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Phosphorylcreatine shuttle enzymes during perinatal heart development.

Biochemical Medicine and Metabolic Biology

|June 1, 1987

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During mammalian heart development, the phosphorylcreatine shuttle system significantly enhances cardiac function. Key enzymes like creatine kinase show substantial increases, contributing to improved heart performance from weaning to adulthood.

Area of Science:

Cardiovascular Physiology
Biochemistry
Developmental Biology

Background:

Mammalian heart function significantly improves from weaning to adulthood.
This enhancement correlates with increased aerobic metabolism and contractile protein ATPase activity.

Purpose of the Study:

To investigate the role of phosphorylcreatine shuttle enzymes in developmental changes in heart performance.
To understand the enzymatic basis for enhanced cardiac function during postnatal development.

Main Methods:

Assessed mitochondrial and myofibrillar ATPase specific activity in weanling and adult hearts.
Measured creatine kinase activity in both mitochondrial and myofibrillar fractions.
Evaluated changes in calcium sensitivity and purified myosin ATPase activity.

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Main Results:

Mitochondrial ATPase activity remained unchanged, but creatine kinase activity increased threefold.
Myofibrillar ATPase activity doubled, with a proportionally greater increase in myofibrillar creatine kinase activity.
Enhanced myofibrillar ATPase activity was not linked to calcium sensitivity or purified myosin alterations.

Conclusions:

Enzymatic reactions of the phosphorylcreatine shuttle system are significantly upregulated during normal heart development.
The enhanced phosphorylcreatine shuttle system is a key contributor to improved cardiac function in the perinatal period.
This mechanism is crucial for supporting the energetic demands of the growing mammalian heart.