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Media Availability: Newly discovered features of collagen may help shed light on disease processes

NIH study shows abundant structural protein is dynamic, not just an inert scaffold for cells

For Immediate Release:
July 12, 2016

WHAT:  Scientists at the National Institutes of Health are reporting new, unexpected details about the fundamental structure of collagen, the most abundant protein in the human body. In lab experiments, they demonstrated that collagen, once viewed as inert, forms structures that regulate how certain enzymes break down and remodel body tissue.  The finding of this regulatory system provides a molecular view of the potential role of physical forces at work in heart disease, cancer, arthritis, and other disease-related processes, they say.  The study appears in the current online issue of the Proceedings of the National Academy of Sciences.

Scientists have known for years that collagen remodeling plays an important role in a wide variety of biological processes ranging from wound healing to cancer growth.  In particular, researchers know that collagen is broken down by a certain class of enzymes called matrix metalloproteinases (MMPs), but exactly how they did this remained somewhat of a mystery, until now.

In the NIH study, the scientists isolated individual, nano-sized collagen fibrils from rat-tail tendons.  They then exposed the collagen fibrils to fluorescently-labeled human MMP enzymes.  Using video microscopy, the scientists tracked thousands of enzymes moving along a fibril. Unexpectedly, the scientists observed that the enzymes preferred to attach at certain sites along the fibril, and over time these attachment sites slowly moved, or disappeared and reappeared in other positions.  These observations revealed collagen fibrils have defects that spontaneously form and heal.  In the presence of tension, such as when tendons stretch, defects are likely eliminated, preventing enzymes from breaking down collagen that is loaded by physical force, the researchers suggest. In short, they identified a possible strain-sensitive mechanism for regulating tissue remodeling.    

In addition to primary support by the National Heart, Lung, and Blood Institute (NHLBI), the current study is also supported by the National Institute of Arthritis and Musculoskeletal and Skin Diseases (NIAMS) and the National Cancer Institute (NCI). All are part of the National Institutes of Health.

WHO:  Keir C. Neuman, Ph.D., senior investigator in the Laboratory of Single Molecule Biophysics at the NHLBI and corresponding author of the study, is available to comment on the findings and implications of this research.

CONTACT:  For more information or to schedule an interview, please contact the NHLBI Office of Science Policy, Engagement, Education, and Communications at 301-496-5449 or nhlbi_news@nhlbi.nih.gov (link sends e-mail).