| Literature References | 1. TROYANOVSKY, B., LEVCHENKO, T., MANSSON, G., MATVIJENKO, O. AND
HOLMGREN, L.
Angiomotin: an angiostatin binding protein that regulates endothelial cell
migration and tube formation.
J.CELL BIOL. 152(6) 1247-1254 (2001).
2. ZETTER, B.R.
Hold that line. Angiomotin regulates endothelial cell motility.
J.CELL BIOL. 152(6) F35-F36 (2001).
3. BRATT, A., WILSON, W.J., TROYANOVSKY, B., AASE, K., KESSLER, R.,
MEIR, E.G. AND HOLMGREN, L.
Angiomotin belongs to a novel protein family with conserved coiled-coil and
PDZ binding domains.
GENE 298(1) 69-77 (2002).
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| Documentation | Angiogenesis, the process whereby new blood vessels are formed by a
mechanism of sprouting from existing vessels, has recently been the subject
of intense research. Angiostatin, a proteolytically generated fragment of
plasminogen consisting of the first four kringle domains, is a potent
angiogenesis inhibitor. Whilst this protein has been known for some time,
until recently its mechanism of action was unknown. A functional angiostatin-
binding protein has been described that inhibits endothelial cell motility
and proliferation, key stages in angiogenesis [1]. This protein has been
named angiomotin.
Angiomotin was identififed via a yeast two-hybrid screen for proteins that
interact with angiostatin. It is a 72kDa cell-surface associated protein
expressed in endothelium and other tissues where angiogenesis occurs, such
as placenta and tumours. It appears that angiomotin stimulates angiogenesis
by increasing cell motility and that binding of angiostatin inhibits this
process [2]. Two paralogues of angiomotin have recently been cloned and
their amino acid sequences determined. Together with angiomotin, these
proteins form a novel family bearing little sequence similarity to other
known proteins. Sequence analysis has revealed putative coiled-coil and
PDZ-binding domains [3].
ANGIOMOTIN is a 7-element fingerprint that provides a signature for the
angiomotin family. The fingerprint was derived from an initial alignment of
4 sequences: the motifs were drawn from conserved regions in the central
portion of the alignment, motifs 1-5 residing in the putative coiled-coil
domain. Two iterations on SPTR40_20f were required to reach convergence, at
which point a true set comprising 6 sequences was identified. A single
partial match was also found, Q9H879, a human cDNA that shares a high degree
of similarity with the coiled-coil domain.
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