Clinical Chemistry 56: 202-211, 2010. First published November 19, 2009; 10.1373/clinchem.2009.134858
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(Clinical Chemistry. 2010;56:202-211.)
© 2010 American Association for Clinical Chemistry, Inc.

Mini-Reviews

Full-Length Characterization of Proteins in Human Populations

Chad R. Borges1, Doug S. Rehder1, Jason W. Jarvis1, Mathew R. Schaab1, Paul E. Oran1 and Randall W. Nelson1,a

1 The Biodesign Institute, Arizona State University, Tempe, AZ.

aAddress correspondence to this author at: Molecular Biomarkers, The Biodesign Institute at Arizona State University, P.O. Box 876601, Tempe, AZ 85287. Fax 480-727-9464; e-mail randal.nelson{at}asu.edu.


Abstract

Background: Diversity in human proteins often gives rise to pluralities of structurally similar but functionally distinct proteins. Such microheterogeneity generally escapes proteomics discovery technologies, as well as conventional immunometric assays. As an intermediate between these 2 technological approaches, targeted, full-length characterization of proteins using mass spectrometry is a suitable means of defining microheterogeneity evident in human populations.

Content: We describe and explore the implications of microheterogeneity using the exemplar of human vitamin D binding protein (Gc-Globulin) as observed in cohorts of 400 individuals. Our investigations yielded: (a) population frequency data comparable to genotyping; (b) population frequency data for protein variants, with and without genotype linkage; (c) reference values for the different protein variants per cohort and genotype; and (d) associations between variant, frequency, relative abundance, and diseases.

Summary: With the exception of the genotype frequency, such population data are unique and illustrate a need to more fully understand the exact full-length qualitative and quantitative idiosyncrasies of individual proteins in relation to health and disease as part of the standardized biomarker development and clinical proteomic investigation of human proteins.




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