Membrane structures and functional correlates in the bi-segmented eye lens of the cephalopod

Author:

Regini Justyn W.1ORCID,Yagi Naoto2,Young Robert D.1,Tanioka Hidetoshi3,Kinoshita Shigeru3ORCID,Hoshino Masato2,Uesugi Kentaro2,Meek Keith M.1,Augousti Andy T.4,Knupp Carlo1,Pierscionek Barbara K.5,Quantock Andrew J.1,Elliott Gerald F.1

Affiliation:

1. Cardiff Centre for Vision Science, School of Optometry and Vision Sciences, Cardiff University 1 Structural Biophysics Group , , Maindy Road, Cardiff, CF24 4HQ , Wales, UK

2. SPring-8, Japan Synchrotron Radiation Research Institute 2 , 1-1-1, Kouto, Sayo-cho, Sayo-gun, Hyogo, 679-5198 Japan

3. Kyoto Prefectural University of Medicine, Hirokoji Kawaramachi 3 Department of Ophthalmology , , Kyoto, 602-0841 , Japan

4. Kingston University London 4 Faculty of Science, Engineering and Computing , , Friars Avenue, London SW15 , UK

5. Medical Technology Research Centre, Anglia Ruskin University 5 Faculty of Health Medicine and Social Care , , Bishop Hall Lane, Chelmsford CM1 1SQ , UK

Abstract

ABSTRACT The cephalopod eye lens is unique because it has evolved as a compound structure with two physiologically distinct segments. However, the detailed ultrastructure of this lens and precise optical role of each segment are far from clear. To help elucidate structure–function relationships in the cephalopod lens, we conducted multiple structural investigations on squid. Synchrotron x-ray scattering and transmission electron microscopy disclose that an extensive network of structural features that resemble cell membrane complexes form a substantial component of both anterior and posterior lens segments. Optically, the segments are distinct, however, and Talbot interferometry indicates that the posterior segment possesses a noticeably higher refractive index gradient. We propose that the hitherto unrecognised network of membrane structures in the cephalopod lens has evolved to act as an essential conduit for the internal passage of ions and other metabolic agents through what is otherwise a highly dense structure owing to a very high protein concentration.

Funder

Spring-8 beamtime access awards

Great Britain Sasakawa Foundation

Fight for Sight

Cardiff University

Publisher

The Company of Biologists

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