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Hepatic SPARC expression is associated with liver injury and fibrogenic processes in non-alcoholic fatty liver disease.
Plasma samples from lung cancer patients and healthy heavy-smokers controls were tested for levels of COL11A1 (Montrer COL11A1 Protéines) and COL10A1 (Montrer COL10A1 Protéines) (n = 57 each) and SPARC (n = 90 each). Higher plasma levels of COL10A1 (Montrer COL10A1 Protéines) were detected in patients (p = 0.001), a difference that was driven specifically by females (p < 0.001). No difference in COL11A1 (Montrer COL11A1 Protéines) levels between patients and controls was found
The authors have confirmed the presence of SPARC expression in melanoma, Kaposi sarcomas (KS), leiomyosarcomas (LMS) and angiosarcomas (AS) and also detected it for the first time in atypical fibroxanthomas (AFX (Montrer FOXO4 Protéines)).
Results revealed that hypermethylation of the SPARC promoter was the primary mechanism of SPARC downregulation in prostate cancer. SPARC expression was frequently lost during the promoter hypermethylation but could be restored by 5-Aza-Cdr (Montrer RUNX1T1 Protéines).
Stromal SPARC expression was a useful biomarker for predicting prognosis in patients with resected pancreatic ductal adenocarcinoma.
SPARC is closely related to the development of breast cancer and can be used as a tumor marker for breast cancer recurrence.
SPARC expression was inversely associated with the degree of malignancy and it had a negative correlation with VEGF-C (Montrer VEGFC Protéines) and VEGF-D (Montrer Figf Protéines) expression. Results suggest SPARC might function as a tumor suppressor inhibiting angiogenesis and lymphangiogenesis in ovarian cancer by reducing the expression of VEGF-C (Montrer VEGFC Protéines) and VEGF-D (Montrer Figf Protéines).
SPARC may be involved in gastric cancer metastasis by effecting on tumor microenvironment
SPARC treatment enhances the epithelial mesenchymal transition signaling pathway via activation of AKT (Montrer AKT1 Protéines), and exogenous SPARC and tumor expressing SPARC might be associated with tumor progression in head and neck cancers.
The epicardial adipose tissue expresses the mRNA of osteopontin (Montrer SPP1 Protéines), osteoprotegerin (Montrer TNFRSF11B Protéines), and osteonectin genes that have been implicated in the calcification process; such expression is statistically associated with some components of HDL (Montrer HSD11B1 Protéines) subclasses in coronary artery disease patients.
Sparc levels in tendons are critical for proper collagen fibril maturation.
miR (Montrer MLXIP Protéines)-29 directly targeted SPARC, resulting in degradation of SPARC-encoding mRNA and reduction in the SPARC protein level.
SPARC plays a crucial role in the proliferation and differentiation of C2C12 and may be involved in the link between the ECM (Montrer MMRN1 Protéines) remodeling and mitochondrial func
SPARC is regulating the interplay between myeloid-derived suppressor cells and the extracellular matrix to drive the induction of epithelial-to-mesenchymal transition in tumor cells.
The results demonstrate for the first time a functional role of the N-propeptide in regulating collagen fiber assembly and cell behavior and suggest that SPARC and the N-propeptide of collagen I have distinct activities in regulating collagen fiber assembly and fibroblast function.
SPARC plays a key role in influencing the spatial organization of the anterior segment, potentially via modulation of collagen properties, while Hevin is not likely to be involved.
An ADAMTS1 (Montrer ADAMTS1 Protéines) blocking antibody suppressed the SPARC-induced collagen I secretion, indicating that SPARC promoted collagen production directly through ADAMTS1 (Montrer ADAMTS1 Protéines) interaction. In conclusion, ADAMTS1 (Montrer ADAMTS1 Protéines) is an important mediator of SPARC-regulated cardiac aging.
SPARC appears to be an important modulator of the actin cytoskeleton, implicating maintenance of muscular function
resistivity measurements were taken on 22 mice, 11 wild-type and 11 sparc-/- (knock out for the protein SPARC: secreted protein acidic and rich in cysteine), bearing mammary carcinomas.
SPARC isoforms, acting on Adipose stromal cells through distinct mechanisms, have an additive effect in inducing ASC (Montrer STS Protéines) migration.
findings indicate that secreted protein acidic cysteine-rich (SPARC) is intricately regulated by pro-angiogenic and other growth factors together with components of the extracellular matrix during the follicle-luteal transition
This study reports the temporal changes in vascular endothelial growth factor A (VEGFA (Montrer VEGFA Protéines)), fibroblast growth factor 2 (FGF2 (Montrer FGF2 Protéines)) and osteonectin during the follicular-luteal transition and corpus luteum development in the cow.
these data identify a contributory role for DNA methylation (Montrer HELLS Protéines) in regulating sparc expression in zebrafish embryogenesis.
Results establish a role for an ECM (Montrer MMRN1 Protéines) protein (Sparc) as an important regulator of embryonic haematopoiesis during early development in zebrafish.
Data show that Sparc (Osteonectin) functions in morphogenesis of the pharyngeal skeleton and inner ear in zebrafish.
Sparc is directly required for normal otolith growth
data suggest that SPARC might modulate angiogenesis during wound healing in the horse, which could protect against the disproportionate fibroplasia commonly afflicting limb wounds and leading to the development of exuberant granulation tissue
Data suggest a critical requirement for SPARC during post-gastrula development in Xenopus embryos and that SPARC, directly or indirectly, promotes cell-cell adhesion in vivo.
This gene encodes a cysteine-rich acidic matrix-associated protein. The encoded protein is required for the collagen in bone to become calcified but is also involved in extracellular matrix synthesis and promotion of changes to cell shape. The gene product has been associated with tumor suppression but has also been correlated with metastasis based on changes to cell shape which can promote tumor cell invasion.
, basement-membrane protein 40
, cysteine-rich protein
, secreted protein acidic and rich in cysteine
, Secreted acidic cystein-rich glycoprotein (osteonectin)
, secreted acidic cysteine rich glycoprotein
, secreted protein, acidic, cysteine-rich (osteonectin) S homeolog
, secreted protein, acidic, cysteine-rich (osteonectin)