SPARC protein

Bone SPARC protein (osteonectin) Not bone-specific. 

CS-PG, chondroitin sulfate-proteoglycan these are similar to the dermatan sulfate PGs (DS-PGs) of cartilage ffable 48-11). SPARC, secreted protein acidic and rich in cysteine. 

Vajkoczy P, Menger MD, Goldbrunner R et al (2000) Targeting angiogenesis inhibits tumor infiltration and expression of the pro-invasive protein SPARC. Int J Cancer 87 261-268... 

SPARC (Secreted Protein Acidic and Rich in Cysteine), 46 484-485 Specific activity method, of isotope half-life determination, 2 326-327 Specific interaction theory, application, 43 19-21... 

The possible involvement of kallikreins in brain tumors has been examined recently. A recent report showed expression of the hK6 protein by glioblastoma cells implanted intracranially in nude mice. Moreover, hK6 expression was shown to colocalize with the expression of an invasion-associated matri-cellular protein called SPARC [248]. Given the high level of expression of some kallikreins in the brain, it is logical to speculate a possible involvement of kallikrein in brain tumors. Ongoing studies are now being conducted to evaluate the possible functional importance of kallikreins in brain tumor invasiveness [248]. 

Puolakkainen P, Bradshaw AD, Kyriakides TR, Reed M, Brekken R, Wight T, Bomstein P, Ratner B, Sage EH. Compromised production of extracellular matrix in mice lacking secreted protein, acidic and rich in cysteine (SPARC) leads to a reduced foreign body reaction to implanted biomaterials. American Journal of Pathology 2003,162, 627-635. 

Complete sequence analysis based on cDNA was achieved for osteonectin and SPARC and indicated a disulfide-bonded, four-domain structure for the protein (Fig. 12). Remarkable features of the structure are a cluster of 16 glutamic acid residues at the N terminus and an EF-hand domain located between the last two cysteine residues, both regions having the potential for calcium-binding (Bolander et al., 1988 Engel et al., 1987). Studies with BM-40 demonstrated a reversible change in a helix from 30 to 20% upon removal of calcium. The data indicate the... 

Fig. 12. Predicted domain structure of the small calcium-binding protein BM-40/os-teonectin/SPARC. Numbering is according to the sequence of SPARC (Mason et al., 1986a), but omits the signal peptide. A dashed line denotes predicted a helix, C identifies cysteine residues, and + indicates clusters of basic residues. A potential calcium-binding domain of the EF type is noted as well as a cluster of glutamic acids. Modified from Engel et al. (1987).

NOESY was performed at 32 °C on a VXR-500 spectrometer operating at a proton frequency of 500 MHz. The protein was dissolved in 20 mM sodium phosphate, pH 7.5 (direct pH meter reading), 100 mM NaCl, 5 mM DTT in D2O. The protein concentration was 2 mM. The data was acquired in the hypercomplex mode with a mixing time of 150 ms (Jeener et al., 1979 Macura Ernst,1980). The spectral width was 7200 Hz in both dimensions. 2048 complex points in the t2 dimension and 256 complex points in the tl dimension were acquired. 96 transients were collected for each FID. Data processing was performed on a Sun Sparc 10 station using VNMR software from Varian. The time domain data were zero-filled once and multiplied by shifted sinebell or Gaussian functions before Fourier transformation in both dimensions. Chemical shifts were referenced to internal sodium 3-(trimethylsilyl)-propionate-2,2,3,3-d4. 

Multiple sclerosis Cartilage acidic protein, tetranectin, SPARC-like protein, autotaxin t 2D SDS-PAGE and LC -MS/MS (Hammack et al., 2004)... 

Kamihagi K, Katayama M, Ouchi R, et al. Osteonectin/SPARC regulates cellular secretion rates of fibronectin and laminin extracellular matrix proteins. Biochem Biophys Res Commun. 1994 200 423-428. 

Anti-adhesive molecules affect cell adhesion by changing the arrangement of cytoskeletal proteins and by altering signaling cascades. Specifically, tenascin-C, TSP-1, and SPARC all downregulate the actin stress fiber system and disrupt focal adhesions when added in solution to spread cells (Murphy-Ullrich, 2001 Orend and Chiquet-Ehrismann, 2000). Reorganization of the actin cytoskeleton is a major pathway by which... 

Bleomycin (0.15 U/mouse) given intratracheally induced significantly more pulmonary fibrosis in mice deficient in SPARC (secreted protein, acidic and rich in cysteine) compared with that in wild-type control mice, with the mutant mice demonstrating greater neutrophil accumulation in the lungs (Savani et al. 2000). However, in wild-type and SPARC-deficient mice given intraperitoneal bleomycin (0.8 U/injectionx 5 injections over 14 days), the pattern and severity of pulmonary fibrosis, as well as the levels of leucocyte recruitment, were similar in both strains of mice. 

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