Sweet-Sensitive Protein from Bovine Taste Buds: Isolation and Assay

Dastoli, Frank R.; Price, Samantha A.

doi:10.1126/science.154.3751.905

Cited by 109 publications

(39 citation statements)

References 6 publications

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“…Biological assay of the lingual epithelium (DASTOLI and PRICE, 1966) suggested the occurrence of a sweet-sensitive protein, which reacts specifically to sugars.…”

Section: Discussionmentioning

confidence: 99%

Taste Buds in the Vallate Papillae of the Rat Studied with Freeze-Fracture Preparation

Akisaka

Oda

1978

Arch. Histol. Jap., Arch. Histol. Jpn

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“…Biological assay of the lingual epithelium (DASTOLI and PRICE, 1966) suggested the occurrence of a sweet-sensitive protein, which reacts specifically to sugars.…”

Section: Discussionmentioning

confidence: 99%

Taste Buds in the Vallate Papillae of the Rat Studied with Freeze-Fracture Preparation

Akisaka

Oda

1978

Arch. Histol. Jap., Arch. Histol. Jpn

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“…The accumulated evidence during the past decade therefore fails to support the original claim (38,39) that a "sweet-sensitive protein," which is the receptor molecule for sweet compounds, was in fact isolated. The weak binding interactions of sugars with receptors underlies the earlier lack of a reliable assay method, which has hindered more definitive approaches.…”

Section: Methodsmentioning

confidence: 75%

“…Considerable interest is being maintained in structure-taste activity correlations among sweet-tasting compounds (1-4, 6, 27-37). (38) and received wide and often uncritical acceptance. Dastoli and Price reported the isolation (38) and characterization (39), from bovine tongues, of a "sweet-sensitive protein."…”

Section: Methodsmentioning

confidence: 99%

“…(38) and received wide and often uncritical acceptance. Dastoli and Price reported the isolation (38) and characterization (39), from bovine tongues, of a "sweet-sensitive protein." Interactions with sweet compounds were measured by using changes in refractive index upon mixing a sweet compound with the protein fraction; they also reported that difference spectral changes in the ultraviolet region could equally well be used.…”

Section: Methodsmentioning

confidence: 99%

See 1 more Smart Citation

Biochemical studies of taste sensation: binding to taste tissue of 3H-labeled monellin, a sweet-tasting protein.

Çağan¹,

Morris²

1979

Proc. Natl. Acad. Sci. U.S.A.

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Binding of 3H-labeled methylated monellin to taste receptor tissue was demonstrated in vitro. Preparations of bovine and human circumvallate (taste) papillae bound more of the ligand than did lingual and nonlingual epithelial preparations devoid of taste buds. Binding to the taste preparations saturated at high ligand concentrations. Furthermore, sugars and other sweet-tasting molecules appeared to compete to some extent with this sweet-tasting protein for its binding sites. These binding measurements of the intensely sweet-tasting protein monellin to taste receptor preparations help to establish the binding interaction as an initial step in taste sensation.Relatively little is understood about the biochemical basis of sweet taste despite considerable knowledge of a wide variety of sweet-tasting chemical compounds (1)(2)(3)(4)(5)(6). Most of the behavioral, physiological, and biochemical research on sweet taste has used sucrose or other sugars. The inherently weak binding (6-8) of sugars to taste receptors, with values of KD in the range of 10-1 to 10-3 M (9, 10), presents a substantial difficulty in directly studying the biochemical basis of how a sugar binds to and triggers a taste receptor to respond. The interest in our laboratory (11)(12)(13)(14)(15)(16) formaldehyde was diluted with unlabeled formaldehyde to yield 2.7 M and a specific radioactivity of 9.5 Ci/ mol). This was followed by reduction with 100 ,ul of 1.2 M NaBH4 (in water) for 5 min and then with 400,l for another 5 min. The preparation was washed at room temperature with 10 mM sodium phosphate buffer ( To prepare the tissue fraction, we thawed the frozen tongues or human tissue samples and dissected the circumvallate papillae free, with the top surface (0.2-0.5 mm) having been removed with a scalpel. Small (5 X 5 mm) blocks of tongue epithelium provided control tissue devoid of taste buds (bovine and human), and pectoral skin (human) was also used as a control tissue where indicated. The epidermal sidewalls of the papillae and the upper layer from the control epithelial blocks were teased off with forceps (18,19) PA 19013. 1692 The publication costs of this article were defrayed in part by page charge payment. This article must therefore be hereby marked "advertisement" in accordance with 18 U. S. C. §1734 solely to indicate this fact.

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“…Third, treatment of the two types of cells with some proteolytic enzymes attenuates their responses to glucose without affecting responses to other stimuli (HIJI,1975;KRAUSE et al, 1973). Fourth, proteins which bind to glucose have been reported to be extracted from the membrane fractions of the two cell types, although the exact nature of the proteins has not been determined (DASTOLI and PRICE, 1966;PRICE, 1973). Fifth, in non-insulin-dependent diabetics (NIDD), the physiological responses to glucose of the two types of cells are believed to decrease, even when they respond normally to other stimuli.…”

mentioning

confidence: 99%

Receptors of paraneurons, with special reference to glucoreceptors.

Niki

Hashioka

1989

Archives of Histology and Cytology

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Summary. Among glucose-recognizing paraneurons, the gustatory cell is believed to have a glucoreceptor, while the pancreatic B cell is thought to metabolize glucose for signal production for insulin release. To investigate whether a common mechanism of glucose recognition exists among these cells, we have studied the interaction of the anomers of glucose or its derivative, known as a sugar taste inhibitor, with the pancreatic B cell of normal and diabetic rats. Inhibitors of the sugar taste response inhibited glucose-induced insulin release in various manners. A non-specific inhibitor, dibucaine, impaired not only the insulin response to glucose but also the ability to discriminate the anomers of glucose, without inhibiting glucose oxidation in the islets. Dibucaine also inhibited insulin release induced by a non-glucose secretagogue, tolbutamide. The a anomer, but not the b anomer, of p-nitrophenyl-D-glucopyranoside, a specific-competitive inhibitor of the sugar taste response, inhibited glucose-induced insulin release, but did not inhibit insulin release induced by nonglucose secretagogues or glucose oxidation. The pancreatic B cell of a non-insulin-dependent diabetes (NIDD) rat model, the NSZ rat, exhibited low insulin response to glucose and did not discriminate between the two anomers of glucose. The diabetic B cell responded to non-glucose secretagogues to the same extent as the control. Glucose oxidation in the diabetic islets was not impaired. These findings, together with previous ones, suggest that the gustatory and pancreatic B cells have a common glucose recognition site, which has a steric preference for the a anomer and is impaired in NIDD.

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Sweet-Sensitive Protein from Bovine Taste Buds: Isolation and Assay

Cited by 109 publications

References 6 publications

Taste Buds in the Vallate Papillae of the Rat Studied with Freeze-Fracture Preparation

Taste Buds in the Vallate Papillae of the Rat Studied with Freeze-Fracture Preparation

Biochemical studies of taste sensation: binding to taste tissue of 3H-labeled monellin, a sweet-tasting protein.

Receptors of paraneurons, with special reference to glucoreceptors.

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