Sterebins E, F, G and H, diterpenoids of Stevia rebaudiana leaves

Oshima, Yoshiteru; Saito, Jun; Hikino, H.

doi:10.1016/0031-9422(88)83157-1

Cited by 31 publications

(28 citation statements)

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“…In contrast to the very acidic C-terminal region of carboxypeptidase E, this portion of carboxypeptidase N is extremely basic. On keeping freshly prepared material at + 4 T , increasing amounts of subunits can be observed in disk gel electrophoresis under non-dissociating conditions [3]. C-terminal proteolytic processing of the small subunits, as discussed below, may be accompanied by complex dissociation and therefore support the view that the C-terminus of the small subunit is involved in complex formation.…”

Section: Discussionmentioning

confidence: 71%

cDNA cloning and complete primary structure of the small, active subunit of human carboxypeptidase N (kininase 1)

Gebhard¹,

M²,

Eulitz

1989

European Journal of Biochemistry

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The human plasma metallo-protease carboxypeptidase N of M , 280000 consists of two small, enzymatically active subunits of M , 50000 and two large subunits. Only the large subunits are glycosylated. They may have a function in stabilizing the complex in plasma. The N-terminal sequence of the small subunit was determined from the isolated protein and used to specify a unique 59-mer oligonucleotide probe. A cDNA clone of 1.7 kbp containing the entire coding sequence of the small subunit of carboxypeptidase N was isolated from a humanliver cDNA library. The cDNA clone encodes a signal sequence of 20 amino acids and the 438 amino acids of the mature subunit. There is a remarkable primary structure similarity of 49% to bovine carboxypeptidase E (enkephalin convertase). A more distant relationship to the bovine pancreatic, digestive carboxypeptidases A and B or even to the metallo-endopeptidases is based mainly on the occurrence of conserved, mechanistically important residues.Carboxypeptidase N (arginine carboxypeptidase) cleaves basic amino acid residues from the C-terminal of peptides and proteins. In the circulation, the enzyme plays a central role in regulating the biological activity of peptides such as kinins and anaphylatoxins, and therefore it is also known as kininase 1 and anaphylatoxin inactivator [l, 23.The liver was proposed as the site of origin of the plasma enzyme which is a tetrameric complex of M , 280 000 -320 000. It can be dissociated into two large, identical subunits of M , 83000-98000 and two small, identical subunits of M , 42000 -55000. Enzymatic activity resides only in the small, unglycosylated subunits. The large, glycosylated subunits are supposed to prevent proteolytic degradation of the enzymatically active, small subunits and/or their rapid removal from blood by glomerular filtration [3 -51.The reported M , values of the small subunit of carboxypeptidase N and other mammalian metallo-carboxypeptidases vary clearly in size. This is true for the pancreatic carboxypeptidases A and B ( M , 34400 and 34600, respectively, as calculated from primary structure), human urinary carboxypeptidase (M, 75 700 [6], a membrane-bound carboxypeptidase in human placenta ( M , 67000) [7] and carboxypeptidase E ( M , 50000) from bovine adrenal-medulla chromaffin granules, brain and pituitary [8,9], secretory granules of rat pituitary [lo] and rat insulinoma (M, 54000) [ll]. Because of their common properties as metallo-carboxypeptiCorrespondence to W. Gebhard,

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Section: Discussionmentioning

confidence: 71%

cDNA cloning and complete primary structure of the small, active subunit of human carboxypeptidase N (kininase 1)

Gebhard¹,

M²,

Eulitz

1989

European Journal of Biochemistry

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“…The mouse endoA gene is a useful model for studies on developmental regulation [1,2], and particularly the features of chromatin structure that differ in active and inactive genes [3].…”

Section: Introductionmentioning

confidence: 99%

Activation of the mouse cytokeratin A (endo A) gene in teratocarcinoma F9 cells by the histone deacetylase inhibitor Trichostatin A

