Evidence from molecular cloning that SPARC, a major product of mouse embryo parietal endoderm, is related to an endothelial cell ‘culture shock’ glycoprotein of Mr 43,000.

Mason, Ivor; Taylor, Amanda; Williams, Jeffrey; Sage, Helene; Hogan, Brigid L.M.

doi:10.1002/j.1460-2075.1986.tb04383.x

Cited by 297 publications

(163 citation statements)

References 38 publications

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“…The protein seems to be instrumental in cellular growth by its interactions with cytokines, and the extracellular matrix and has been found to mainly be expressed in cells that are experiencing morphogenesis. 8,9 The stringent rinsing technique developed in this paper can be used in the future to identify more proteins of interest secreted from endothelial cells and could even be used to compare the difference in the secretome from healthy and diseased endothelial cell states. Percentage of BSA scans versus total scans identified by mass spectrometry.…”

Section: Discussionmentioning

confidence: 99%

Improved Mass Spectrometric Proteomic Profiling of the Secretome of Rat Vascular Endothelial Cells

et al. 2006

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Serum albumin contamination of cells cultured in vitro significantly impedes the mass spectrometric analysis of proteins secreted by the cells. Here we report a novel washing and culturing technique for rat vascular endothelial cells that considerably reduces the concentration of the commonly used additive for cell culture, bovine serum albumin (BSA), in the secretome of these cells. Cells are rinsed stringently and cultured for 24 h in serum-free media without appreciably impeding cell growth or viability. The percentage of BSA scans identified by tandem mass spectrometry (LC-MS/MS) in stringently rinsed cells (average 13.2%) was significantly lower than either the moderately rinsed or no rinse cell treatments (average 35.2% and 45.2% respectively). Furthermore, the stringent wash treatment allowed the confident identification of a larger portion of the secretome of rat endothelial cells by LC-MS/MS.

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Section: Discussionmentioning

confidence: 99%

Improved Mass Spectrometric Proteomic Profiling of the Secretome of Rat Vascular Endothelial Cells

et al. 2006

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“…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: 98%

“…The following mouse eDNA probes were used: 2ar (Smith and Denhardt, 1987), SPARC (Mason et al, 1986a) and routine glyceratdehyde 3-phosphate dehydrogenase obtained from Dr. P. Curtis (Wistar Institute, Philadelphia, PA). The 2at eDNA probe was 1226-bp long, covering the entire 3" noncoding region and ,~90% of the protein coding region, as judged by alignment to the sequence of rat osteopontin (Oldberg et al, 1986;Denhardt et al, 1988).…”

Section: Growth Factors and Dna Probesmentioning

confidence: 99%

“…They have been assumed to be osteoblasts or osteoblast precursors (Termine et al, 1985;Holland et al, 1987). However, SPARC is known to be expressed at high levels by aortic endothelial cells (Mason et al, 1986a), and the possibility that the positive cells in the periosteum, and later also the endosteum, are members of the endothelial lineage cannot be excluded. Fig.…”

Section: Ar and Sparc Expression During Embryonic Bone Developmentmentioning

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

490

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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“…Full-length mouse SPARC cDNA (Mason et al 1986) was subcloned, in both orientations, into the Pst 1 site of pGEM 4Z. Orientation was determined using restriction enzyme analysis.…”

Section: Sparc Rna and Proteinmentioning

confidence: 99%

Ectopic Expression of SPARC inXenopusEmbryos Interferes with Tissue Morphogenesis: Identification of a Bioactive Sequence in the C-terminal EF Hand

Damjanovski

Karp

Funk

et al. 1997

J Histochem Cytochem.

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SUMMARY SPARC is a matricellular Ca 2 ϩ -binding glycoprotein that exhibits both counteradhesive and antiproliferative effects on cultured cells. It is secreted by cells of various tissues as a consequence of morphogenesis, response to injury, and cyclic renewal and/or repair. In an earlier study with Xenopus embryos we had shown a highly specific and regulated pattern of SPARC expression. We now show that ectopic expression of SPARC before its normal embryonic activation produces severe anomalies, some of which are consistent with the functions of SPARC proposed from studies in vitro. Microinjection of SPARC RNA, protein, and peptides into Xenopus embryos before endogenous embryonic expression generated different but overlapping phenotypes. (a) Injection of SPARC RNA into one cell of a two-cell embryo resulted in a range of unilateral defects. (b) Precocious exposure of embryos to SPARC by microinjection of protein into the blastocoel cavity was associated with certain axial defects comparable to those obtained with SPARC RNA. (c) SPARC peptides containing follistatin-like and copper-binding sequences were without obvious effect, whereas SPARC peptide 4.2, corresponding to a disulfide-bonded, Ca 2 ϩ -binding domain, was associated with a reduction in axial structures that led eventually to complete ventralization of the embryos. Histological analysis of ventralized embryos indicated that the morphogenetic events associated with gastrulation might have been inhibited. Microinjection of other Ca 2 ϩ -binding glycoproteins, such as osteopontin and bone sialoprotein, resulted in phenotypes that were unique. We probed further the structural correlates of this region of SPARC in the context of tissue development. Co-injection of peptide 4.2 with Ca 2 ϩ or EGTA, and injection of peptide 4.2K (containing a mutated consensus Ca 2 ϩ -binding sequence), demonstrated that the developmental defects associated with peptide 4.2 were independent of Ca 2 ϩ . However, the disulfide bridge in this region of SPARC was found to be critical, as injection of peptide 4.2AA, a mutant lacking the cystine, generated no axial defects. We have therefore shown for the first time in vivo that the temporally inappropriate presence of SPARC is associated with perturbations in tissue morphogenesis. Moreover, we have identified at least one bioactive region of SPARC as the C-terminal disulfide-bonded, Ca 2 ϩ -binding loop that was previously shown to be both counteradhesive and growth-inhibitory. (J Histochem Cytochem 45:643-655, 1997) E xtracellular matrix glycoproteins make major morphoregulatory contributions to early embryonic development. Their complex, transient expression patterns, structural heterogeneity, and functional diversity indicate important roles in the modulation of a broad spectrum of cellular activities, such as adhesion, migration, communication, and/or proliferation. For example, the blastocoel roof of amphibian embryos is coated with an elaborate network of fibronectin fibers before the involution of mesodermal cells durin...

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Evidence from molecular cloning that SPARC, a major product of mouse embryo parietal endoderm, is related to an endothelial cell ‘culture shock’ glycoprotein of Mr 43,000.

Cited by 297 publications

References 38 publications

Improved Mass Spectrometric Proteomic Profiling of the Secretome of Rat Vascular Endothelial Cells

Improved Mass Spectrometric Proteomic Profiling of the Secretome of Rat Vascular Endothelial Cells

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

Ectopic Expression of SPARC inXenopusEmbryos Interferes with Tissue Morphogenesis: Identification of a Bioactive Sequence in the C-terminal EF Hand

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