First published online March 23, 2006
Development 133, 803e (2006)
© The Company of Biologists Limited
Skin-deep ADAMTS similarities
The major structural elements of most tissues are formed from type I, II
and III collagens, which are made as procollagens. An aminopropeptidase called
ADAMTS2 can remove the N-propeptide of all three procollagens, but,
surprisingly, ADAMTS2 defects in animals cause only dermatosparaxis (severe
skin fragility caused by a lack of collagen), suggesting that its homologues,
ADAMTS3 and ADAMTS14, compensate for its loss in tissues other than skin. Now,
by studying the temporal and spatial expression of these proteases and their
procollagen substrates during mouse embryogenesis, Le Goff and co-workers show
that these closely related proteins have distinct biological roles because of
different tissue-specific expression patterns (see p.
1587). For example,
the expression pattern of Adamts3 identifies it as the major
procollagen I and II aminopropeptidase during development, and studies of
Adamts2-null mice reveal that ADAMTS2 is the predominant procollagen
III-processing enzyme in mice. Other results confirm that dermatosparaxis
occurs in Adamts2-null mice because neither ADAMTS3 nor ADAMTS14 is
significantly expressed in adult mouse skin.
Related articles in Development:
- Regulation of procollagen amino-propeptide processing during mouse embryogenesis by specialization of homologous ADAMTS proteases: insights on collagen biosynthesis and dermatosparaxis
- Carine Le Goff, Robert P. T. Somerville, Frederic Kesteloot, Kimerly Powell, David E. Birk, Alain C. Colige, and Suneel S. Apte
Development 2006 133: 1587-1596.
[Abstract]
[Full Text]
