respiratory disease.