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Review
. 2001 May;107(9):1049-54.
doi: 10.1172/JCI12939.

SPARC, a matricellular protein that functions in cellular differentiation and tissue response to injury

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Review

SPARC, a matricellular protein that functions in cellular differentiation and tissue response to injury

A D Bradshaw et al. J Clin Invest. 2001 May.
No abstract available

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Figures

Figure 1
Figure 1
Structure of SPARC protein. A ribbon diagram derived from crystallographic data shows the three modular domains of SPARC. Representative activities attributed to each domain are shown beneath the designated amino acids. The follistatin-like domain contains the peptide 2.1 (see ref. 1) shown in green and the (K)GHK angiogenic peptide (amino acids 114–130) shown in black. The E-C domain contains the amino acids 255–274 (peptide 4.2) shown in yellow. Adapted from Hohenester et al. (29) and the Brookhaven Protein Database (30), accession no. 1BM0 from Ref.1, with permission.
Figure 2
Figure 2
SPARC-null lens epithelial cells display changes in cell shape and alignment in comparison with wild-type cells. Sections from similar areas of wild-type and SPARC-null lens were stained with hematoxylin and eosin. Cortical fibers from a 3-month-old wild-type lens (a) are regular and precisely aligned, whereas those from a SPARC-null lens (b) are irregular in shape and alignment. Magnification, ×220.

References

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    1. Norose K, Lo W-K, Clark JI, Sage EH, Howe CC. Lenses of SPARC-null mice exhibit an abnormal cell surface-basement membrane interface. Exp Eye Res. 2000;71:295–307. - PubMed
    1. Ringuette M, Drysdale T, Liu F. Expression and distribution of SPARC in early Xenopus laevis embryos. Roux’s Archives of Developmental Biology. 1992;202:4–9. - PubMed
    1. Kyriakides TR, et al. Mice that lack thrombospondin 2 display connective tissue abnormalities that are associated with disordered collagen fibrillogenesis, an increased vascular density, and a bleeding diathesis. J Cell Biol. 1998;140:419–430. - PMC - PubMed

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