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To elucidate the localization of post-translational modifications of different classes of human salivary proteins and peptides [acidic and basic proline-rich proteins [PRPs], Histatins, Statherin, P-B peptide, and “S type” Cystatins] a comparative reversed phase HPLC-ESI-MS analysis on intact proteins of enriched granule preparations from parotid and submandibular glands as well as parotid, submandibular/sublingual [Sm/Sl], and whole saliva was performed. The main results of this study indicate the following. [i] Phosphorylation of all salivary peptides, sulfation of Histatin 1, proteolytic cleavages of acidic and precursor basic PRPs occur before granule storage. [ii] In agreement with previous studies, basic PRPs are secreted by the parotid gland only, whereas all isoforms of acidic PRPs [aPRPs] are secreted by both parotid and Sm/Sl glands. [iii] Phosphorylation levels of aPRPs, Histatin 1, and Statherin are higher in the parotid gland, whereas the extent of cleavage of aPRP is higher in Sm/Sl glands. [iv] O-Sulfation of tyrosines of Histatin 1 is a post-translational modification specific for the submandibular gland. [v] The concentration of Histatin 3, Histatin 5, and Histatin 6, but not Histatin 1, is higher in parotid saliva. [vi] Histatin 3 is submitted to the first proteolytic cleavage [generating Histatins 6 and 5] during granule maturation, and it occurs to the same relative extent in both glands. [vii] The proteolytic cleavages of Histatin 5 and 6, generating a cascade of Histatin 3 fragments, take place after granule secretion and are more extensive in parotid secretion. [viii] Basic PRPs are cleaved in the oral cavity by unknown peptidases, generating various small proline-rich peptides. [ix] C-terminal removal from Statherin is more extensive in parotid saliva. [x] P-B peptide is secreted by both glands, and its relative quantity is higher in submandibular/sublingual secretion. [xi] In agreement with previous studies, S type Cystatins are mainly the product of Sm/Sl glands.
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Published, MCP Papers in Press, January 9, 2008, DOI 10.1074/mcp.M700501-MCP200
This work was supported by Università di Cagliari, Università Cattolica in Rome, Telethon Grant GGP06170, International Scientific Institute “Paolo VI” [ISI], Ministero dell'Università e della Ricerca, Italian National Research Council [CNR], Regione Sardegna, and Fondazione Banco di Sardegna. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked “advertisement” in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.
These authors contributed equally to this work.
© 2008 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology.