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Human Erythrocyte D-Aspartyl/L-Isoaspartyl Methyltransferases: Enzymes that Recognize Age-Damaged Proteins

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Red Blood Cell Aging

Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 307))

Abstract

Among the large number of protein post-biosynthetic modifications described so far are a group of non-enzymatic reactions that reflect the spontaneous, intrinsic, decomposition of these macromolecules as they age in cells. These alterations include oxidation (1), formation of advanced glycosylation end products (2), and linked deamination/isomerization/ racemization reactions (3). Our interest has been focused on the latter reactions that lead to the loss of L-aspartyl and L-asparaginyl residues in proteins and the recognition of the damaged proteins by enzymes that can lead to their cellular removal by repair or degradation reactions (4–9).

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Author information

Authors and Affiliations

  1. Istituto di Biochimica delle Macromolecole I Facoltà di Medicina e Chirurgia, Università di Napoli, Napoli, Italy

    Diego Ingrosso

  2. Department of Chemistry and Biochemistry and the Molecular Biology Institute, University of California Los Angeles, Los Angeles, California, USA

    Diego Ingrosso & Steven Clarke

Authors
  1. Diego Ingrosso
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  2. Steven Clarke
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Editor information

Editors and Affiliations

  1. University of Urbino, Urbino, Italy

    Mauro Magnani

  2. University of Genoa, Genoa, Italy

    Antonio De Flora

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© 1991 Plenum Press, New York

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Ingrosso, D., Clarke, S. (1991). Human Erythrocyte D-Aspartyl/L-Isoaspartyl Methyltransferases: Enzymes that Recognize Age-Damaged Proteins. In: Magnani, M., De Flora, A. (eds) Red Blood Cell Aging. Advances in Experimental Medicine and Biology, vol 307. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-5985-2_24

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  • DOI: https://doi.org/10.1007/978-1-4684-5985-2_24

  • Publisher Name: Springer, Boston, MA

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