Homology modeling, binding site identification and docking study of human angiotensin II type I (Ang II-AT1) receptor

2015 ◽  
Vol 74 ◽  
pp. 42-48 ◽  
Author(s):  
Vivek K. Vyas ◽  
Manjunath Ghate ◽  
Kinjal Patel ◽  
Gulamnizami Qureshi ◽  
Surmil Shah
Keyword(s):  
Angiotensin Ii ◽  
Homology Modeling ◽  
Binding Site ◽  
Docking Study ◽  
At1 Receptor ◽  
Type I ◽  
Ang Ii ◽  
Binding Site Identification ◽  
Site Identification

Cellulase enzyme: Homology modeling, binding site identification and molecular docking

2017 ◽  
Vol 1150 ◽  
pp. 61-67 ◽  
Author(s):  
K. Selvam ◽  
D. Senbagam ◽  
T. Selvankumar ◽  
C. Sudhakar ◽  
S. Kamala-Kannan ◽  
...  
Keyword(s):  
Molecular Docking ◽  
Homology Modeling ◽  
Binding Site ◽  
Cellulase Enzyme ◽  
Binding Site Identification ◽  
Site Identification

scholarly journals Postnatal hypoxemia increases angiotensin II sensitivity and up-regulates AT1a angiotensin receptors in rat carotid body chemoreceptors

2002 ◽  
Vol 173 (2) ◽  
pp. 305-313 ◽  
Author(s):  
Fung M-L ◽  
SY Lam ◽  
X Dong ◽  
Y Chen ◽  
PS Leung
Keyword(s):  
Angiotensin Ii ◽  
Carotid Body ◽  
At1 Receptor ◽  
Type I ◽  
Ang Ii ◽  
Type I Cells ◽  
Increased Sensitivity ◽  
Carotid Body Chemoreceptors ◽  
I Cells ◽  
Hypoxic Group

In the present study, the effects of postnatal hypoxemia on the AT1 angiotensin receptor-mediated activities in the rat carotid body were studied. Angiotensin II (Ang II) concentration-dependently increased the chemoreceptor afferent activity in the isolated carotid body. Single- or pauci-fiber recording of the sinus nerve revealed that the afferent response to Ang II was enhanced in the postnatally hypoxic carotid body. To determine whether the increased sensitivity to Ang II is mediated by changes in the functional expression of Ang II receptors in the carotid body chemoreceptors, cytosolic calcium ([Ca2+]i) was measured by spectrofluorimetry in fura-2 acetoxymethyl ester-loaded type I cells dissociated from carotid bodies. Ang II (25-100 nM) concentration-dependently increased [Ca2+]i in the type I cells. The proportion of clusters of type I cells responsive to Ang II was higher in the postnatally hypoxic group than in the normoxic control (89 vs 66%). In addition, the peak [Ca2+]i response to Ang II was enhanced 2- to 3-fold in the postnatally hypoxic group. The [Ca2+]i response to Ang II was abolished by pretreatment with losartan (1 microM), an AT1 receptor antagonist, but not by PD-123177 (1 microM), an AT(2) antagonist. Double-labeling immunohistochemistry confirmed that an enhanced immunoreactivity for AT1 receptor was co-localized to the lobules of type I cells in the hypoxic group. In addition, RT-PCR analysis of subtypes of AT1 receptors showed an up-regulation of AT1a but a down-regulation of AT1b receptors, indicating a differential regulation of the expression of AT1 receptor subtypes by postnatal hypoxia in the carotid body. These data suggest that postnatal hypoxemia is associated with an increased sensitivity of peripheral chemoreceptors in response to Ang II and an up-regulation of AT1a receptor-mediated [Ca2+]i activity of the chemoreceptors. This modulation may be important for adaptation of carotid body functions in the hypoxic ventilatory response and in electrolyte and water homeostasis during perinatal and postnatal hypoxia.

scholarly journals In Silico Molecular Characterization of Cysteine Protease YopT from Yersinia pestis by Homology Modeling and Binding Site Identification

2014 ◽  
Vol 8 (1) ◽  
Author(s):  
Md. Anayet Hasan ◽  
S. M. Alauddin ◽  
Mohammad Al Amin ◽  
Suza Mohammad Nur ◽  
Adnan Mannan
Keyword(s):  
Homology Modeling ◽  
Binding Site ◽  
Yersinia Pestis ◽  
Molecular Characterization ◽  
Cysteine Protease ◽  
In Silico ◽  
Binding Site Identification ◽  
Site Identification

Abstract non disponibile

scholarly journals In SilicoMolecular Characterization of Cysteine Protease YopT fromYersinia pestisby Homology Modeling and Binding Site Identification

2014 ◽  
Vol 8 ◽  
pp. DTI.S13529 ◽  
Author(s):  
Md. Anayet Hasan ◽  
S. M. Alauddin ◽  
Mohammad Ai Amin ◽  
Suza Mohammad Nur ◽  
Adnan Mannan
Keyword(s):  
Homology Modeling ◽  
Binding Site ◽  
Cysteine Protease ◽  
Binding Site Identification ◽  
Site Identification

scholarly journals Salvianolic Acid B Attenuates Rat Hepatic Fibrosis via Downregulating Angiotensin II Signaling

2012 ◽  
Vol 2012 ◽  
pp. 1-10 ◽  
Author(s):  
Shu Li ◽  
Lina Wang ◽  
Xiuchuan Yan ◽  
Qinglan Wang ◽  
Yanyan Tao ◽  
...  
Keyword(s):  
Angiotensin Ii ◽  
Hepatic Fibrosis ◽  
Water Soluble ◽  
Salvianolic Acid B ◽  
Type I ◽  
Ang Ii ◽  
Radix Salviae Miltiorrhizae ◽  
Fibrotic Liver ◽  
Salvianolic Acid

The renin-angiotensin system (RAS) plays an important role in hepatic fibrosis. Salvianolic acid B (Sal B), one of the water-soluble components from Radix Salviae miltiorrhizae, has been used to treat hepatic fibrosis, but it is still not clear whether the effect of Sal B is related to angiotensin II (Ang II) signaling pathway. In the present study, we studied Sal B effect on rat liver fibrosis and Ang-II related signaling mediators in dimethylnitrosamine-(DMN-) induced rat fibrotic modelin vivoand Ang-II stimulated hepatic stellate cells (HSCs)in vitro, with perindopril or losartan as control drug, respectively. The results showed that Sal B and perindopril inhibited rat hepatic fibrosis and reduced expression of Ang II receptor type 1 (AT1R) and ERK activation in fibrotic liver. Sal B and losartan also inhibited Ang II-stimulated HSC activation including cell proliferation and expression of type I collagen I (Col-I) andα-smooth muscle actin (α-SMA) productionin vitro, reduced the gene expression of transforming growth factor beta (TGF-β), and downregulated AT1R expression and ERK and c-Jun phosphorylation. In conclusion, our results indicate that Sal B may exert an antihepatic fibrosis effect via downregulating Ang II signaling in HSC activation.

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