Although microglia are derived from the same haemopoietic lineage as macrophages, we did not detect SPARC in macrophages in any embryonic or postnatal organ.
SPARC can similarly be cleaved by proteases and MMPs to yield peptides with distinct functions (Lane et al.,1994; Iruela‐Arispe et al.,1995; Sasaki et al.,1997), and can also regulate protease expression and activation (Brekken and Sage,2000; McClung et al.,2007).
Indeed, Bergmann glia in the cerebellum and Müller glia in the retina express SPARC in the adult brain (Fig. Enter your email address below and we will send you your username, If the address matches an existing account you will receive an email with instructions to retrieve your username, I have read and accept the Wiley Online Library Terms and Conditions of Use, Tenascin‐R is antiadhesive for activated microglia that induce downregulation of the protein after peripheral nerve injury: a new role in neuronal protection, Radial glia serve as neuronal progenitors in all regions of the central nervous system, SPARC from olfactory ensheathing cells stimulates Schwann cells to promote neurite outgrowth and enhances spinal cord repair, Osteonectin is a Schwann cell‐secreted factor that promotes retinal ganglion cell survival and process outgrowth, SPARC regulates extracellular matrix organization through its modulation of integrin‐linked kinase activity, Matricellular homologs in the foreign body response: hevin suppresses inflammation, but hevin and SPARC together diminish angiogenesis, Impaired wound healing in mice deficient in a matricellular protein SPARC (osteonectin, BM‐40), FAK deficiency in cells contributing to the basal lamina results in cortical abnormalities resembling congenital muscular dystrophies, SPARC, a matricellular protein that functions in cellular differentiation and tissue response to injury, SPARC‐null mice exhibit accelerated cutaneous wound closure, SPARC‐null mice exhibit increased adiposity without significant differences in overall body weight, SPARC‐null mice display abnormalities in the dermis characterized by decreased collagen fibril diameter and reduced tensile strength, SPARC, a matricellular protein: at the crossroads of cell‐matrix communication, Cellular and molecular mechanisms of neural repair after stroke: making waves, Osteonectin/SPARC is a product of articular chondrocytes/cartilage and is regulated by cytokines and growth factors, SPARC is a key Schwannian‐derived inhibitor controlling neuroblastoma tumor angiogenesis, Basal lamina: Schwann cells wrap to the rhythm of space‐time, ATP mediates rapid microglial response to local brain injury in vivo, Microglial activation and matrix protease generation during focal cerebral ischemia, Basic fibroblast growth factor destabilizes osteonectin mRNA in osteoblasts, Osteopenia and decreased bone formation in osteonectin‐deficient mice, Subventricular zone astrocytes are neural stem cells in the adult mammalian brain, Identification of SparcL1/Hevin as an astrocyte secreted protein that promotes central nervous system synapse formation, Imaging neuronal subsets in transgenic mice expressing multiple spectral variants of GFP, Brain lipid‐binding protein (BLBP): a novel signaling system in the developing mammalian CNS, Importance of the basement membrane protein SPARC for viability and fertility in Caenorhabditis elegans.
Furthermore, SPARC is concentrated at brain flexures in the embryonic brain (Fig.
SPARC is maintained at a low level in the adult subventricular zone (SVZ; Fig. Concomitantly, astrocytes in the brainstem begin to express SPARC in their endfeet surrounding blood vessels (part of the blood‐brain barrier), and this is maintained in the adult (Fig.
This may also explain why oligodendrocytes, whose myelin does not have a basal lamina, do not express SPARC. A–C: Allen Brain Atlas images of SPARC mRNA expression in the adult mouse brain (boxes represent the positions of D,E,I,K, and vertical lines represent the positions of coronal sections in B,C,F–H). As a highly conserved basement membrane molecule (Fitzgerald and Schwarzbauer,1998; Bradshaw and Sage,2001; Martinek et al.,2002), SPARC may be involved in the assembly and maintenance of fractones by regulating the production of ECM molecules such as laminin (Kamihagi et al.,1994; Weaver et al.,2006) and collagen (Francki et al.,1999; Bradshaw et al.,2003b). K–M: SPARC is expressed by (K,M) microglia (Iba‐1+, arrow in M) in the olfactory bulb (OB), but not by (K,L) macrophages (Iba‐1+, arrow in L) in the olfactory nerve (ON). ), and the Canadian Institutes of Health Research (to J.R.). During postnatal development, SPARC may facilitate neuronal migration along the RMS, which contains SPARC during the peak of postnatal interneuron migration to the olfactory bulb (Fig.
