Bilayer interaction and protein kinase C-C1 domain binding studies of kojic acid esters

RSC Advances ◽  
2014 ◽  
Vol 4 (49) ◽  
pp. 25520-25531 ◽  
Author(s):  
Rituparna Borah ◽  
Dipjyoti Talukdar ◽  
Sukhamoy Gorai ◽  
Dipankar Bain ◽  
Debasis Manna
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Lipid Bilayer ◽  
Acid Ester ◽  
Kojic Acid ◽  
Binding Studies ◽  
Binding Properties ◽  
Kinase C ◽  
C1 Domain ◽  
Acid Esters

Synthesis of kojic acid ester analogues and their lipid bilayer interaction and PKC-C1 domain binding properties have been demonstrated in this present work.

The C1 Domain of Protein Kinase C as a Lipid Bilayer Surface Sensing Module†

Biochemistry ◽  
2001 ◽  
Vol 40 (34) ◽  
pp. 10334-10341 ◽  
Author(s):  
Cojen Ho ◽  
Simon J. Slater ◽  
Brigid Stagliano ◽  
Christopher D. Stubbs
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Lipid Bilayer ◽  
Kinase C ◽  
Surface Sensing ◽  
C1 Domain

Synthesis and protein kinase C (PKC)-C1 domain binding properties of diacyltetrol based anionic lipids

2014 ◽  
Vol 10 (11) ◽  
pp. 3002-3013 ◽  
Author(s):  
Narsimha Mamidi ◽  
Subhankar Panda ◽  
Rituparna Borah ◽  
Debasis Manna
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Binding Specificity ◽  
Binding Properties ◽  
Kinase C ◽  
P Protein ◽  
C1 Domain ◽  
Anionic Lipids

Protein kinase C-C1 domain binding specificity of the anionic hybrid lipids.

Membrane Interaction and Protein Kinase C-C1 Domain Binding Properties of 4-Hydroxy-3-(hydroxymethyl) Phenyl Ester Analogues

2014 ◽  
Vol 118 (27) ◽  
pp. 7541-7553 ◽  
Author(s):  
Dipjyoti Talukdar ◽  
Subhankar Panda ◽  
Rituparna Borah ◽  
Debasis Manna
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Phenyl Ester ◽  
Binding Properties ◽  
Membrane Interaction ◽  
Kinase C ◽  
C1 Domain

Renal angiotensin II receptors and protein kinase C in diabetic rats: effects of insulin and ACE inhibition

2000 ◽  
Vol 278 (4) ◽  
pp. F603-F612 ◽  
Author(s):  
Farhad Amiri ◽  
Raul Garcia
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Ace Inhibition ◽  
Treated Group ◽  
Diabetic Rats ◽  
Competitive Binding ◽  
Ang Ii ◽  
Binding Studies ◽  
Kinase C ◽  
High Insulin

It has been shown that glomerular ANG II receptors are downregulated and protein kinase C (PKC) activity is enhanced in diabetes mellitus. Therefore, we investigated glomerular and preglomerular vascular ANG II receptors and PKC isoform regulation in streptozotocin (STZ)-diabetic rats treated with insulin and/or captopril. Diabetic rats were prepared by injecting STZ (60 mg/kg). Those that developed diabetes after 48 h were treated with low or high doses of insulin, or with a low dose of insulin as well as captopril, and killed 14 days later. Their glomeruli and preglomerular vessels were purified, competitive binding studies were performed by using the ANG II antagonists losartan and PD-123319, and PKC analysis was carried out by Western blotting. Competitive binding studies showed that the AT1 receptor was the only ANG II receptor detected on both glomeruli and preglomerular vessels of all groups. Preglomerular vascular AT1 receptor density (Bmax) was significantly upregulated in low insulin-treated STZ rats, whereas glomerular AT1 Bmax was downregulated. Furthermore, both the captopril- and high insulin-treated groups had less glomerulosclerosis and vascular damage than the low insulin-treated group. PKCα, PKCδ, PKCε, and PKCμ isoforms found in preglomerular vessels were upregulated by captopril and high insulin doses, respectively, whereas no such regulation occurred in glomeruli. We conclude that in STZ-diabetic rats ANG II receptors and PKC isoforms on preglomerular vessels and glomeruli are differentially regulated by treatment with insulin and/or captopril.

Alkyl cinnamates as regulator for the C1 domain of protein kinase C isoforms

2012 ◽  
Vol 165 (3) ◽  
pp. 320-330 ◽  
Author(s):  
Narsimha Mamidi ◽  
Sukhamoy Gorai ◽  
Jashobanta Sahoo ◽  
Debasis Manna
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Kinase C ◽  
C1 Domain ◽  
Protein Kinase C Isoforms

Bidirectional modulation of parathyroid hormone-responsive adenylyl cyclase by protein kinase C

1994 ◽  
Vol 266 (6) ◽  
pp. E897-E904 ◽  
Author(s):  
A. M. Kitten ◽  
T. K. Hymer ◽  
M. S. Katz
Keyword(s):  
Protein Kinase C ◽  
Parathyroid Hormone ◽  
Protein Kinase ◽  
Adenylyl Cyclase ◽  
Catalytic Subunit ◽  
Mrna Levels ◽  
Binding Studies ◽  
Kinase C ◽  
Bidirectional Modulation ◽  
Umr 106

The temporal pattern with which phorbol 12-myristate 13-acetate (PMA), an activator of protein kinase C (PKC), modulates parathyroid hormone (PTH)-responsive adenylyl cyclase (AC) was evaluated in a clonal osteoblast-like cell line (UMR-106). Brief (< or = 1 h) exposure of UMR-106 cells to PMA enhanced PTH stimulation of AC, whereas more prolonged PMA treatment decreased the PTH response, with maximum inhibition occurring at < or = 6 h. PMA treatment also resulted in initial activation followed by downregulation of PKC. Exposure of cells to 1,2-dioctanoyl-sn-glycerol, which activated but did not downregulate PKC, resulted in bidirectional modulation of PTH-responsive AC identical to that produced by PMA. Prolonged PMA exposure decreased PTH receptor number, as determined by radioligand binding studies, and reduced PTH receptor mRNA levels, assessed by Northern blot analysis. Forskolin activation of the catalytic subunit of AC was also decreased after prolonged PMA treatment. The results suggest that activation of PKC sequentially stimulates and then inhibits PTH responsiveness. Inhibition of the PTH response occurs by PKC actions exerted on the PTH receptor and the AC catalytic subunit.

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