Endothelial binding sites for lipoprotein lipase are not diminished in perfused hearts from diabetic rats

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Population

Perfused hearts from an acute, insulin-deficient rat model of diabetes and control rats

Comparison

Perfusion with exogenous lipoprotein lipase… vs Perfused hearts from control rats

Design

Preclinical

Authors

Discussion

Preserved endothelial LPL binding in diabetic rat hearts; leaves open mechanisms of reduced activity and relevance to human diabetic cardiomyopathy.

Population

Perfused hearts from an acute, insulin-deficient rat model of diabetes (induced by 100 mg/kg streptozotocin 4-5 days prior) and control rats

Intervention

Perfusion with exogenous lipoprotein lipase purified from bovine milk (mLPL) (0.05-2 micrograms/mL) followed by heparin perfusion

Comparator

Perfused hearts from control rats

Outcome

Binding and heparin-induced release of exogenous lipoprotein lipase (mLPL)surrogate

Diabetes does not alter low-affinity, high-capacity proteoglycan binding sites for lipoprotein lipase on the endothelium of perfused hearts.

Liu et al. (1996) studied this question.

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Preserved endothelial LPL binding in diabetic rat hearts; leaves open mechanisms of reduced activity and relevance to human diabetic cardiomyopathy.