Graduate Studies Faculty

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Larry David, PhD

Adjunct Professor
Admin Unit: SOM-Biochemistry & Molecular Biology Department
Phone: 503-494-8774
Fax: 503-494-8393
Office: SOD 401
Mail Code: L224
Biochemistry & Molecular Biology
Program in Molecular & Cellular Biosciences
Cancer Biology
Research Interests:
» PubMed Listing
Preceptor Rotations
Dr. David has not indicated availability for preceptor rotations at this time.
Faculty Mentorship
Dr. David has not indicated availability as a mentor at this time.

1982-86           Research Assistant, Dept. of Biochemistry, School of Medicine, Oregon Health and Sciences University, Portland, OR

1986-92           Assistant Professor, Depts. of Biochemistry and Opthamology, Schools of Dentistry and Medicine, OHSU

1992-2000       Associate Professor (OHSU)

2000-Present    Professor (OHSU)

Other Experience

Ad Hoc member of National Eye Institute VISA-1 Study Section, Feb 1999

Special Emphasis Panel, Center for Scientific Review, National Institutes of Health, July 1999

Adjunct Professorship, 1999-Present, Department of Animal Science, Oregon State University, Corvallis, OR  

1999-2000 President of Oregon Health and Sciences University Faculty Senate

2001-Present Director, Mass spectrometry and Proteomics Module, OHSU Casey Eye Institute

2003-Present Supervisor, Metallobiochemistry Mass Spectrometry Core facility, OHSU School of Medicine


2003 OHSU Faculty Senate Outstanding Research Award


Cataracts result from any opacification of the normally clear lens of the eye. Since cataracts are a leading cause of blindness, studies determining the cause of cataract are an active area of vision research. Our interest is in the changes occurring in the structural proteins of the lens when cataracts form. These structural proteins are called crystallins. Crystallins are some of the oldest proteins found in the body, since ones found in the center of the lens were synthesized before birth and remain with us for our entire lives. Due to their age, these proteins undergo extensive modifications, including proteolytic cleavage, deamidation, phosphorylation, and oxidation. The challenge in this research is to distinguish between normal age-related modifications and unique modifications causing cataract. To make this distinction, my group analyzes the structure of crystallins using mass spectrometry. Measurement of the molecular mass of the crystallins and their peptides allows an unambiguous identification of their modifications. Once the modifications unique to crystallins from cataractous lenses are known, it will be possible to model how the alterations cause these proteins to lose their normal transparency. Hopefully, this information will be used to help develop agents to slow the rate of cataract formation.

Mass spectrometric analysis is also useful to identify and analyze proteins in other research projects. Our future interest is in the growing field of proteomics, which uses mass spectrometry to both identify proteins and quantify changes in their relative abundance during disease. This field becomes increasingly important as new genes are sequenced and complete databases of all proteins found in humans and other species becomes available. A growing interest of our group is to develop new methodologies to measure global changes in relative protein abundance in complex protein mixtures using stable isotope tagging of peptides. These analysis provide opportunities for research using both biochemical and informatics tools.