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UCLA identifies new molecule involved in the body's processing of dietary fat

in the absence of GPIHBP1.

Laboratory tests confirmed that GPIHBP1-deficient mice had much higher levels of chylomicrons in the bloodstream than normal mice. The GPIHBP1-deficient mice had grossly milky plasma, reflecting very large amounts of triglycerides in the blood.

"These findings indicate a defect in the breakdown of chylomicrons in mice that don't have GPIHBP1," Beigneux said.

Investigators predicted that if GPIHBP1 were involved in the processing of chylomicrons in the bloodstream, then the protein would be made by endothelial cells of capillaries, where the breakdown of triglycerides takes place. Indeed, microscopy showed that GPIHBP1 is expressed highly and exclusively on the endothelial cells of capillaries of heart, adipose tissue and skeletal muscle.

Interestingly, scientists found that this protein was absent from the brain, which mainly uses glucose for energy.

"These differences suggest that endothelial cells may play an active role in regulating the delivery of lipid nutrients to different tissues," Beigneux said.

Experiments with cultured cells revealed that GPIHBP1 binds both chylomicrons and lipoprotein lipase, suggesting GPIHBP1 is a key platform for the processing of chylomicrons.

The next step, according to investigators, will be to determine if GPIHBP1 provides the only binding site for chylomicrons and lipoprotein lipase within capillaries. In addition, investigators would like to define the molecular basis for how GPIHBP1 binds to chylomicron particles.


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Contact: Rachel Champeau
rchampeau@mednet.ucla.edu
310-794-2270
University of California - Los Angeles
3-Apr-2007


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