Enzyme found to control formation of collagen carriers and inhibit collagen secretion

phys.org | 6/11/2018 | Staff
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Researchers at Tokyo Institute of Technology (Tokyo Tech) have identified an enzyme that controls how much collagen cells secrete. As collagen imbalance is linked to a range of human diseases, the study provides clues to new therapeutic strategies. Moreover, the findings could facilitate efficient production of collagen for the food, cosmetic and pharmaceutical industries.

All cells make and release proteins. The proteins are packaged as "cargo" in tiny, bubble-like vesicles before being transported outside the cell. This process, known as secretion, is vital to healthy growth and development.

Studies - Vesicles - COPII - Carriers - Cargo

Although many studies have shown how these vesicles, called COPII carriers, handle relatively small-sized cargo, few have focused on the workings of unusually large carriers known to package very large proteins, such as collagen.

Now, a study by researchers including Masayuki Komada, Toshiaki Fukushima and graduate student Kohei Kawaguchi at Tokyo Institute of Technology has identified USP8 as a key enzyme involved in controlling the formation of large collagen carriers. They have reported their findings in the journal Biochemical and Biophysical Research Communications.

Findings - Implications - Medicine - Biotechnology - Collagen

The findings have big implications for medicine and biotechnology. Excessive collagen secretion in the human body is known to cause organ fibrosis, while too little collagen secretion is associated with bone diseases including cranio-lenticulo-sutural dysplasia (CLSD) and Cole-Carpenter syndrome. New treatments for these diseases could be developed through further understanding of USP8's exact mode of action. Such knowledge could also provide new ways of scaling up commercial production of collagen.

The researchers have demonstrated that the...
(Excerpt) Read more at: phys.org
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