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Prog Retin Eye Res. 2019 Sep 4:100777. doi: 10.1016/j.preteyeres.2019.100777. [Epub ahead of print]

Membrane-associated mucins of the ocular surface new genes, new protein functions and new biological roles in human and mouse.

Author information

1
Department of Ophthalmology, Tufts University School of Medicine, At New England Eye Center, Tufts Medical Center, 800 Washington St, Boston, MA, 02111, USA. Electronic address: mefini@tuftsmedicalcenter.org.
2
USC Roski Eye Institute and Department of Ophthalmology, Keck School of Medicine of USC, University of Southern California, 1975 Zonal Ave, Los Angeles, CA, 90033, USA. Electronic address: shinwuje@med.usc.edu.
3
Department of Ophthalmology, Boston University School of Medicine, 72 E Concord St, Boston, MA02118, USA. Electronic address: haiyan2k@yahoo.com.
4
Department of Ophthalmology, Tufts University School of Medicine, At New England Eye Center, Tufts Medical Center, 800 Washington St, Boston, MA, 02111, USA. Electronic address: rmartinezcarras@tuftsmedicalcenter.org.
5
Department of Ophthalmology, Tufts University School of Medicine, At New England Eye Center, Tufts Medical Center, 800 Washington St, Boston, MA, 02111, USA. Electronic address: nlaver@tuftsmedicalcenter.org.
6
Department of Pathophysiology and Host Defense, The Research Institute of Tuberculosis, Japan Anti-Tuberculosis Association, 3-1-24 Matsuyama, Kiyose-shi, Tokyo, 204-8533, Japan. Electronic address: mhijikata@jata.or.jp.
7
Department of Pathophysiology and Host Defense, The Research Institute of Tuberculosis, Japan Anti-Tuberculosis Association, 3-1-24 Matsuyama, Kiyose-shi, Tokyo, 204-8533, Japan. Electronic address: nkeicho@jata.or.jp.
8
Department of Ophthalmology, Harvard Medical School, At Schepens Eye Research Institute of Mass. Eye and Ear, 20 Staniford St, Boston, MA, 02114, USA. Electronic address: Pablo_Argueso@MEEI.HARVARD.EDU.

Abstract

The mucosal glycocalyx of the ocular surface constitutes the point of interaction between the tear film and the apical epithelial cells. Membrane-associated mucins (MAMs) are the defining molecules of the glycocalyx in all mucosal epithelia. Long recognized for their biophysical properties of hydration, lubrication, anti-adhesion and repulsion, MAMs maintain the wet ocular surface, lubricate the blink, stabilize the tear film and create a physical barrier to the outside world. However, it is increasingly appreciated that MAMs also function as cell surface receptors that transduce information from the outside to the inside of the cell. A number of excellent review articles have provided perspective on the field as it has progressed since 1987, when molecular cloning of the first MAM was reported. The current article provides an update for the ocular surface, placing it into the broad context of findings made in other organ systems, and including new genes, new protein functions and new biological roles. We discuss the epithelial tissue-equivalent with mucosal differentiation, the key model system making these advances possible. In addition, we make the first systematic comparison of MAMs in human and mouse, establishing the basis for using knockout mice for investigations with the complexity of an in vivo system. Lastly, we discuss findings from human genetics/genomics, which are providing clues to new MAM roles previously unimagined. Taken together, this information allows us to generate hypotheses for the next stage of investigation to expand our knowledge of MAM function in intracellular signaling and roles unique to the ocular surface.

KEYWORDS:

Epithelial tissue-equivalent; Glycocalyx; Knockout mouse; Membrane-associated mucin; Ocular surface; Signal transduction

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