scholarly journals Teleost and elasmobranch eye lenses as a target for life-history stable isotope analyses

PeerJ ◽  
2018 ◽  
Vol 6 ◽  
pp. e4883 ◽  
Author(s):  
Katie Quaeck-Davies ◽  
Victoria A. Bendall ◽  
Kirsteen M. MacKenzie ◽  
Stuart Hetherington ◽  
Jason Newton ◽  
...  

Incrementally grown, metabolically inert tissues such as fish otoliths provide biochemical records that can used to infer behavior and physiology throughout the lifetime of the individual. Organic tissues are particularly useful as the stable isotope composition of the organic component can provide information about diet, trophic level and location. Unfortunately, inert, incrementally grown organic tissues are relatively uncommon. The vertebrate eye lens, however, is formed via sequential deposition of protein-filled fiber cells, which are subsequently metabolically inert. Lenses therefore have the potential to serve as biochemical data recorders capturing life-long variations in dietary and spatial ecology. Here we review the state of knowledge regarding the structure and formation of fish eye lenses in the context of using lens tissue for retrospective isotopic analysis. We discuss the relationship between eye lens diameter and body size, describe the successful recovery of expected isotopic gradients throughout ontogeny and between species, and quantify the isotopic offset between lens protein and white muscle tissue. We show that fish eye lens protein is an attractive host for recovery of stable isotope life histories, particularly for juvenile life stages, and especially in elasmobranchs lacking otoliths, but interpretation of lens-based records is complicated by species-specific uncertainties associated with lens growth rates.

Biochemistry ◽  
2013 ◽  
Vol 52 (20) ◽  
pp. 3579-3587 ◽  
Author(s):  
Bryon Mahler ◽  
Yingwei Chen ◽  
Jason Ford ◽  
Caleb Thiel ◽  
Graeme Wistow ◽  
...  

2004 ◽  
Vol 30 (3) ◽  
pp. 385-386 ◽  
Author(s):  
Carine Baraguey ◽  
F�riel Skouri-Panet ◽  
Fran�ois Bontems ◽  
Annette Tardieu ◽  
G�rard Chassaing ◽  
...  

2018 ◽  
Author(s):  
Eugene Serebryany ◽  
Shuhuai Yu ◽  
Sunia A. Trauger ◽  
Bogdan Budnik ◽  
Eugene I. Shakhnovich

AbstractSeveral mutations in human γD-crystallin (HγD), a long-lived eye lens protein, cause misfolding and aggregation, leading to cataract. Surprisingly, wild-type HγD catalyzes aggregation of its cataract related W42Q variant while itself remaining soluble – the inverse of the classical prion-like scenario whereby misfolded polypeptides catalyze aggregation of natively folded ones. The search for a biochemical mechanism of catalysis of W42Q aggregation by WT has revealed that WT HγD can transfer a disulfide bond to the W42Q variant. The transferred disulfide kinetically traps an aggregation-prone intermediate made accessible by the W42Q mutation, facilitating light-scattering aggregation of the W42Q variant. The aggregating variant thus becomes a disulfide sink, removing the disulfides from solution. Such redox “hot potato” competitions among wild-type and mutant or modified polypeptides may be relevant for many long-lived proteins that function in oxidizing environments. In these cases aggregation may be forestalled by inhibiting disulfide flow toward damaged polypeptides.


1985 ◽  
Vol 147 (1) ◽  
pp. 129-136 ◽  
Author(s):  
Steven O. STAPEL ◽  
Anneke ZWEERS ◽  
Huub J. DODEMONT ◽  
Jaap H. KAN ◽  
Wilfried W. JONG

1987 ◽  
Vol 498 (1 Third Confere) ◽  
pp. 460-463 ◽  
Author(s):  
J. BLONDIN ◽  
V. BARAGI ◽  
E. R. SCHWARTZ ◽  
J. A. SADOWSKI ◽  
A. TAYLOR

2001 ◽  
Vol 52 (3) ◽  
pp. 239-248 ◽  
Author(s):  
Martinus A.M. van Boekel ◽  
Daan M.F. van Aalten ◽  
Gert-Jan Caspers ◽  
Beate Röll ◽  
Wilfried W. de Jong

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