Distinctive roles of PHAP proteins and prothymosin-alpha in a death regulatory pathway

Science. 2003 Jan 10;299(5604):223-6. doi: 10.1126/science.1076807.

Abstract

A small molecule, alpha-(trichloromethyl)-4-pyridineethanol (PETCM), was identified by high-throughput screening as an activator of caspase-3 in extracts of a panel of cancer cells. PETCM was used in combination with biochemical fractionation to identify a pathway that regulates mitochondria-initiated caspase activation. This pathway consists of tumor suppressor putative HLA-DR-associated proteins (PHAP) and oncoprotein prothymosin-alpha (ProT). PHAP proteins promoted caspase-9 activation after apoptosome formation, whereas ProT negatively regulated caspase-9 activation by inhibiting apoptosome formation. PETCM relieved ProT inhibition and allowed apoptosome formation at a physiological concentration of deoxyadenosine triphosphate. Elimination of ProT expression by RNA interference sensitized cells to ultraviolet irradiation-induced apoptosis and negated the requirement of PETCM for caspase activation. Thus, this chemical-biological combinatory approach has revealed the regulatory roles of oncoprotein ProT and tumor suppressor PHAP in apoptosis.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Apoptosis*
  • Apoptotic Protease-Activating Factor 1
  • Caspase 3
  • Caspase 9
  • Caspases / metabolism
  • Cell Extracts
  • Cytochrome c Group / metabolism
  • Deoxyadenine Nucleotides / metabolism
  • Deoxyadenine Nucleotides / pharmacology
  • Enzyme Activation
  • HeLa Cells
  • Humans
  • Intracellular Signaling Peptides and Proteins
  • Mitochondria / metabolism
  • Molecular Sequence Data
  • Neuropeptides*
  • Nuclear Proteins / chemistry
  • Nuclear Proteins / isolation & purification
  • Nuclear Proteins / metabolism*
  • Nuclear Proteins / pharmacology
  • Protein Precursors / chemistry
  • Protein Precursors / isolation & purification
  • Protein Precursors / metabolism*
  • Protein Precursors / pharmacology
  • Proteins / chemistry
  • Proteins / isolation & purification
  • Proteins / metabolism*
  • Proteins / pharmacology
  • Pyridines / chemistry
  • Pyridines / pharmacology*
  • RNA Interference
  • RNA-Binding Proteins
  • Recombinant Proteins / metabolism
  • Recombinant Proteins / pharmacology
  • Signal Transduction
  • Thymosin / analogs & derivatives*
  • Thymosin / chemistry
  • Thymosin / isolation & purification
  • Thymosin / metabolism*
  • Thymosin / pharmacology
  • Tumor Suppressor Proteins / chemistry
  • Tumor Suppressor Proteins / isolation & purification
  • Tumor Suppressor Proteins / metabolism

Substances

  • ANP32A protein, human
  • ANP32B protein, human
  • APAF1 protein, human
  • Apoptotic Protease-Activating Factor 1
  • Cell Extracts
  • Cytochrome c Group
  • Deoxyadenine Nucleotides
  • Intracellular Signaling Peptides and Proteins
  • Neuropeptides
  • Nuclear Proteins
  • Protein Precursors
  • Proteins
  • Pyridines
  • RNA-Binding Proteins
  • Recombinant Proteins
  • Tumor Suppressor Proteins
  • alpha-(trichloromethyl)-4-pyridineethanol
  • prothymosin alpha
  • Thymosin
  • CASP3 protein, human
  • CASP9 protein, human
  • Caspase 3
  • Caspase 9
  • Caspases
  • 2'-deoxyadenosine triphosphate