Lamellar Structures of MUC2-Rich Mucin: A Potential Role in Governing the Barrier and Lubricating Functions of Intestinal Mucus

Round, Andrew N., Rigby, Neil M., Garcia de la Torre, Angela, Macierzanka, Adam, Mills, E. N. Clare and Mackie, Alan R. (2012) Lamellar Structures of MUC2-Rich Mucin: A Potential Role in Governing the Barrier and Lubricating Functions of Intestinal Mucus. Biomacromolecules, 13 (10). pp. 3253-3261. ISSN 1525-7797

[img]
Preview
PDF (bm301024x.pdf)
Download (4MB) | Preview

Abstract

Mucus is a ubiquitous feature of mammalian wet epithelial surfaces, where it lubricates and forms a selective barrier that excludes a range of particulates, including pathogens, while hosting a diverse commensal microflora. The major polymeric component of mucus is mucin, a large glycoprotein formed by several MUC gene products, with MUC2 expression dominating intestinal mucus. A satisfactory answer to the question of how these molecules build a dynamic structure capable of playing such a complex role has yet to be found, as recent reports of distinct layers of chemically identical mucin in the colon and anomalously rapid transport of nanoparticles through mucus have emphasized. Here we use atomic force microscopy (AFM) to image a MUC2-rich mucus fraction isolated from pig jejunum. In the freshly isolated mucin fraction, we find direct evidence for trigonally linked structures, and their assembly into lamellar networks with a distribution of pore sizes from 20 to 200 nm. The networks are two-dimensional, with little interaction between lamellae. The existence of persistent cross-links between individual mucin polypeptides is consistent with a non-self-interacting lamellar model for intestinal mucus structure, rather than a physically entangled polymer network. We only observe collapsed entangled structures in purified mucin that has been stored in nonphysiological conditions.

Item Type: Article
Faculty \ School: Faculty of Science > School of Pharmacy
Depositing User: Andrew Round
Date Deposited: 25 Jan 2013 22:54
Last Modified: 21 Sep 2020 23:25
URI: https://ueaeprints.uea.ac.uk/id/eprint/39857
DOI: 10.1021/bm301024x

Actions (login required)

View Item View Item