Protein-bound γ-glutamylpolyamines have highlighted a new pathway in polyamine metabolism. Human foreskin keratinocytes offer a suitable model for this study. Indeed, they develop polymerized envelopes, as they differentiate, rich in ϵ-(γ-glutamyl)lysine and N1,N8-bis(γ-glutamyl)spermidine cross-links. We have found that the selective oxidation of N1-(γ-glutamyl)spermidine and N-(γ-glutamyl)spermine by FAD-dependent polyamine oxidase (PAO) may be one of the cellular mechanisms regulating the preferential formation of a sterically defined bis(γ-glutamyl)spermidine cross-link. The significance of this finding is unknown, but it suggests that the target of this PAO-modulation is to achieve the biochemical prerequisite for production of a normal epidermal stratum corneum.
Role of the FAD-dependent polyamine oxidase in the selective formation of N1,N8-bis(γ- glutamyl)spermidine protein cross-links1
A. Lentini, P. Mattioli, B. Provenzano, A. Abbruzzese, M. Caraglia, S. Beninati; Role of the FAD-dependent polyamine oxidase in the selective formation of N1,N8-bis(γ- glutamyl)spermidine protein cross-links. Biochem Soc Trans 1 April 2007; 35 (2): 396–400. doi: https://doi.org/10.1042/BST0350396
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