Substrate Specificity of the Nateglinide/H+Cotransport System for Phenolic Acids

2005 ◽  
Vol 53 (15) ◽  
pp. 6100-6104 ◽  
Author(s):  
Yoshitaka Saito ◽  
Shirou Itagaki ◽  
Yukio Otsuka ◽  
Yoko Kobayashi ◽  
Hideo Okumura ◽  
...  
Keyword(s):  
Substrate Specificity ◽  
Phenolic Acids ◽  
Cotransport System

Substrate specificity and inducibility of TACE (tumour necrosis factor α-converting enzyme) revisited: the Ala-Val preference, and induced intrinsic activity

2003 ◽  
Vol 70 ◽  
pp. 39-52 ◽  
Author(s):  
Roy A. Black ◽  
John R. Doedens ◽  
Rajeev Mahimkar ◽  
Richard Johnson ◽  
Lin Guo ◽  
...  
Keyword(s):  
Substrate Specificity ◽  
Recent Work ◽  
Tumour Necrosis Factor ◽  
Tumour Necrosis ◽  
Transforming Growth Factor ◽  
Intrinsic Activity ◽  
Converting Enzyme ◽  
Tumour Necrosis Factor Α ◽  
Factor Α ◽  
Necrosis Factor

Tumour necrosis factor α (TNFα)-converting enzyme (TACE/ADAM-17, where ADAM stands for a disintegrin and metalloproteinase) releases from the cell surface the extracellular domains of TNF and several other proteins. Previous studies have found that, while purified TACE preferentially cleaves peptides representing the processing sites in TNF and transforming growth factor α, the cellular enzyme nonetheless also sheds proteins with divergent cleavage sites very efficiently. More recent work, identifying the cleavage site in the p75 TNF receptor, quantifying the susceptibility of additional peptides to cleavage by TACE and identifying additional protein substrates, underlines the complexity of TACE-substrate interactions. In addition to substrate specificity, the mechanism underlying the increased rate of shedding caused by agents that activate cells remains poorly understood. Recent work in this area, utilizing a peptide substrate as a probe for cellular TACE activity, indicates that the intrinsic activity of the enzyme is somehow increased.

Screening of sage and thyme plant extracts for some phenolic acids and rutin

Planta Medica ◽  
2010 ◽  
Vol 76 (12) ◽  
Author(s):  
S Huseinovic ◽  
M Salihovic ◽  
A Topcagic ◽  
K Kalcher ◽  
S Cavar ◽  
...  
Keyword(s):  
Phenolic Acids ◽  
Plant Extracts

Content of some phenolic acids and rutin in the leaves and roots of Symphytum officinale L.

Planta Medica ◽  
2010 ◽  
Vol 76 (12) ◽  
Author(s):  
I Tahirovic ◽  
Z Rimpapa ◽  
S Cavar ◽  
S Huseinovic ◽  
S Muradic ◽  
...  
Keyword(s):  
Phenolic Acids ◽  
Symphytum Officinale ◽  
Leaves And Roots

Phenolic acids and C-glycoside flavonoids in Merostachys riedeliana (bamboo)

Planta Medica ◽  
2014 ◽  
Vol 80 (16) ◽  
Author(s):  
L Torres ◽  
C José ◽  
R Shirasuna ◽  
MT Grombone-Guaratini
Keyword(s):  
Phenolic Acids

Substrate Specificity of Leukocyte and Platelet Elastases

1978 ◽  
Vol 39 (03) ◽  
pp. 785-786 ◽  
Author(s):  
Y Legrand ◽  
J Caen ◽  
L Robert
Keyword(s):  
Substrate Specificity

Inhibition by Phenol and Phenolic Acids of Platelet Release Reaction

1973 ◽  
Vol 30 (02) ◽  
pp. 334-338 ◽  
Author(s):  
Felisa C. Molinas
Keyword(s):  
Renal Failure ◽  
Phenolic Compounds ◽  
Phenolic Acids ◽  
Platelet Function ◽  
Deleterious Effect ◽  
Release Reaction ◽  
Contributory Factors ◽  
Adp Release ◽  
Platelet Release

SummaryIt has been postulated that the high phenol and phenolic acids plasmatic levels found in patients with chronic renal failure are contributory factors in the abnormal platelet function described in these patients. This hypothesis was corroborated by “in vitro” studies showing the deleterious effect of these compounds on certain platelet function after pre-incubation of PRP with phenol and phenolic compounds. The present studies were conducted to determine the influence of phenolic compounds on platelet release reaction. It was found that phenol inhibited from 62.5 to 100% the effect of the aggregating agents thrombin, adrenaline and ADP on platelet 5-HT-14C release. The phenolic acids p-, m-, and o-HPAA inhibited from 36.35 to 94.8% adrenaline and ADP-induced platelet 5-HT-14C release. Adrenaline-induced platelet ADP release was inhibited from 27.45 to 38.10% by the phenolic compounds. These findings confirm the hypothesis that phenolic compounds interfere with platelet function through the inhibition of the release reaction.

PRKACA mutations in adrenal Cushing can alter substrate specificity

2017 ◽  
Author(s):  
Kerstin Bathon ◽  
Isabel Weigand ◽  
Jens T Vanselow ◽  
Cristina L Ronchi ◽  
Dalmazi Guido Di ◽  
...  
Keyword(s):  
Substrate Specificity
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