Short-Term Modification of Human Salivary Proteome Induced by Two Bitter Tastants, Urea and Quinine

被引：21

作者：

Quintana, Mercedes ^{[1
,2
,3
]}

Palicki, Olivier ^{[1
,2
,3
]}

Lucchi, Geraldine ^{[4
]}

Ducoroy, Patrick ^{[4
]}

Chambon, Christophe ^{[5
]}

Salles, Christian ^{[1
,2
,3
]}

Morzel, Martine ^{[1
,2
,3
]}

机构：

[1] INRA, UMR 1129, FLAVIC, F-21065 Dijon, France

[2] ENESAD, UMR 1129, FLAVIC, F-21000 Dijon, France

[3] Univ Bourgogne, UMR 1129, FLAVIC, F-21000 Dijon, France

[4] CLIPP, IFR 100, Sante STIC, F-21000 Dijon, France

[5] INRA, Plate Forme Explorat Metab Genes Metabolites, F-63122 St Genes Champanelle, France

来源：

CHEMOSENSORY PERCEPTION | 2009年 / 2卷 / 03期

关键词：

Bitterness; Saliva Proteome; Taste; Urea; Quinine; 2-DIMENSIONAL GEL-ELECTROPHORESIS; ANHYDRASE ISOENZYME-VI; MASS-SPECTROMETRY; PAROTID-SALIVA; ORAL-CAVITY; HUMAN WHOLE; TASTE; PROTEINS; AMYLASE; IDENTIFICATION;

D O I：

10.1007/s12078-009-9048-2

中图分类号：

TS2 [食品工业];

学科分类号：

0832 ;

摘要：

Salivary proteome patterns of healthy volunteers (n = 12) were compared before and after they tasted bitter solutions made of either urea (0.36M) or quinine-hydrochloride (40 A mu M). Relative abundance of 22 and 18 spots was modified 15 min after stimulation by urea and quinine, respectively. Only two spots were common to both tastants, indicating a molecule-specific response. Proteins, relative quantity of which was altered, were agents of the oral cavity defense (e.g., thioredoxin, cystatin, parotid secretory proteins, etc.) and markers of inflammation (transthyretin and transferrin) or enzymes. In particular, the relative abundance of carbonic anhydrase VI, a protein previously described as crucial to taste function, declined after tasting the urea solution.

引用

页码：133 / 142

页数：10

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