TY - JOUR
T1 - Trafficking and post-secretory events responsible for the formation of secreted human salivary peptides. A proteomic approach
AU - Messana, Irene
AU - Cabras, Tiziana
AU - Pisano, Elisabetta
AU - Sanna, Maria Teresa
AU - Olianas, Alessandra
AU - Manconi, Barbara
AU - Pellegrini, Magi
AU - Paludetti, Gaetano
AU - Scarano, Emanuele
AU - Fiorita, Antonella
AU - Agostino, Stefania
AU - Contucci, Alessia Maria
AU - Calo', Lea
AU - Picciotti, Pasqualina Maria
AU - Manni, Armando
AU - Vitali, Alberto
AU - Fanali, Chiara
AU - Inzitari, Rosanna
AU - Castagnola, Massimo
PY - 2008
Y1 - 2008
N2 - 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/SI), and whole saliva was performed. The main results of this study indicate the following. (1) 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/SI 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/SI glands. (iv) O-Sulfation of tyrosines of Histatin 1 is a posttranslational 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/SI glands.
AB - 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/SI), and whole saliva was performed. The main results of this study indicate the following. (1) 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/SI 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/SI glands. (iv) O-Sulfation of tyrosines of Histatin 1 is a posttranslational 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/SI glands.
KW - PEPTIDES
KW - PROTEOMIC
KW - SALIVARY
KW - PEPTIDES
KW - PROTEOMIC
KW - SALIVARY
UR - http://hdl.handle.net/10807/26019
U2 - 10.1074/mcp.M700501-MCP200
DO - 10.1074/mcp.M700501-MCP200
M3 - Article
SN - 1535-9476
SP - 911
EP - 926
JO - MOLECULAR & CELLULAR PROTEOMICS
JF - MOLECULAR & CELLULAR PROTEOMICS
ER -