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Calcium and pH-dependent packing and release of the gel-forming MUC2 mucin.

Artikel i vetenskaplig tidskrift
Författare Daniel Ambort
Malin E V Johansson
Jenny K Gustafsson
Harriet E Nilsson
Anna Ermund
Bengt R Johansson
Philip J B Koeck
Hans Hebert
Gunnar C. Hansson
Publicerad i Proceedings of the National Academy of Sciences of the United States of America
Volym 109
Nummer/häfte 15
Sidor 5645-50
ISSN 1091-6490
Publiceringsår 2012
Publicerad vid Institutionen för biomedicin, avdelningen för medicinsk kemi och cellbiologi
Sidor 5645-50
Språk en
Länkar dx.doi.org/10.1073/pnas.1120269109
Ämnesord Animals, CHO Cells, Calcium, metabolism, Cricetinae, Cricetulus, Gels, metabolism, Goblet Cells, metabolism, ultrastructure, Hydrogen-Ion Concentration, Mice, Mice, Inbred C57BL, Models, Molecular, Mucin-2, chemistry, metabolism, ultrastructure, Protein Structure, Tertiary
Ämneskategorier Cell- och molekylärbiologi

Sammanfattning

MUC2, the major colonic mucin, forms large polymers by N-terminal trimerization and C-terminal dimerization. Although the assembly process for MUC2 is established, it is not known how MUC2 is packed in the regulated secretory granulae of the goblet cell. When the N-terminal VWD1-D2-D'D3 domains (MUC2-N) were expressed in a goblet-like cell line, the protein was stored together with full-length MUC2. By mimicking the pH and calcium conditions of the secretory pathway we analyzed purified MUC2-N by gel filtration, density gradient centrifugation, and transmission electron microscopy. At pH 7.4 the MUC2-N trimer eluted as a single peak by gel filtration. At pH 6.2 with Ca(2+) it formed large aggregates that did not enter the gel filtration column but were made visible after density gradient centrifugation. Electron microscopy studies revealed that the aggregates were composed of rings also observed in secretory granulae of colon tissue sections. The MUC2-N aggregates were dissolved by removing Ca(2+) and raising pH. After release from goblet cells, the unfolded full-length MUC2 formed stratified layers. These findings suggest a model for mucin packing in the granulae and the mechanism for mucin release, unfolding, and expansion.

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