evels. MIG-17 molecules designed with deficient glycosylation sites also failed to localize at the gonad and showed no ability to direct its migration. Genetic analyses revealed that MIG-23 is expressed in muscle cells, which reconciles well with MIG-17fs muscle cell origins. Taken together, these results indicate that MIG-17 molecules are secreted from muscle cells after glycosylation by MIG-23, a modification which enables their recruitment to the migrating gonad.

Although Golgi NDPases such as MIG-23 can conceivably modify a number of other secreted proteins, the Nishiwaki study indicates that the effects of the NDPase dysfunction are especially prominent in the abnormal glycosylation and function of an ADAM family protease, suggesting that glycosylation may play a more important role in the function of proteins in this family than it does in that of other secreted proteins. ADAM family proteases are known to be involved in a number of human diseases, and the question of whether glycosylation defects play a role in their pathogenesis merits further investigation. Research such as this provides insights into basic biological mechanisms that may one day make it possible to treat a range of health conditions by restoring normal ADAM protease glycosylation in cases in which it is aberrant.

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Contact: Doug Sipp
sipp@cdb.riken.jp
RIKEN Center for Developmental Biology
25-Dec-2003

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