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Related Concept Videos

Overview of Protein Metabolism01:21

Overview of Protein Metabolism

Proteins are broken down into amino acids during digestion. Unlike fats and carbohydrates, which are stored for later use, proteins are not. Instead, amino acids are either used to produce ATP through oxidation or contribute to the creation of new proteins for the growth and repair of the body. Any surplus amino acids from the diet are converted into glucose or triglycerides rather than excreted.
Amino acids play various roles in the body once they are absorbed into cells. They are restructured...
Biosynthesis of Nucleic Acids01:28

Biosynthesis of Nucleic Acids

Nucleic acid biosynthesis is a fundamental biochemical process that produces the purine and pyrimidine nucleotides essential for DNA and RNA synthesis. This pathway maintains a balanced nucleotide pool, preventing imbalances that could jeopardize genetic integrity and cellular function. Given the crucial role of nucleotides, their synthesis is tightly regulated to ensure proper cellular homeostasis.Purine BiosynthesisThe biosynthesis of purine nucleotides begins with ribose-5-phosphate, a...
Amino Acid Catabolism01:18

Amino Acid Catabolism

Microorganisms rely on proteins as an essential carbon and energy source, particularly in environments with limited polysaccharides or lipids. However, proteins are too large to cross the plasma membrane unaided, necessitating enzymatic degradation. Microbes secrete extracellular proteases and peptidases that hydrolyze proteins into peptides, which can then be transported across the membrane. Once inside the cell, intracellular proteases degrade these peptides into free amino acids, which...
Urea Cycle01:23

Urea Cycle

The urea cycle describes how liver cells convert ammonia to urea. Ammonia is a toxic waste product of protein catabolism. Land animals must convert ammonia into the less toxic urea which can be safely eliminated by the kidneys through urine. Marine animals excrete ammonia directly, and the surrounding water dilutes the ammonia to safe levels.
Lysosomal Hydrolases01:22

Lysosomal Hydrolases

Lysosomes are the site for the degradation of macromolecules and biological polymers released during membrane trafficking events such as secretory, endocytic, autophagic, and phagocytic pathways. The membrane-enclosed area of the lysosome, called the lumen, contains hydrolytic enzymes active in an acidic environment. These acid hydrolases are functional at a pH between 4.5 and 5 and are involved in cellular processes such as cell signaling, energy metabolism, restoration of the plasma membrane,...
Amino Acid Biosynthetic Pathways01:29

Amino Acid Biosynthetic Pathways

Amino acid biosynthesis is essential for cell growth, protein synthesis, and metabolic regulation. Cells generate essential and non-essential amino acids from metabolic intermediates to sustain vital biological functions. These intermediates originate from key metabolic pathways: glycolysis, the tricarboxylic acid (TCA) cycle, and the pentose phosphate pathway. Important precursors include α-ketoglutarate, pyruvate, oxaloacetate, phosphoenolpyruvate, and erythrose-4-phosphate, which provide...

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Updated: Jun 21, 2026

Caenorhabditis elegans as a Model System for Discovering Bioactive Compounds Against Polyglutamine-Mediated Neurotoxicity
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Polyamine catabolism and disease.

Robert A Casero1, Anthony E Pegg

  • 1Department of Oncology, Johns Hopkins University School of Medicine and the Sidney Kimmel Comprehensive Cancer Center at Johns Hopkins, Baltimore, MD 21231, USA. rcasero@jhmi.edu

The Biochemical Journal
|July 11, 2009
PubMed
Summary
This summary is machine-generated.

Polyamine catabolism, involving enzymes like SSAT, SMO, and APAO, is crucial for drug response and disease, including cancer. Understanding its dysregulation offers therapeutic targets for various pathological states.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cellular Biology

Background:

  • Polyamine catabolism significantly influences cellular processes, including drug response, apoptosis, and stress reactions.
  • Dysregulation of polyamine catabolism is linked to various diseases, notably cancer, highlighting its pathological relevance.
  • Key enzymes in polyamine catabolism include spermidine/spermine N1-acetyltransferase (SSAT), spermine oxidase (SMO), and N1-acetylpolyamine oxidase (APAO).

Purpose of the Study:

  • To review the role of polyamine catabolism in disease etiology and treatment.
  • To provide a comprehensive background on the critical aspects of polyamine catabolism in biological systems.
  • To explore the therapeutic potential of targeting polyamine catabolism pathways.

Main Methods:

  • Review of existing literature on polyamine catabolism and its role in disease.
  • Analysis of the functions of key enzymes: SSAT, SMO, and APAO.
  • Examination of the impact of polyamine catabolism on cellular homeostasis and signaling.

Main Results:

  • Polyamine catabolism enzymes significantly impact drug response, apoptosis, and stress responses.
  • Enzyme dysregulation contributes to pathological conditions, offering potential therapeutic targets.
  • Oxidative stress, via H2O2 and aldehydes produced by SMO and APAO, is a key mechanism in disease pathogenesis.

Conclusions:

  • Polyamine catabolism is a critical regulator of cellular functions and a significant contributor to disease development.
  • Targeting enzymes involved in polyamine catabolism presents a promising therapeutic strategy for various diseases.
  • Further research into polyamine catabolism offers insights into disease mechanisms and novel treatment opportunities.