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Related Concept Videos

Phase II Reactions: Acetylation Reactions01:24

Phase II Reactions: Acetylation Reactions

Acetylation, a phase II biotransformation reaction, introduces an acetyl group to drugs or their metabolites. Acetyltransferase enzymes facilitate this reaction, which resembles α-amino acid conjugation due to the addition of a functional group to the drug molecule.
The substrates for acetylation are typically drugs or their metabolites with an amino, sulfonamide, or hydrazine functional group. Acetylation can occur at several points in the drug molecule, including primary, secondary, and...
Allosteric Proteins-ATCase01:19

Allosteric Proteins-ATCase

Binding sites linkages can regulate a protein's function.  For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor.
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to  N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis pathway,...
Antiplatelet Drugs: Prostaglandin Synthesis, P2Y12 and Glycoprotein IIb/IIIa Inhibitors01:20

Antiplatelet Drugs: Prostaglandin Synthesis, P2Y12 and Glycoprotein IIb/IIIa Inhibitors

Antiplatelet drugs emerge as frontline defenders against the insidious threat of thromboembolic diseases, where abnormal clots obstruct vital blood vessels. These drugs stand as bulwarks, inhibiting platelet aggregation and clot formation, thereby mitigating the risk of life-threatening conditions like myocardial infarction, coronary artery disease, and thrombotic strokes.
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Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
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Phase II Reactions: Sulfation and Conjugation with α-Amino Acids01:19

Phase II Reactions: Sulfation and Conjugation with α-Amino Acids

Sulfation and α-amino acid conjugation are two critical biotransformation reactions in drug metabolism. Sulfation, a phase II biotransformation reaction, involves adding a polar sulfate group to a drug, enhancing its water solubility and promoting excretion. This process can either co-occur with or occur independently of glucuronidation. Nonmicrosomal sulfotransferase enzymes catalyze the process. The reaction involves 3'-phosphoadenosine-5'-phosphosulfate or PAPS coenzyme activation, sulfur...
Intracellular Signaling Affects Focal Adhesions01:17

Intracellular Signaling Affects Focal Adhesions

Integrins act both as extracellular input receivers and as intracellular processing activators. As their name suggests, integrins are entirely integrated into the membrane structure. Their hydrophobic membrane-spanning regions interact with the phospholipid bilayer's hydrophobic region. These membrane receptors provide extracellular attachment sites for effectors like hormones and growth factors. They activate intracellular response cascades when their effectors are bound and active.
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Synthesis and Characterization of an Aspirin-fumarate Prodrug that Inhibits NF&#954;B Activity and Breast Cancer Stem Cells
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Does aspirin acetylate multiple cellular proteins? (Review).

Lloyd F Alfonso1, Kalkunte S Srivenugopal, G J Bhat

  • 1Department of Pharmaceutical Sciences and Cancer Biology Center, Texas Tech University Health Sciences Center, Amarillo, TX 79106, USA.

Molecular Medicine Reports
|April 9, 2011
PubMed
Summary

Aspirin (acetylsalicylic acid) acetylates proteins beyond cyclooxygenases, including tumor suppressor p53. This protein acetylation may explain aspirin's beneficial and adverse effects, opening new research avenues.

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Synthesis and Characterization of an Aspirin-fumarate Prodrug that Inhibits NF&#954;B Activity and Breast Cancer Stem Cells
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Detection of Protein S-Acylation using Acyl-Resin Assisted Capture
08:31

Detection of Protein S-Acylation using Acyl-Resin Assisted Capture

Published on: April 10, 2020

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Pharmacology

Background:

  • Aspirin (acetylsalicylic acid) is widely used for anti-inflammatory, analgesic, and anti-thrombotic effects.
  • Emerging evidence suggests aspirin may decrease epithelial cancer incidence.
  • While cyclooxygenase inhibition is well-understood, aspirin's chemopreventive and some adverse effects remain unclear.

Purpose of the Study:

  • To review current literature on aspirin-induced protein acetylation.
  • To present an immunological method for detecting acetylated proteins.
  • To explore the potential role of protein acetylation in aspirin's effects.

Main Methods:

  • Literature review of studies on aspirin and protein acetylation.
  • Description of an immunological approach using anti-acetyl lysine antibodies.
  • Demonstration of aspirin-induced acetylation in multiple proteins in treated cells.

Main Results:

  • Aspirin acetylates proteins beyond cyclooxygenases, including the tumor suppressor p53.
  • An immunological method effectively detects aspirin-acetylated proteins.
  • Multiple cellular proteins were found to be acetylated by aspirin.

Conclusions:

  • Aspirin-induced protein acetylation is a significant post-translational modification.
  • This acetylation may underlie previously unexplained beneficial and adverse effects of aspirin.
  • Identifying novel aspirin acetylation targets is a promising new research direction.