描述：
Human WISP-1 (Wnt-induced secreted protein-1; also CNN4) is a 40 kDa, secreted,
heparinbinding glycoprotein that is a member of the CCN (or CTGF/Cyr61/Nov) cysteine-rich
protein family. It is synthesized as a 367 aa precursor that contains a series of structural
homology modules. Following a 22 amino acid (aa) signal sequence, there is a 68 aa
IGFBP-like domain (aa 53-120), a 57 aa von Willebrand factor type C (VWC) module
(aa 126-182), a 40 aa TSP type I domain (aa 220-259) and a 75 aa, C-terminal cysteine
knot motif (aa 273-347). The VWC module is associated with proteinprotein interaction,
the TSP domain binds sulfated glycoconjugates, and the cysteine knot mediates dimerization
and receptor binding.It is likely that WISP-1 normally circulates as an 80 kDa homodimer.
At least five alternative splice forms are known for WISP-1. One is 30 kDa in size, 258 aa in
length, and shows a substitution of a His for aa 95-182. This removes the VWC domain.
A second isoform is 155 aa in length and shows a frameshift at Arg 117 with a unique 38
aa C-terminal extension. A third is 195 aa in length and shows a 31 aa substitution for the
first 203 aa of the full length precursor. This retains the VWC and cysteine knot domains.
A fourth shows a 43 aa substitution for aa 117-367 for a total length of 163 aa. This effectively
removes everything but the IGFBP-like domain. The last splice form contains a deletion
of aa 25-269 for a total length of 122 aa. Thus, only the signal sequence and cysteine knot
motifs are retained. This leaves only the IGFBP-like domain. Fulllength mature human WISP-1
is 85% aa identical to both mouse and rat WISP-1. WISP-1 is expressed by osteoblasts and
may contribute to fracture healing by promoting bone cell formation.
原厂资料：
Human WISP-1 (Wnt-induced secreted protein-1; also CNN4) is a 40 kDa, secreted,
heparinbinding glycoprotein that is a member of the CCN (or CTGF/Cyr61/Nov) cysteine-rich
protein family. It is synthesized as a 367 aa precursor that contains a series of structural
homology modules. Following a 22 amino acid (aa) signal sequence, there is a 68 aa
IGFBP-like domain (aa 53-120), a 57 aa von Willebrand factor type C (VWC) module
(aa 126-182), a 40 aa TSP type I domain (aa 220-259) and a 75 aa, C-terminal cysteine
knot motif (aa 273-347). The VWC module is associated with proteinprotein interaction,
the TSP domain binds sulfated glycoconjugates, and the cysteine knot mediates dimerization
and receptor binding.It is likely that WISP-1 normally circulates as an 80 kDa homodimer.
At least five alternative splice forms are known for WISP-1. One is 30 kDa in size, 258 aa in
length, and shows a substitution of a His for aa 95-182. This removes the VWC domain.
A second isoform is 155 aa in length and shows a frameshift at Arg 117 with a unique 38
aa C-terminal extension. A third is 195 aa in length and shows a 31 aa substitution for the
first 203 aa of the full length precursor. This retains the VWC and cysteine knot domains.
A fourth shows a 43 aa substitution for aa 117-367 for a total length of 163 aa. This effectively
removes everything but the IGFBP-like domain. The last splice form contains a deletion
of aa 25-269 for a total length of 122 aa. Thus, only the signal sequence and cysteine knot
motifs are retained. This leaves only the IGFBP-like domain. Fulllength mature human WISP-1
is 85% aa identical to both mouse and rat WISP-1. WISP-1 is expressed by osteoblasts and
may contribute to fracture healing by promoting bone cell formation.
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