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A calcium-protease activator associated with brain microsomal-insoluble elements.

Y Takeyama, H Nakanishi, Y Uratsuji

|January 1, 1986

Summary

A novel heat-stable protein factor was identified that significantly activates calcium-dependent thiol protease (calpain) in bovine brain microsomes. This protein, distinct from calmodulin, also activates calpain in human platelets.

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Area of Science:

Biochemistry
Molecular Biology
Cell Biology

Background:

Calpains are calcium-dependent cysteine proteases involved in various cellular processes.
The regulation of calpain activity is crucial for cellular function and homeostasis.
Previous studies have identified calmodulin as a key regulator of some calpains.

Purpose of the Study:

To identify and characterize novel regulatory factors of calpain activity.
To investigate the association of calpain activators with cellular structural components.
To determine if calmodulin can substitute for the identified factor.

Main Methods:

Extraction of Triton X-100-insoluble materials from bovine brain microsomes.
Partial purification of the activating factor using KCl extraction, sucrose density gradient centrifugation, and hydroxyapatite column chromatography.

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Assay of the factor's effect on calpain I and calpain II activity using casein as a substrate.

Main Results:

A heat-stable protein factor (approximate Mr 15,000) activating calpains was isolated from insoluble cellular fractions.
The factor significantly increased calpain activity (several-fold to over 10-fold) without altering calcium affinity.
Calmodulin did not substitute for the activity of this novel factor.
A similar factor was found in human platelet insoluble materials.

Conclusions:

A novel protein factor, distinct from calmodulin, significantly activates both calpain I and calpain II.
This calpain-activating factor is associated with cytoskeletal or other insoluble cellular components.
The findings suggest a new regulatory mechanism for calpain activity in both brain and platelets.