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. 2005 Mar 18;32(6):521–530. doi: 10.1165/rcmb.2005-0009OC

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Copyright © 2005, American Thoracic Society

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Figure 1. — Wild-type SP-C is trafficked to vesicles distal to the Golgi independent of cell type. (A) Amino acid sequence of the human SP-C pro-protein showing cytosolic, transmembrane, luminal, and BRICHOS domains. The secreted mature SP-C, the BRICHOS domain (hatched oval circle), and mutations found in association with ILD are shown. The Δexon 4 BRICHOS domain mutation and a non–BRICHOS domain mutation analyzed in the present study are highlighted in gray. The BRICHOS domain flanks the C-terminal starting at phenylalanine 94. Amino acid nomenclature is based on the published SP-C sequence (31). (B) A549, MLE, and HEK cells transiently transfected with EGFP/SP-C^WT (top row) show similarities in vesicular co-localization (bottom row) with Texas Red–conjugated CD63 (middle row) antibody. Bar, 5 μm.

Figure 1. — Wild-type SP-C is trafficked to vesicles distal to the Golgi independent of cell type. (A) Amino acid sequence of the human SP-C pro-protein showing cytosolic, transmembrane, luminal, and BRICHOS domains. The secreted mature SP-C, the BRICHOS domain (hatched oval circle), and mutations found in association with ILD are shown. The Δexon 4 BRICHOS domain mutation and a non–BRICHOS domain mutation analyzed in the present study are highlighted in gray. The BRICHOS domain flanks the C-terminal starting at phenylalanine 94. Amino acid nomenclature is based on the published SP-C sequence (31). (B) A549, MLE, and HEK cells transiently transfected with EGFP/SP-C^WT (top row) show similarities in vesicular co-localization (bottom row) with Texas Red–conjugated CD63 (middle row) antibody. Bar, 5 μm.