ABSTRACT
Free D-aspartic acid (D-Asp) has been reported to occur in a wide variety of tissues and cells, exclusively in central nervous system and endocrine tissues. In this manuscript, we demonstrate that large amounts of D-Asp are present in the exocrine tissue, salivary glands. In adult male rats, D-Asp concentrations in parotid and submandibular gland were 212+/-68 and 233+/-34 nmol/g wet weight, respectively, and were low (38+/-20 nmol/g wet weight) in sublingual gland. This result indicates that substantial level of D-Asp exists not only in central nervous system and endocrine tissues but also in exocrine tissues. Furthermore, D-Asp concentration in parotid gland increased transiently at 3 weeks of age and decreased thereafter. In contrast, the D-Asp level in submandibular gland continued to increase gradually from 1 to 7 weeks of age and remained at an adult level after 7 weeks of age. Using anti-D-Asp antibody, immunohistochemical study was done against these glands and it showed that the predominant localization of D-Asp in acinar cells in parotid gland, while D-Asp is specifically located in striated duct cells in submandibular gland. These results suggest that D-Asp may play different roles between the two glands.
Subject(s)
Aging/metabolism , D-Aspartic Acid/metabolism , Parotid Gland/metabolism , Submandibular Gland/metabolism , Animals , Female , Male , Organ Specificity , Rats , Rats, Wistar , Salivary Glands/metabolism , Tissue DistributionABSTRACT
In tooth dentine, owing to its slow metabolism after its formation, racemized and transformed D-aspartic acid remains in the tissue and accumulates with age. However, no dentinal proteins which contain D-aspartic acid have been identified. In this study, a non-collagenous phosphoprotein was purified from bovine dentine. Its molecular mass was about 130 kDa and its amino acid composition was very similar to that of bovine dentine phosphophoryn. The purified protein contained a large proportion of aspartic acid residues and some of them were stereoinverted from the L-isomer to the D-isomer. The D-/L-aspartic acid ratio of dentine non-collagenous phosphoproteins purified from 8-month-old fetal, postnatal and 1-year-old bovine first incisors showed that the stereoinversion tended to increase with age. These results suggest that the purified non-collagenous phosphoprotein is a candidate for the protein in dentine containing D-aspartic acid.
