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Composition changes in human tracheal cartilage in growth and aging, including changes in proteoglycan structure
1Pulmonary Research Laboratory, St. Paul's Hospital, University of British Columbia, Vancouver, Canada.
The American Journal of Physiology
|August 1, 1991
Summary
As humans age, tracheal cartilage proteoglycans change, impacting lung function. Link protein and proteoglycan aggregation decrease, while cartilage biomechanics are altered.
Area of Science:
- Biochemistry
- Biophysics
- Human Physiology
Background:
- Tracheal cartilage composition changes throughout life.
- Proteoglycans and link proteins are key cartilage components.
- Age-related changes in cartilage may affect lung function.
Purpose of the Study:
- To investigate age-related changes in human tracheal cartilage proteoglycans.
- To understand the functional implications of these changes on cartilage biomechanics and lung function.
Main Methods:
- Extraction and purification of high-buoyant-density proteoglycans from human tracheal cartilage (ages 1-58).
- Analysis of proteoglycan species, link protein concentration, and aggregation properties using gel electrophoresis.
- Assessment of hyaluronan-binding capacity and hydroxyproline content.
Main Results:
- Young cartilage had one major proteoglycan species; link protein increased with age until 14 years.
- Older individuals showed increased abundance of two other proteoglycan populations with higher mobility.
- Proteoglycan association with hyaluronan decreased with age, despite functional binding domains.
- Link proteins showed increased proteolysis, and hydroxyproline content decreased with age.
Conclusions:
- Age-related alterations in proteoglycan characteristics, including size, charge density, and aggregation, occur in human tracheal cartilage.
- These molecular changes likely contribute to altered cartilage biomechanics.
- Such biomechanical shifts may play a role in age-dependent changes observed in human lung function.