Vertebrate-like betagamma-crystallins in the ocular lenses of a copepod.
The diverse crystallins are water-soluble proteins that are responsible for the optical properties of cellular lenses of animal eyes. While all vertebrate lenses contain physiological stress-related alpha- and betagamma-crystallins, some also contain taxon-specific, often enzyme-related crystallins. To date, the alpha- and betagamma-crystallins have been found only in vertebrate lenses. Here we report lenses from an invertebrate, the pontellid copepod Anomalocera ornata, accumulate betagamma-crystallin family members as judged by immunocytochemistry, western immunoblotting and microsequencing. Our data provide the first example of betagamma-crystallin members in an invertebrate lens, establishing that the use of this protein family as lens crystallins is not confined to vertebrates.
Cohen
Jonathan H
JH
Duke University Marine Laboratory and Department of Biology, Duke University, Beaufort, NC 28516, USA. jcohen@hboi.edu
Piatigorsky
Joram
J
Ding
Linlin
L
Colley
Nansi J
NJ
Ward
Rebecca
R
Horwitz
Joseph
J
D000595:Amino Acid Sequence; D000818:Animals; D015153:Blotting, Western / Q000379:methods; D002417:Cattle; D033342:Copepoda; D006801:Humans; D007150:Immunohistochemistry / Q000379:methods; D007908:Lens, Crystalline / Q000378:metabolism*; D051381:Rats; D038204:beta-Crystallins / Q000378:metabolism*; D038222:gamma-Crystallins / Q000378:metabolism*
D038204:beta-Crystallins; D038222:gamma-Crystallins