Cinnamomin--a versatile type II ribosome-inactivating protein

Acta Biochim Biophys Sin (Shanghai). 2004 Mar;36(3):169-76. doi: 10.1093/abbs/36.3.169.

Abstract

Ribosome-inactivating proteins (RIPs) are a group of toxic proteins that can specifically act on the universally conserved sarcin/ricin domain (S/R domain) of the largest RNA in ribosome and thus irreversibly inactivate ribosome for protein synthesis. Cinnamomin is a multifunctional type II RIP isolated in our laboratory from the mature seeds of the camphor tree. This protein has been extensively studied with regard to its purification, characteristics, structure and function, genetic expression, enzymatic mechanism, physiological role in seed cell and toxicity to cancer cells and insect larvae. The research results of cinnamomin obtained in our laboratory are summarized in this review. Understanding of cinnamomin and the relative new proteins will help expand our knowledge of RIPs and may accelerate theoretical study and the development of their potential applications.

Publication types

  • Review

MeSH terms

  • Algal Proteins
  • Animals
  • Antineoplastic Agents, Phytogenic / chemistry
  • Antineoplastic Agents, Phytogenic / metabolism
  • Antineoplastic Agents, Phytogenic / pharmacology
  • Enzyme Activation
  • Humans
  • Insecta / drug effects
  • Larva / drug effects
  • Plant Proteins / chemistry
  • Plant Proteins / metabolism
  • Proteins / chemistry*
  • Proteins / metabolism*
  • Proteins / pharmacology
  • Rats
  • Ribosome Inactivating Proteins, Type 2
  • Ribosomes / chemistry*
  • Seeds / metabolism
  • Structure-Activity Relationship
  • Tumor Cells, Cultured / drug effects

Substances

  • Algal Proteins
  • Antineoplastic Agents, Phytogenic
  • Plant Proteins
  • Proteins
  • Ribosome Inactivating Proteins, Type 2
  • cinnamomin, Phytophthora cinnamomi