UNC-CH Ligament-Tendon Structure Discovery May Lead To Better Treatment, Scientists Explain

February 01, 1999

CHAPEL HILL -- Researchers at the University of North Carolina at Chapel Hill have discovered that a simple molecule known as a pentapeptide tends to block binding of one collagen fibril to another.

The discovery will be important, the scientists say, because collagen fibrils make up dense connective tissues in the body such as ligaments and tendons. One day, they and other researchers should be able to take advantage of that fact to improve restricted movement due to joint injuries, including damage from athletics, accidents and aging.

"We have been working on trying to figure out what holds different collagen fibrils together for a long time, and recently we found that this peptide tends to break them apart," said Dr. Laurence E. Dahners, professor of orthopaedics at the UNC-CH School of Medicine. "We also have found that tendons become more stretchy when they are immersed in this material."

Dahners, Dr. Gayle Lester, research associate professor of orthopaedics, and resident Dr. Peter Caprise conducted the experiments. They presented their findings Feb. 1 at the Orthopaedic Research Society's annual meeting in Anaheim, Calif.

"This work, which we did on rat tail tendons, is exciting because no one has been able to release fibrils from vertebrate tissue before," Dahners said. "We now have pictures of fibrils that we have been able to extract from the rat tail tendons. No one has ever seen these structures before either."

Although the research was conducted on rat tissues it likely will apply to humans as well since humans and other mammals have far more similarities in tissues than differences, the surgeon said. Further experiments should confirm that identical or comparable peptides work in humans.

"We have known for a long time that after injuries, the body heals by making tiny collagen fibrils although we don't know how long they are yet," Dahners said. "With further work, we should now be able to learn more about them - how long they are, what their shapes are and how they are formed in the body. Then we will understand a lot more about the healing process and how we might be able to take advantage of it in treatment or change it."

One unproven possibility is that doctors might one day be able to inject the peptides into patients to loosen up stiff joints, he said. Injured joints often stiffen because collagen fibers stick together and restrict normal movement in hips, shoulders and knees, for example.

The Aileen Stock Orthopaedic Research Fund supported the UNC-CH medical studies.
-end-
Note: Dahners can be reached at 919-966-3340, Lester at 966-9078. During the meeting they will stay at the Best Western Stovall's Inn in Anaheim. Phone: 714-778-1880. Fax: 714-778-3805.



University of North Carolina at Chapel Hill

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