e disease. Other scientists, in fact, had found that some individuals with an early onset and severe form of osteoarthritis harbor mutations that change an amino acid sequence in collagen II. But it wasn't clear why this led to osteoarthritis. In the study, Dr. Fertala and his group followed the formation of the cartilage scaffolding and watched how the mutation in collagen II and the resulting amino acid change in the protein altered the precise alignment of the two types of collagens.

According to Dr. Fertala, the results will help to identify "weak points" in the complex cartilage structure in patients with a mutated collagen gene and protein.

He was surprised by the findings. "The problem with understanding how these mutations work is that in many cases, a collagen mutation results in a protein still behaving normally. But when you study the interaction with its normal partner, it shows something has gone awry. This is very new in the collagen research field.

"The next step with this model would be to try to somehow block the mutated sites to prevent these unspecific interactions, which results in osteoarthritis," he notes. Finding ways to counteract such weak points in the cartilage structure might slow down or reduce the development of the disease.

Osteoarthritis is a very common and disabling disease of cartilage of the joints that affects millions of people worldwide. It is the most common cause of disability, absence to work and places an enormous socioeconomic burden. Its cause is unknown, but a number of factors such as aging, mechanical stress, inflammation and trauma are often associated with its development.

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Contact: Steve Benowitz
steven.benowitz@mail.tju.edu
215-955-5291
Thomas Jefferson University
11-Dec-2001

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