Distinct energy metabolism of auditory and vestibular sensory epithelia revealed by quantitative mass spectrometry using MS2 intensity.
Measuring the abundance of many proteins over a broad dynamic range requires accurate quantitation. We show empirically that, in MS experiments, relative quantitation using summed dissociation-product ion-current intensities is accurate, albeit variable from protein to protein, and outperforms spectral counting. By applying intensities to quantify proteins in two complex but related tissues, chick auditory and vestibular sensory epithelia, we find that glycolytic enzymes are enriched threefold in auditory epithelia, whereas enzymes responsible for oxidative phosphorylation are increased at least fourfold in vestibular epithelia. This striking difference in relative use of the two ATP-production pathways likely reflects the isolation of the auditory epithelium from its blood supply, necessary to prevent heartbeat-induced mechanical disruptions. The global view of protein expression afforded by label-free quantitation with a wide dynamic range reveals molecular specialization at a tissue or cellular level.
Oregon Hearing Research Center, Vollum Institute, Proteomics Shared Resource, Oregon Health and Science University, Portland, OR 97239, USA.
Kateri J
KJ
Spinelli
John E
JE
Klimek
Phillip A
PA
Wilmarth
Jung-Bum
JB
Shin
Dongseok
D
Choi
Larry L
LL
David
Peter G
PG
Gillespie
D000255:Adenosine Triphosphate / Q000096:biosynthesis; D000818:Animals; D002645:Chickens; D002853:Chromatography, Liquid; D003051:Cochlea / Q000098:blood supply / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D004734:Energy Metabolism; D004848:Epithelium / Q000378:metabolism; D006019:Glycolysis; D018919:Neovascularization, Physiologic; D011506:Proteins / Q000235:genetics / Q000378:metabolism; D012333:RNA, Messenger / Q000235:genetics; D053719:Tandem Mass Spectrometry; D014722:Vestibule, Labyrinth / Q000378:metabolism*
D011506:Proteins; D012333:RNA, Messenger; D000255:Adenosine Triphosphate