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First published online 29 April 2009
doi: 10.1242/dev.030775

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Extracellular matrix modifications at fertilization: regulation of dityrosine crosslinking by transamidation

Department of Molecular Biology, Cell Biology, and Biochemistry, Box G-L173, 185 Meeting Street, Brown University, Providence, RI 02912, USA.

^* Author for correspondence (e-mail: rhet{at}brown.edu)

Accepted 9 March 2009

Fertilization is accompanied by the construction of an extracellular matrix that protects the new zygote. In sea urchins, this structure is built from glycoproteins residing at the egg surface and in secretory vesicles at the egg cortex. Four enzymatic activities are required for the transformation of these proteins into the mechanically and chemically resilient fertilization envelope: proteolysis, transamidation, NADPH-dependent oxidation and peroxidation. Here, we identify the Strongylocentrotus purpuratus enzymes responsible for the formation of (-glutamyl)lysine crosslinks (transamidation). We find that these two transglutaminases are activated by local acidification and act on specific substrates within the fertilization envelope (including ovoperoxidase, rendezvin and SFE9). Surprisingly, these enzymes also regulate dityrosine crosslinking both by direct conjugation of ovoperoxidase and by modulating hydrogen peroxide production. Together, these results emphasize how transglutaminases can coordinate the activities of other enzymes during extracellular matrix transmogrifications.

Key words: Extracellular matrix, Fertilization, Transamidation, Transglutaminase, Sea urchin

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				J. L. Wong and G. M. Wessel Extracellular matrix modifications at fertilization: regulation of dityrosine crosslinking by transamidation J. Cell Sci., June 1, 2009; 122(11): e1 - e1. [Full Text]