In vivo expression of mRNA for the Ca++-binding protein SPARC (osteonectin) revealed by in situ hybridization.

Holland, Peter W.H.; Harper, SJ; McVey, John H.; Hogan, Brigid L.M.

doi:10.1083/jcb.105.1.473

Cited by 284 publications

(172 citation statements)

References 27 publications

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“…In contrast to the pattern of 2ar expression, SPARC transcripts are detected in virtually all of the tissues examined, the relative levels corresponding to those already reported (Mason et al, 1986b;Holland et al, 1987). In particular, they can be seen clearly in quiescent fibroblasts, and exhibit only modest, if any, increases after growth factor stimulation ( Fig.…”

Section: Northern Analysis Of 2ar Expression In Embryonic Rnamentioning

confidence: 56%

“…The filters were then rehybridized with a probe for SPARC, an acidic phosphorylated Ca++-binding glycoprotein identical to osteonectin (Mason et al, 1986a, b;Engel et al, 1987;Holland et al, 1987). In contrast to the pattern of 2ar expression, SPARC transcripts are detected in virtually all of the tissues examined, the relative levels corresponding to those already reported (Mason et al, 1986b;Holland et al, 1987).…”

Section: Northern Analysis Of 2ar Expression In Embryonic Rnamentioning

confidence: 99%

“…Hybridization conditions were essentially as described (Ingham et al, 1985;Hogan et al, 1986;Holland et al, 1987). After hybridization, washing conditions were also as described except that the RNase A treatment was with 5 lxg/ml RNase A at 37"C for 90 rain.…”

Section: In Situ Hybridizationmentioning

confidence: 99%

“…Embryo and adult organs were fixed in 4% paraformaldehyde in PBS, pH 7.4, at 4"C for 16 h, dehydrated, and embedded in paraffin wax (Fibrowax pastillated, Raymond lamb formulation). Sections of 6 ttm were transferred to polylysine-coated slides and heated at 40"C for 2 h. Slides were stored dessicated at 4~ for up to 6 w. For in situ hybridization, slides were treated essentially as described by Hafen et al (1983) with modifications suggested by Ingham et al (1985). A 984-bp Hind III fragmem of 2ar was subeloned into pGEMI and pGEM2 (Promnga Biotec, Madison, Wl).…”

Section: In Situ Hybridizationmentioning

confidence: 99%

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Developmental expression of 2ar (osteopontin) and SPARC (osteonectin) RNA as revealed by in situ hybridization

Nomura¹,

Wills²,

Edwards³

et al. 1988

The Journal of Cell Biology

492

244

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Abstract. 2ar has been identified as a gene inducible by tumor promoters and growth factors in a variety of cultured mouse cell lines (Smith, J. H., and D. T. Denhardt. 1987. J. Cell. Biochem. 34:13-22 262:2900-3907.). In this paper we use Northern blot analysis and in situ hybridization to localize expression of 2ar during mouse embryogenesis. 2ar RNA is first detected in developing limb bones and calvaria at 14.5 d p.c., in a population of cells distinct from those expressing SPARC (osteonectin). High levels of 2ar expression are also seen in the bone marrow-derived granulated metrial gland cells of the deciduum and placenta, and in a number of epithelial tissues, including embryonic and postnatal kidney tubules, uterine epithelium and sensory epithelium of the embryonic ear. The temporal and spatial pattern of 2ar expression seen in vivo suggests that the protein plays a wider role than previously realized, in processes which are not confined to bone development.

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Section: Northern Analysis Of 2ar Expression In Embryonic Rnamentioning

confidence: 56%

Section: Northern Analysis Of 2ar Expression In Embryonic Rnamentioning

confidence: 99%

Section: In Situ Hybridizationmentioning

confidence: 99%

Section: In Situ Hybridizationmentioning

confidence: 99%

See 2 more Smart Citations

Developmental expression of 2ar (osteopontin) and SPARC (osteonectin) RNA as revealed by in situ hybridization

