D-Asp-containing proteins have been implicated in many aging-related diseases. To clarify the role of D-Asp-containing proteins in such diseases, we developed a screening system for these proteins using a D-aspartyl endopeptidase that specifically cleaves the proteins at the C-terminus. The digested proteins were detected by means of two-dimensional gel electrophoresis and identified using nano-liquid chromatography/tandem mass spectrometry. We were able to detect myelin basic protein, a known D-Asp-containing protein, in the brain tissues of mice; this indicates that our system is effective for screening D-Asp-containing proteins.
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http://dx.doi.org/10.1007/s00726-008-0040-y | DOI Listing |
Biochim Biophys Acta Proteins Proteom
June 2020
Institute for Integrated Radiation and Nuclear Science, Kyoto University, Osaka, Japan. Electronic address:
Isomerization of aspartate (Asp) is a common non-enzymatic posttranslational modification. Isomerized residues accumulate in proteins associated with age-related human disorders such as cataract and are well known to affect protein structure and function. We previously detected d-Asp-containing peptides in human serum.
View Article and Find Full Text PDFJ Bacteriol
August 2018
Department of Microbiology, University of Georgia, Athens, Georgia, USA
Mounting evidence suggests that d-amino acids play previously underappreciated roles in diverse organisms. In bacteria, even d-amino acids that are absent from canonical peptidoglycan (PG) may act as growth substrates, as signals, or in other functions. Given these proposed roles and the ubiquity of d-amino acids, the paucity of known d-amino-acid-responsive transcriptional control mechanisms in bacteria suggests that such regulation awaits discovery.
View Article and Find Full Text PDFPLoS One
January 2018
Research Reactor Institute, Kyoto University, Osaka, Japan.
Biologically uncommon d-aspartate (d-Asp) residues have been shown to accumulate in proteins associated with age-related human disorders, such as cataract and Alzheimer disease. Such d-Asp-containing proteins are unlikely to be broken down completely because metabolic enzymes recognize only proteins or peptides composed exclusively of l-amino acids. Therefore, undigested d-Asp-containing peptides may exist in blood and, if detectable, may be a useful biomarker for associated diseases.
View Article and Find Full Text PDFJ Cell Physiol
February 2016
Dipartimento di Scienze e Tecnologie Ambientali, Biologiche e Farmaceutiche, Seconda Università di Napoli, Caserta, Italy.
D-aspartate (D-Asp) is an endogenous amino acid present in vertebrate tissues, with particularly high levels in the testis. In vivo studies indicate that D-Asp indirectly stimulates spermatogenesis through the hypothalamic-pituitary-gonadal axis. Moreover, in vitro studies have demonstrated that D-Asp up-regulates testosterone production in Leydig cells by enhancing expression of the steroidogenic acute regulatory protein.
View Article and Find Full Text PDFJ Biol Chem
July 2013
INRA, UMR1319 Micalis, 78352 Jouy-en-Josas, France.
Peptidoglycan hydrolases (PGHs) are responsible for bacterial cell lysis. Most PGHs have a modular structure comprising a catalytic domain and a cell wall-binding domain (CWBD). PGHs of bacteriophage origin, called endolysins, are involved in bacterial lysis at the end of the infection cycle.
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