Acetoxy drug: Protein transacetylase catalyzed activation of human platelet nitric oxide synthase by polyphenolic peracetates

Khurana, Pulkit; Kumari, Rita; Vohra, Parag; Kumar, Ajit; Seema, .; Gupta, Garima; Raj, Hanumantharao G.; Dwarakanath, Bilikere S.; Parmar, Virinder S.; Saluja, Daman; Bose, Mridula; Vij, Anjana G; Chaudhary, Nabo K.; Adhikari, Jawahar Singh; Tyagi, Yogesh Kumar; Kohli, Ekta

doi:10.1016/j.bmc.2005.08.044

Cited by 42 publications

(26 citation statements)

References 23 publications

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“…Sodium nitrite was preincubated with the platelets followed by incubation with dichloro fluorescein-diacetate (DCFH-DA), the intense fluorescence of DCF was considered proportional to the extent of NO formation. 8) NO production in platelets was found to be linear with the concentration of nitrite (Fig. 3).…”

Section: Nitrite Dependent Enhancement Of No Levels In Plateletsmentioning

confidence: 83%

“…4) Previous work carried out in our laboratory projected polyphenolic acetates (PA) as the enhancers of NO in cells such as human platelets and rat tracheal smooth muscle cells. 8,21) In this connection polyphenolic acetate such as DAMC was found to produce NO from nitrite to a greater extent compare to parent polyphenol, DHMC. Our persistent investigations demonstrated for the first time the remarkable activation of CYPR by DAMC (Fig.…”

Section: Fig 7 Nitrite Reductase Catalyzed Modulation Of Cgmp Levelmentioning

confidence: 90%

“…7) Earlier work from our laboratory highlighted the presence of CRTAase in human platelets and activation of platelets NOS by polyphenolic acetates (PA) catalyzed by CRTAase. 8) Purified human placental CRTAase mediated acetylation of neuronal nitric oxide synthax (nNOS) by 7,8-diacetoxy-4-methylcoumarin (DAMC) was demonstrated. 9) Our earlier investigations strongly indicated the CRTAase 10) These observations prompted us to examine whether CYPR which is responsible for NR function; could similarly be activated leading to enhancement of intracellular levels of NO upon the addition of sodium nitrite.…”

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confidence: 99%

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The Role of Calreticulin Transacetylase in the Activation of Human Platelet Nitrite Reductase by Polyphenolic Acetates

Arora

Tyagi

Kumar

et al. 2009

Biological & Pharmaceutical Bulletin

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Nitric oxide (NO) is known to play an important role in the regulation of physiological functions. Various cell types are capable of synthesizing NO mainly from L-arginine with the participation of nitric oxide synthase (NOS). The action of NOS on L-arginine is the principal pathway to meet the tissue requirements of NO. The additional demand of NO in certain conditions of stress could be met by inducible nitric oxide synthase (iNOS). Several biological phenomena such as hypoxia is beset with the conditions where NOS is compromised, where the utilization of nitrates for the production of NO is encountered. 1) Nitrite reductase (NR) originally described in plants is discernible in microorganisms as well as mammalian cells. Panesar and Chan reported the NR activity in Mouse Leydig Tumor Cells and was attributed to mitochondrial respiratory chain complex III. Also, NO was found to be generated by the utilization of nitrite under basal conditions.2) Nitrate-NR system comprising of protein components such as pyridine nucleotides, flavoproteins and cytochromes are reported to be present in the mitochondria as well as the endoplasmic reticulum for the purpose of NO formation.1) In addition nitrite can function as a signaling molecule independent of the formation of NO.3) The oxidoreductase such as the cytochrome P-450 reductase (CYPR) is known to reduce inorganic nitrate to nitrite and then to NO. The reduction of nitrite to NO is ascribed to various factors including mitochondrial enzymes, polyphenols and protons. Keeping in view of the cardinal role played by NO in the physiology of the organisms it has become necessary to study the formation of nitrite and conversion to NO. It is worth mentioning that nitrate, mimics the role of NO in conditions such as normoxia and ischemic-reperfusion. 4) NO generated by reduction of nitrite by enzymes of cytochrome P-450 family is also responsible for the activation of cyclic guanosine monophosphate (cGMP) signaling pathway. 5,6) The extensive investigations carried out in our laboratory deciphered the identity of TAase with Calreticulin (CRT), a resident protein of the endoplasmic reticulum and consequently the TAase was given a name "Calreticulin transacetylase" (CRTAase). 7) Earlier work from our laboratory highlighted the presence of CRTAase in human platelets and activation of platelets NOS by polyphenolic acetates (PA) catalyzed by CRTAase.8) Purified human placental CRTAase mediated acetylation of neuronal nitric oxide synthax (nNOS) by 7,8-diacetoxy-4-methylcoumarin (DAMC) was demonstrated. 9)Our earlier investigations strongly indicated the CRTAase

