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- W1492154178 abstract "Surfactant protein C (SP-C) is a small lipopeptide of which the main part consists of a typical valyl-rich transmembrane domain. The protein is expressed as a propeptide (proSP-C) which is processed and sorted via the regulated secretory pathway to the lamellar body, where mature SP-C is stored before secretion into the alveolar space. In this study we investigated the identity of the compartment to which proSP-C is sorted in cells that do not have a regulated secretory pathway, such as CHO cells. By electron microscopy we determined that proSP-C was localized in an uncommon membrane compartment with very regular morphology, which was not present in control cells. This membrane compartment is not influenced by the palmitoylation of proSP-C and is probably derived from the endoplasmic reticulum. However, proSP-C chimeras with artificial transmembrane domains induced a membrane compartment with a different morphology. Therefore we propose that the typical amino acid sequence of the transmembrane domain of proSP-C plays a role in membrane formation and morphology, which may be relevant under physiological conditions." @default.
- W1492154178 created "2016-06-24" @default.
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- W1492154178 date "2003-06-01" @default.
- W1492154178 modified "2023-09-26" @default.
- W1492154178 title "The transmembrane domain of surfactant protein C precursor determines the morphology of the induced membrane compartment in CHO cells" @default.
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- W1492154178 doi "https://doi.org/10.1078/0171-9335-00320" @default.
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