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Plasminogen activation system in human milk

C W Heegaard¹, L B Larsen, L K Rasmussen

¹Department of Molecular and Structural Biology, University of Aarhus, Denmark.

Journal of Pediatric Gastroenterology and Nutrition

|August 1, 1997

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Human milk contains plasminogen activators tissue-type plasminogen activator (t-PA) and urokinase-type plasminogen activator (u-PA) with distinct distributions. Casein micelles bind t-PA and plasminogen, while cells bind u-PA.

Area of Science:

Biochemistry
Protease activity in biological fluids

Background:

Plasmin is a key protease in milk, regulated by plasminogen, activators, and inhibitors.
Previous studies showed differential distribution of tissue-type plasminogen activator (t-PA) and urokinase-type plasminogen activator (u-PA) in bovine milk.

Purpose of the Study:

To investigate the distribution of plasminogen activation system components in human milk fractions.
To determine if the differential distribution of t-PA and u-PA is a conserved feature across species.

Main Methods:

Human milk samples fractionated into fat, skim milk, and cells via centrifugation.
Plasminogen and plasminogen activators detected using immunoblotting and zymography.
Ligand binding analysis and chromogenic assays used to study t-PA and u-PA distribution and activity.

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Main Results:

Differential distribution of plasminogen, t-PA, and u-PA observed in human milk fractions.
Casein micelles demonstrated binding activity for t-PA and plasminogen.
Cellular fractions identified u-PA receptors as the binding component for u-PA.

Conclusions:

The distinct distribution of u-PA and t-PA suggests specialized physiological roles.
These roles may include antimicrobial defense (u-PA) and maintaining mammary duct patency (t-PA).