Nicholas A Delamere

Nicholas A Delamere

Department Head, Physiology
Professor, Physiology
Professor, Ophthalmology
Member of the Graduate Faculty
Professor, BIO5 Institute
Primary Department
Department Affiliations
Contact
(520) 626-6425

Research Interest

Nicholas Delamere, Ph.D., studies how ocular pressure (pressure in the eye) is controlled and the way cells transport fluid, and seeks to find methods to regulate the mechanisms involved. His goal is to develop drugs that reduce intraocular pressure, thereby decreasing the severity of glaucoma and damage to the retina. His cataract research also offers a promising model for tissue preservation, which will delay the onset of cataracts. https://delamerelab.medicine.arizona.edu/

Publications

Paterson, C. A., Delamere, N. A., Mawhorter, L., & Cuizon, J. V. (1983). Na,K-ATPase in simulated eye bank and cryoextracted rabbit lenses, and human eye bank lenses and cataracts. Investigative ophthalmology & visual science, 24(11), 1534-8.

In the rabbit, cryoextraction of the lens and subsequent storage in Tyrode's solution did not alter the Na,K-ATPase activity from that determined in immediately excised rabbit lenses. Similarly, the procedures employed with the rabbit eye to simulate collection and storage of normal human eyes (eye banking) had no effect upon the Na,K-ATPase activity of the lens. These results permitted the investigation of human lenses with the knowledge that measured Na,K-ATPase activity had not been altered grossly by any manipulation procedures. Analysis of Na,K-ATPase activity in 44 eye bank lenses, 14 primary nuclear cataracts, 11 primary cortical cataracts, 18 primary posterior subcapsular cataracts, and 31 mixed cataracts revealed no significant difference in the enzyme activity between these groups. Similarly, there was no correlation between electrolyte levels and Na,K-ATPase in a further 18 mixed cataracts. It is concluded that, despite an often pronounced electrolyte imbalance, human cataract can develop without significant alteration in Na,K-ATPase activity.