Miyashita¹,

Yamamoto²,

Nishimune³

et al. 1994

FEBS Letters

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Absa'aet Treatment of cultured ceils with sodium butyrate, that is the histone deacetylase inhibitor, induces the historic hyperacetylation and the expressions of various mammalian genes without affecting the level of protein synthesis. However, butyrate is a non-specific inhibitor of deacetylase because of its effects on various other enzymes and nuclear proteins other than histones. On the other hand, Trichostatin A (TSA) was recently found to be a potent and specific inhibitor of histone deacetylase. We examined the effect of TSA on the expression of mouse cytokeratin A (endoA). TSA increased endoA expression in F9 ceils, and was efffective at a much lower concentration than sodium butyrate. We also examined the changes of chromatin structure induced by the two drugs by a DNase 1-hypersensitivity assay. Both drugs induced the formation of a DNase 1-hypersensitive site (DH site) in only the promoter region. The precise mechanism(s) by which the two drugs increase endoA gene expression is unknown, but these results suggest that endoA expression is induced by inhibition of histone deacetylase and that the effect is at the transcriptional level.

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“…Jhanol, austroinulin, 6-O-acetylaustroinulin and 7-O-acetylaustroinulin as well as steviosde and rebaudioside A have been obtained from stevia flowers (Darise et al 1983). Eight additional diterpenes, called sterebins A-H, have been isolated from leaves and identified (Oshima et al 1986(Oshima et al , 1988.…”

Section: Other Constituentsmentioning

confidence: 99%

Stevia rebaudiana: Its agricultural, biological, and chemical properties

Brandle

Starratt²,

Gijzen³

1998

Can. J. Plant Sci.

290

209

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Brandle, J. E., Starratt, A. N. and Gijzen, M. 1998. Stevia rebaudiana: Its agricultural, biological, and chemical properties. Can. J. Plant Sci. 78: 527-536. Stevia rebaudiana is a member of the Compositae, native to Paraguay. It produces a number of high-potency low-calorie sweeteners in its leaf tissue. The sweeteners are diterpene glycosides and range between 30 and 320 times sweeter than sugar. Increasing consumer interest in natural food ingredients means that products like stevia sweeteners will be subject to increasing demand. Such demand will need to be supported by a modern mechanised production system. The purpose of this review is to summarize the existing agricultural, chemical and biochemical literature to provide a baseline for new research.Key words: Stevia, diterpene, steviol glycoside, sweeteners Brandle, J. E., Starratt, A. N. et Gijzen, M. 1998. Stevia rebaudiana : qualités agricoles, biologiques et chimiques. Can. J. Plant Sci. 78: 527-536. Stevia rebaudiana, plante originaire du Paraguay, appartient à la famille des Composées. Il produit dans les tissus foliaires un certain nombre d'agents édulcorants puissants mais hypocaloriques. Ces produits, des glycosides diterpéniques sont de 30 à 320 fois plus sucrés que le sucre. Compte tenu de l'intérêt croissant du consommateur pour les ingrédients alimentaires naturels, la demande de produits comme les édulcorants du stevia ne pourra qu'aller en croissant, mais il faudra que cette demande soit étayée par un système moderne de production mécanisée. Voulue comme une base pour les recherches futures, cette mise au point vise à compulser la bibliographie actuelle de cette espèce sur les plans tant agricoles que chimiques et biochimiques.

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Sterebins E, F, G and H, diterpenoids of Stevia rebaudiana leaves

Cited by 31 publications

References 1 publication

cDNA cloning and complete primary structure of the small, active subunit of human carboxypeptidase N (kininase 1)

cDNA cloning and complete primary structure of the small, active subunit of human carboxypeptidase N (kininase 1)

Activation of the mouse cytokeratin A (endo A) gene in teratocarcinoma F9 cells by the histone deacetylase inhibitor Trichostatin A

Stevia rebaudiana: Its agricultural, biological, and chemical properties

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