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Proteome analysis of glandular parotid and submandibular‐sublingual saliva in comparison to whole human saliva by two‐dimensional gel electrophoresis
Author(s) -
Walz Anke,
Stühler Kai,
Wattenberg Andreas,
Hawranke Eva,
Meyer Helmut E.,
Schmalz Gottfried,
Blüggel Martin,
Ruhl Stefan
Publication year - 2006
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.200500125
Subject(s) - mucin , saliva , proteome , submandibular gland , glycoprotein , secretion , parotid gland , chemistry , biology , microbiology and biotechnology , biochemistry , medicine , pathology , endocrinology
The secretions of the salivary parotid and submandibular‐sublingual (SMSL) glands constitute the main part of whole human saliva (WS) in which proline‐rich proteins (PRPs) and mucins represent dominant groups. Although proteome analysis had been performed on WS, no identification of PRPs or mucins by 2‐DE and MS was achieved in WS and no comprehensive analysis of both glandular secretions is available so far. The aim of this study was to compare the protein map of WS to parotid and SMSL secretions for the display of PRPs and mucins. WS and glandular secretions were subjected to 2‐DE and spots were analyzed by MALDI‐MS. New components identified in WS were cyclophilin‐B and prolyl‐4‐hydroxylase. Also acidic and basic PRPs as well as the proline‐rich glycoprotein (PRG) could now be mapped in WS. Acidic PRPs were found equally in parotid and SMSL secretions, whereas basic PRPs and PRG were found primarily in parotid secretion. Salivary mucin MUC7 was identified in SMSL secretion. Thus, the more abundant proteins of WS can be explained mainly by mixed contributions of parotid and SMSL secretions with only few components remaining that may be derived from local sources in the oral cavity.