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Lipase activity in the human aorta.

K Hayase, B F Miller

Journal of Lipid Research

|May 1, 1970

Summary

This summary is machine-generated.

Human aortic tissue contains both acid and alkaline lipase enzymes that hydrolyze triglycerides. These enzymes exhibit distinct properties and are affected differently by substrates, ions, and inhibitors, suggesting varied physiological roles.

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Area of Science:

Biochemistry
Human Physiology
Enzymology

Background:

Triglyceride hydrolysis is crucial for lipid metabolism.
Aortic tissue's enzymatic activity in lipid breakdown is not fully understood.

Purpose of the Study:

To investigate the in vitro hydrolysis of triglycerides by human aortic tissue.
To characterize the properties of acid and alkaline lipases present in the aorta.

Main Methods:

In vitro study of triglyceride hydrolysis using human aortic tissue.
Enzyme activity assays at different pH optima (acidic and alkaline).
Analysis of substrate specificity, ion activation, and inhibitor effects.

Main Results:

Aortic tissue possesses both acid (pH 5.4) and alkaline (pH 8.8) lipase activities.

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Both lipases hydrolyze saturated triglycerides, with activity decreasing for longer fatty acyl chains.

Alkaline lipase is sensitive to substrate concentration and activated by bile salts, while acid lipase is inhibited by bile salts and sensitive to homogenization/dialysis media.

Conclusions:

Human aortic lipases display distinct biochemical characteristics.
The presence of both acid and alkaline lipases suggests complex roles in aortic lipid metabolism.
Aortic tissue contains endogenous inhibitors for both acid and alkaline lipases.