Nomura¹,

Wills²,

Edwards³

et al. 1988

The Journal of Cell Biology

492

244

View full text Add to dashboard Cite

show abstract

“…SPARC is highly expressed during embryogenesis and is restricted in the adult to tissues undergoing remodeling, repair, and tumorigenesis (Holland et al, 1987;Sage et al, 1989a;Bradshaw and Sage, 2001;Framson and Sage, 2004). SPARC is a multifunctional protein that regulates extracellular matrix (ECM) organization and cell-ECM interactions, leading to the modulation of cell adhesion and migration, promotion of cell survival, and inhibition of cell proliferation (Brekken and Sage, 2000).…”

Section: Introductionmentioning

confidence: 99%

SPARC is expressed by macroglia and microglia in the developing and mature nervous system

Vincent

Lau

Roskams

2008

Developmental Dynamics

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SPARC (secreted protein, acidic and rich in cysteine) is a matricellular protein that is highly expressed during development, tissue remodeling, and repair. SPARC produced by olfactory ensheathing cells (OECs) can promote axon sprouting in vitro and in vivo. Here, we show that in the developing nervous system of the mouse, SPARC is expressed by radial glia, blood vessels, and other pial-derived structures during embryogenesis and postnatal development. The rostral migratory stream contains SPARC that becomes progressively restricted to the SVZ in adulthood. In the adult CNS, SPARC is enriched in specialized radial glial derivatives (Mü ller and Bergmann glia), microglia, and brainstem astrocytes. The peripheral glia, Schwann cells, and OECs express SPARC throughout development and in maturity, although it appears to be down-regulated with maturation. These data suggest that SPARC may be expressed by glia in a spatiotemporal manner consistent with a role in cell migration, neurogenesis, synaptic plasticity, and angiogenesis.

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Type I collagen-deficient Mov-13 mice do not retain SPARC in the extracellular matrix: Implications for fibroblast function

Iruela‐Arispe

Vernon

et al. 1996

Dev. Dyn.

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The Mou-13 strain of mice was created by the insertion of the murine Moloney leukemia virus into the first intron of the d (1) collagen gene. Consequently, Mou-13 embryos do not transcribe a1 (I) collagen mRNA and lack type I collagen protein in the extracellular matrix (ECM). Homozygotes die within 12-14 days of embryonic development, in part from the rupture of large blood vessels, and also exhibit deficiencies in hematopoesis and assembly of the ECM (Liihler et al. [ 19841 Cell 385974307). Several matricellular proteins, proteoglycans, and growth factors bind to type I collagen, e.g., fibronectin, secreted protein acidic and rich in cysteine (SPARC), decorin, and transforming growth factor+. Here we investigate the expression and function of SPARC in the absence of type I collagen. We show that fibroblasts isolated from Mou-13 homozygous, heterozygous, and wild-type embryos transcribed and translated SPARC mRNA in vitro. However, accumulation of extracellular SPARC was severely affected in the tissues of Mou-13 homozygotes, whereas extracellular deposition of the secreted glycoproteins fibronectin and type I11 collagen was not altered. Since SPARC has been shown to be a regulator of cell shape, the functional consequences of the absence of extracellular SPARC were evaluated in collagen gel contraction assays. Fibroblasts isolated from homozygous Mou-13 mice did not contract native type I collagen gels as efficiently as fibroblasts from heterozygous littermates; however, addition of exogenous SPARC enhanced the contraction of collagen by homozygous Mou-13 fibroblasts. The stirnulatory effect of SPARC was blocked by antibodies specific for the amino terminus of the protein. These results provide evidence that type I collagen is one of the major extracellular proteins that binds SPARC in vivo. Furthermore, the capacity of fibroblasts to contract ECM in vitro is enhanced by extracellular SPARC. W e therefore propose that the remodeling of ECM by cells in vivo is regulated in part by a specific interaction between SPARC and type I collagen. D IPPB Wiey-Liss, Inc.

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In vivo expression of mRNA for the Ca++-binding protein SPARC (osteonectin) revealed by in situ hybridization.

Cited by 284 publications

References 27 publications

Developmental expression of 2ar (osteopontin) and SPARC (osteonectin) RNA as revealed by in situ hybridization

Developmental expression of 2ar (osteopontin) and SPARC (osteonectin) RNA as revealed by in situ hybridization

SPARC is expressed by macroglia and microglia in the developing and mature nervous system

Type I collagen-deficient Mov-13 mice do not retain SPARC in the extracellular matrix: Implications for fibroblast function

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