3C).
R, rhombencephalon; DI, diencephalon; TEL, telencephalon; MZ, marginal zone; olf. SPARC negatively regulates signaling by various growth factors known to be involved in neural stem cell proliferation and differentiation, including fibroblast growth factor 2 (FGF2) (Motamed et al.,2003), epidermal growth factor (EGF) (Said et al.,2007a), insulin‐like growth factor‐1 (IGF‐1) (Francki et al.,2003), and transforming growth factor β (TGFβ) (Schiemann et al.,2003; Francki et al.,2004). pit, olfactory pit; D, dorsal; V, ventral; A, anterior; P, posterior. 4C–E; nestin‐positive, Fig. SPARC is expressed by (C,E–H) nestin+ radial glia, in their cell bodies (bracket in F) and processes (inset in C, arrow in F), and overlaps with regions of (A,B,I–K) BLBP+ radial glia (arrows). This suggests that SPARC may have multifunctional roles as a modulator of cell migration, cytoarchitecture, neurogenesis, angiogenesis, and peripheral myelination, and could be an important modulator of integrative growth factor and ECM signaling in neural development and regeneration.
In contrast, astrocytes in more anterior structures express little or no SPARC, such as in the striatum and lateral septal nuclei (Fig.
The novel SPARC family member SMOC‐2 potentiates angiogenic growth factor activity, Regulation of interactions between cells and extracellular matrix: a command performance on several stages, Distribution of the calcium‐binding protein SPARC in tissues of embryonic and adult mice, SPARC, a secreted protein associated with cellular proliferation, inhibits cell spreading in vitro and exhibits Ca+2‐dependent binding to the extracellular matrix, Secreted protein acidic and rich in cysteine (SPARC) inhibits integrin‐mediated adhesion and growth factor‐dependent survival signaling in ovarian cancer, Normalization of the Ovarian Cancer Microenvironment by SPARC, Limited cleavage of extracellular matrix protein BM‐40 by matrix metalloproteinases increases its affinity for collagens, SPARC inhibits epithelial cell proliferation in part through stimulation of the transforming growth factor‐beta‐signaling system, Secreted protein acidic, rich in cysteine (SPARC), mediates cellular survival of gliomas through AKT activation, Targeting SPARC expression decreases glioma cellular survival and invasion associated with reduced activities of FAK and ILK kinases, Differential effects of various growth factors and cytokines on the syntheses of DNA, type I collagen, laminin, fibronectin, osteonectin/secreted protein, acidic and rich in cysteine (SPARC), and alkaline phosphatase by human pulp cells in culture, Transforming growth factor‐beta1 and basic fibroblast growth factor modulate osteocalcin and osteonectin/SPARC syntheses in vitamin‐D‐activated pulp cells, Ultrastructural study of ensheathing cells in early development of olfactory axons, Targeting angiogenesis inhibits tumor infiltration and expression of the pro‐invasive protein SPARC, Absence of SPARC in lens epithelial cells results in altered adhesion and extracellular matrix production in vitro, Regulation of the expression of a secreted acidic protein rich in cysteine (SPARC) in human fibroblasts by transforming growth factor beta.
Ependymal cells form a part of the neural stem cell niche (Doetsch et al.,1999) that suppresses gliogenesis in favor of neurogenesis (Lim et al.,2000). 5F–H), and in the grey matter of the spinal cord (Fig. These detailed cellular SPARC expression erns are largely in accord with low‐power in situ hybridization or immunohistochemistry for SPARC in the developing rodent (Mendis and Brown,1994; Mendis et al.,1995; Mothe and Brown,2001). 2B,G).
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