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HS-No. 294190009000
C16H24O4 Mr 280.4 [20350-15-6]

Brefeldin Macrolide antibiotic from Penicillium brefeldianum. Brefeldin Specifically inhibits translocation of proteins from the endoplasmic reticu lum to the Golgi apparatus

what is brefeldin

Brefeldin A (BFA), a metabolite of the fungus Eupenicillium brefeldianum, specifically and reversibly blocks protein transport from the endoplasmic reticulum (ER) to the Golgi apparatus in many cell types and species. (1-3) These effects are generally accompanied by distinct morphological changes, including the apparent collapse of the Golgi stacks. The fast and reversible redistribution of intracellular membranes is accompanied by various specific and reversible effects on cellular protein traffic (Figure 1). These include blockage of the following processes: protein transport from the ER to the Golgi; protein secretion; vesicular assembly; antigen presentation;

The precise effects of BFA vary among cell types. Studies have implicated GTP-binding proteins and specific integral and peripheral Golgi membrane proteins in the effects of BFA. (4,5) BFA also has antiviral, antibacterial, and antifungal activities. (6) BFA has relatively low toxicity; the LD50 in mice (intraperitoneal injection) is greater than 200 mg/kg. (7) Because of its numerous and reversible effects on protein transport and processing, BFA has become an important tool for cell biologists.

Brefeldin Applications


Brefeldin selected  references

* Brefeldin A effects in plant and fungal cells: something new about vesicle trafficking?
* Brefeldin A and the endocytic pathway. Possible implications for membrane traffic and sorting.
* Biological effects of the antibiotic brefeldin A (decumbin, cyanein, ascotoxin, synergisidin): a retrospective.

Interaction of FK506-binding protein 13 with brefeldin A-inhibited guanine nucleotide-exchange protein 1 (BIG1): Effects of FK506.

* Inhibition of Japanese encephalitis virus maturation and transport in PS cells to cell surface by brefeldin A.

Protein kinase A-anchoring (AKAP) domains in brefeldin A-inhibited guanine nucleotide-exchange protein 2 (BIG2).

* Brefeldin A-induced neurotoxicity in cultured spinal cord neuron




[top] This page was done by a student of Bioinformatics, Open University Jerusalem Israel, in a homage to Fermentek and to Dr Berend.
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