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Most of the identified peptides\/proteins are originated from cellular debris or plasma components while only 26% (<jats:italic>n<\/jats:italic> = 607) correspond to salivary peptides\/proteins species. In spite of the presence of the major salivary peptides in all samples from the six subjects analyzed, each individual presents a different pattern of fragments, many deriving from the same protein sequence. All our data, in particular the large number of fragments found, suggest high proteolytic activity insight the oral cavity. The analysis of samples by gelatin zymography showed that all saliva donors displayed multiple proteolytic bands, two identified as cathepsin D and G by MS. Analysis of the cleavage site distribution on the main peptide sequences based on contingency tables shows that the predominant cleavages occur between Gln\u2010Gly or Tyr\u2010Gly. These cleavages are largely associated with proline\u2010rich proteins peptides and with histatin 1 and P\u2010B peptide, respectively. However, depending on the peptide class, different cleavage hits were observed suggesting the presence of a set of proteases acting in different ways according to different peptide sequences. Comparing the number of cleavages involving all residues, it is possible to observe that 44% (\u00b110%) of the observed cleavages in histatin, statherin and P\u2010B peptide in all individuals may be explained by cathepsin D, suggesting a major role for this enzyme in oral cavity proteolysis.<\/jats:p>","DOI":"10.1002\/prca.200800183","type":"journal-article","created":{"date-parts":[[2009,4,6]],"date-time":"2009-04-06T11:37:49Z","timestamp":1239017869000},"page":"528-540","update-policy":"http:\/\/dx.doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":42,"title":["Towards defining the whole salivary peptidome"],"prefix":"10.1002","volume":"3","author":[{"given":"Rui","family":"Vitorino","sequence":"first","affiliation":[]},{"given":"Ant\u00f3nio","family":"Barros","sequence":"additional","affiliation":[]},{"given":"Armando","family":"Caseiro","sequence":"additional","affiliation":[]},{"given":"Pedro","family":"Domingues","sequence":"additional","affiliation":[]},{"given":"Jos\u00e9","family":"Duarte","sequence":"additional","affiliation":[]},{"given":"Francisco","family":"Amado","sequence":"additional","affiliation":[]}],"member":"311","published-online":{"date-parts":[[2009,4,22]]},"reference":[{"key":"e_1_2_1_2_2","doi-asserted-by":"publisher","DOI":"10.1586\/14789450.2.4.521"},{"key":"e_1_2_1_3_2","doi-asserted-by":"publisher","DOI":"10.1177\/154405910708600802"},{"key":"e_1_2_1_4_2","doi-asserted-by":"publisher","DOI":"10.1177\/08959374000140010301"},{"key":"e_1_2_1_5_2","doi-asserted-by":"publisher","DOI":"10.1002\/bmc.438"},{"key":"e_1_2_1_6_2","doi-asserted-by":"publisher","DOI":"10.1042\/bst0210133"},{"key":"e_1_2_1_7_2","doi-asserted-by":"publisher","DOI":"10.1034\/j.1601-0825.2002.1o816.x"},{"key":"e_1_2_1_8_2","doi-asserted-by":"publisher","DOI":"10.1021\/pr0700706"},{"key":"e_1_2_1_9_2","doi-asserted-by":"publisher","DOI":"10.1002\/jssc.200600244"},{"key":"e_1_2_1_10_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0378-4347(00)00466-7"},{"key":"e_1_2_1_11_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M404322200"},{"key":"e_1_2_1_12_2","doi-asserted-by":"publisher","DOI":"10.1021\/bi048176r"},{"key":"e_1_2_1_13_2","doi-asserted-by":"publisher","DOI":"10.1016\/0003-9969(74)90130-7"},{"key":"e_1_2_1_14_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M008229200"},{"key":"e_1_2_1_15_2","first-page":"1071","article-title":"The amino acid sequence of a salivary proline\u2010rich peptide, P\u2010C, and its relation to a salivary proline\u2010rich phosphoprotein, protein C","volume":"87","author":"Isemura S.","year":"1980","journal-title":"J. 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