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Section: Nitrite Dependent Enhancement Of No Levels In Plateletsmentioning

confidence: 83%

Section: Fig 7 Nitrite Reductase Catalyzed Modulation Of Cgmp Levelmentioning

confidence: 90%

mentioning

confidence: 99%

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The Role of Calreticulin Transacetylase in the Activation of Human Platelet Nitrite Reductase by Polyphenolic Acetates

Arora

Tyagi

Kumar

et al. 2009

Biological & Pharmaceutical Bulletin

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“…Acetyl CoA-independent protein acetylation is also known, but is restricted to the action of aspirin-like drugs that would readily acetylate cyclooxygenase resulting in the inhibition of prostaglandin synthesis and, thus, induce anti-inflammatory effects [14]. Through extensive studies, we identified a microsomal enzyme, protein transacetylase (TAase) in mammalian cells and tissues, catalysing the transfer of acetyl groups from 7,8-diacetoxy-4-methylcoumarin (DAMC) to certain receptor proteins, viz., cytosolic glutathione S-transferase (GST), cytochrome P-450-linked mixed function oxidases (MFO), Nicotinamide Adenine Dinucleotide Phosphate (NADPH) cytochrome c-reductase, protein kinase C (PKC), nitric oxide synthase (NOS), and recombinant glutamine synthetase (rGlnA1) of Mycobacterium tuberculosis, resulting in the modulation of their catalytic activities and associated physiological effects [15][16][17][18][19][20]. The rat liver and human placental microsomal TAase was later identified as calreticulin, a calcium-binding protein in the lumen of the endoplasmic reticulum and, consequently, the acetyltransferase function of calreticulin was appropriately termed calreticulin transacetylase (CRTAase) [21][22][23][24].…”

Section: Introductionmentioning

confidence: 99%

Biocatalytic Synthesis of Novel Partial Esters of a Bioactive Dihydroxy 4-Methylcoumarin by Rhizopus oryzae Lipase (ROL)

et al. 2016

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Abstract:Highly regioselective acylation has been observed in 7,8-dihydroxy-4-methylcoumarin (DHMC) by the lipase from Rhizopus oryzae suspended in tetrahydrofuran (THF) at 45 • C using six different acid anhydrides as acylating agents. The acylation occurred regioselectively at one of the two hydroxy groups of the coumarin moiety resulting in the formation of 8-acyloxy-7-hydroxy-4-methylcoumarins, which are important bioactive molecules for studying biotansformations in animals, and are otherwise very difficult to obtain by only chemical steps. Six monoacylated, monohydroxy 4-methylcoumarins have been biocatalytically synthesised and identified on the basis of their spectral data and X-ray crystal analysis.

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“…19 Acetylation of hydroxy xanthones and thioxanthones can further enhance their biological activities. 23,24 Monohydroxyxanthones, such as 1-hydroxyxanthone, are reported in the literature as monoamine oxidase inhibitors, 25,26 α-glucosidase inhibitors 27,28 and exhibit antioxidant properties. 29 Of the dihydroxyxanthones, 1,3-dihydroxyxanthone possesses antimalarial activity, 30 antihypertensive activity 31 and can inhibit α-glucosidase.…”

Section: Introductionmentioning

confidence: 99%

An efficient and convenient microwave-assisted chemical synthesis of (thio)xanthones with additional in vitro and in silico characterization

Verbanac

Jain

et al. 2012

Bioorganic & Medicinal Chemistry

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Acetoxy drug: Protein transacetylase catalyzed activation of human platelet nitric oxide synthase by polyphenolic peracetates

Cited by 42 publications

References 23 publications

The Role of Calreticulin Transacetylase in the Activation of Human Platelet Nitrite Reductase by Polyphenolic Acetates

The Role of Calreticulin Transacetylase in the Activation of Human Platelet Nitrite Reductase by Polyphenolic Acetates

Biocatalytic Synthesis of Novel Partial Esters of a Bioactive Dihydroxy 4-Methylcoumarin by Rhizopus oryzae Lipase (ROL)

An efficient and convenient microwave-assisted chemical synthesis of (thio)xanthones with additional in vitro and in silico characterization

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