The necessity of functional proteomics: protein species and molecular function elucidation exemplified by in vivo alpha A crystallin N-terminal truncation.
Ten years after the establishment of the term proteome, the science surrounding it has yet to fulfill its potential. While a host of technologies have generated lists of protein names, there are only a few reported studies that have examined the individual proteins at the covalent chemical level defined as protein species in 1997 and their function. In the current study, we demonstrate that this is possible with two-dimensional gel electrophoresis (2-DE) and mass spectrometry by presenting clear evidence of in vivo N-terminal alpha A crystallin truncation and relating this newly detected protein species to alpha crystallin activity regulation by protease cleavage in the healthy young murine lens. We assess the present state of technology and suggest a shift in resources and paradigm for the routine attainment of the protein species level in proteomics.
Hoehenwarter
W
W
Max Planck Institute for Infection Biology, Core Facility Protein Analysis, Berlin, Germany.
Ackermann
R
R
Zimny-Arndt
U
U
Kumar
N M
NM
Jungblut
P R
PR
D000818:Animals; D015180:Electrophoresis, Gel, Two-Dimensional / Q000379:methods*; D007908:Lens, Crystalline / Q000737:chemistry; D051379:Mice; D017434:Protein Structure, Tertiary; D040901:Proteomics; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization / Q000379:methods*; D038202:alpha-Crystallin A Chain / Q000032:analysis* / Q000737:chemistry* / Q000302:isolation & purification
D038202:alpha-Crystallin A Chain