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Publication Detail
Mass spectrometry identification of circulating alpha-1-B glycoprotein, increased in aged female C57BL/6 mice1
  • Publication Type:
    Journal article
  • Publication Sub Type:
  • Authors:
    Stehle Jr JR, Weeks ME, Lin K, Willingham MC, Hicks AM, Timms JF, Cui Z
  • Publication date:
  • Pagination:
    79, 86
  • Journal:
  • Volume:
  • Issue:
  • Keywords:
    1, A, AGE, Aged, analysis, AND, ARTICLE, As, Extramural, Female, Gel, IM, IS, JOURNAL, LA, LEVEL, Male, MALES, Mass, Mice, OF, OLDER, pathology, Phosphorylation, Proteins, Research Support, Result, Spectrometry, Support, THE
  • Addresses:
    Department of Pathology, Wake Forest University School of Medicine, Winston-Salem, NC 27157, USA
  • Notes:
    DA - 20061220IS - 0006-3002 (Print)LA - engPT - Journal ArticlePT - Research Support, N.I.H., ExtramuralSB - IM
In this study, we surveyed the profiles of mouse circulating proteins by 2-dimensional SDS-PAGE in different strains, sexes and ages. Among visible protein spots on 2-D gels with silver-staining, we identified a unique set of 7 seemingly-related proteins whose levels were consistently elevated in older C57BL/6 female mice. This set of 7 proteins was absent in C57BL/6 males or in BALB/c mice of either sex of any age. When C57BL/6 female mice were crossed with BALB/c males, the age-related increase of these proteins became sporadic and not linear in the F1 offspring. All 7 spots of this protein group were picked and subjected to identification by mass spectrometric analysis after tryptic digestion. The results showed that all 7 spots were different isoforms of alpha(1)B-glycoprotein with different degrees of post-translational modifications, such as phosphorylation. These results suggest that alpha(1)B-glycoprotein changes in mice in a sex and age dependent manner
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