Abstract

Publisher Summary This chapter elaborates the structural chemistry and the biological aspects of ADAM28, (mouse form). A fragment of the mouse ADAM28 cDNA encoding the disintegrin domain was identified in a screen for novel ADAM genes by PCR (sequence tag 16–3). There are at least two splice variants of ADAM28, one of which encodes a membrane-anchored form, while the other most likely encodes a soluble form lacking the transmembrane and cytoplasmic domain. Full-length membrane-anchored ADAM28 contains all domains that are typical for an ADAM. Similar to other ADAMs, the cytoplasmic domain of ADAM28 includes signaling motifs, such as proline-rich SH3 ligand domains. Six potential N-linked glycosylation sites are present in the ectodomain of ADAM28. Northern blot analysis of the expression pattern of ADAM28 mRNA in different mouse tissues revealed high expression in the epididymis and lower expression in the lung. A splice variant of ADAM28 that most likely does not contain a transmembrane domain and cytoplasmic domain is found in the epididymis, but not in the lung. Similar to other ADAMs, ADAM28 is produced as a proform in the secretory pathway and is processed in transit to the cell surface.

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