Expression of NCAM and its polysialylated isoforms during mdx mouse muscle regeneration and in vitro myogenesis

Dubois, C.; Figarella‐Branger, Dominique; Pastoret, Christian; Rampini, C; Karpati, George; Rougon, Geneviève

doi:10.1016/0960-8966(94)90018-3

Cited by 45 publications

(30 citation statements)

References 36 publications

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“…The myogenic origin of the hSCs after isolation was confirmed by immunocytochemical (ICC) staining for NCAM (CD56) and desmin. NCAM is known as a satellite cell marker both in human and mouse muscle (Illa et al 1992;Dubois et al 1994), and desmin is expressed by activated satellite cells (myoblasts) and in myotubes (Creuzet et al 1998;Stewart et al 2003) (data not shown). We observed that SPARC was expressed at both protein and mRNA levels during proliferation and differentiation of hSCs (Figure 2).…”

Section: Sparc In Primary Isolated Human Satellite Cellsmentioning

confidence: 99%

Secreted Protein Acidic and Rich in Cysteine (SPARC) in Human Skeletal Muscle

Jørgensen¹,

Petersson

Sellathurai³

et al. 2008

J Histochem Cytochem.

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S U M M A R Y Secreted protein acidic and rich in cysteine (SPARC)/osteonectin is expressed in different tissues during remodeling and repair, suggesting a function in regeneration. Several gene expression studies indicated that SPARC was expressed in response to muscle damage. Studies on myoblasts further indicated a function of SPARC in skeletal muscle. We therefore found it of interest to study SPARC expression in human skeletal muscle during development and in biopsies from Duchenne and Becker muscular dystrophy and congenital muscular dystrophy, congenital myopathy, inclusion body myositis, and polymyositis patients to analyze SPARC expression in a selected range of inherited and idiopathic muscle wasting diseases. SPARC-positive cells were observed both in fetal and neonatal muscle, and in addition, fetal myofibers were observed to express SPARC at the age of 15-16 weeks. SPARC protein was detected in the majority of analyzed muscle biopsies (23 of 24), mainly in mononuclear cells of which few were pax7 positive. Myotubes and regenerating myofibers also expressed SPARC. The expression-degree seemed to reflect the severity of the lesion. In accordance with these in vivo findings, primary human-derived satellite cells were found to express SPARC both during proliferation and differentiation in vitro. In conclusion, this study shows SPARC expression both during muscle development and in regenerating muscle. The expression is detected both in satellite cells/myoblasts and in myotubes and muscle fibers, indicating a role for SPARC in the skeletal muscle compartment.

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Section: Sparc In Primary Isolated Human Satellite Cellsmentioning

confidence: 99%

Secreted Protein Acidic and Rich in Cysteine (SPARC) in Human Skeletal Muscle

Jørgensen¹,

Petersson

Sellathurai³

et al. 2008

J Histochem Cytochem.

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“…2 We performed immunolabeling with anti-NCAM and anti-neonatal/perinatal/fetal MHC (MHCn), both of which are neurally and developmentally regulated. 1,11,12,20,21,25 The multigene family that encodes MHC is expressed in a developmentally regulated sequence. Developmental isoforms that have been characterized include MHCemb and MHCn.…”

mentioning

confidence: 99%

“…9,18 NCAM is also upregulated in newly formed myofibers. 10,12 Both NCAM and the immature isoforms of MHC are re-expressed after denervation. 9,21 Using these markers, we aimed to clarify whether and to what extent small immature fibers are present in biopsies of patients with neurogenic disease.…”

mentioning

confidence: 99%

Myogenesis in human denervated muscle biopsies

2007

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Electron microscopic studies of long-term denervated rat muscles have identified very small, immature myofibers that are believed to arise from detached satellite cells that have fused to form new fibers within the interstitial space. At present, it is unknown whether and to what extent equivalent fibers exist in denervated human muscle. Serial sections of muscle biopsies from 66 patients diagnosed with polyneuropathy or amyotrophic lateral sclerosis were immunolabeled with anti-NCAM and antineonatal myosin heavy chain monoclonal antibodies that are both neurally and developmentally regulated. We evaluated 200 myofibers in each section. Of the biopsy specimens, 75% contained small myofibers that showed a thin perinuclear cytoplasmic rim. Small fibers expressing neonatal myosin heavy chain (MHCnϩ) were found in all of these biopsies (100%) and NCAMϩ fibers in 98%. The percentage of MHCnϩ small fibers averaged 82% and NCAMϩ small myofibers averaged 40%. The percentage of NCAMϩ small fibers was significantly lower than that of MHCnϩ fibers. In contrast, the percentage of MHCnϩ vs. NCAMϩ angular atrophic fibers did not show a significant difference. A substantial subset of neurogenic biopsies showed small fibers that differ from angular atrophic fibers both in size and expression pattern of MHCn and NCAM. Myogenesis appears to be a frequent finding in neurogenic atrophy.

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“…The extended polySia chains on N-CAM are postulated to prevent the intercellular homophilic binding that usually occurs between N-CAM-expressing cells (reviewed in Edelman, 1985;Rutishauser et al, 1988). As a consequence, highly polysialylated N-CAM is believed to play a central role in neurite fasciculation, neuromuscular interactions, and cell migration (Rosenberg et al, 1986;Rutishauser et al, 1988;Seki and Arai, 1993;Dubois et al, 1994;Tang et al, 1994;Wang et al, 1994), and also in the enhancement of the metastatic potential of certain human cancers (McCoy and Troy, 1987;Roth et al, 1988;Grogan et al, 1994;Scheidegger et al, 1994;Martersteck et al, 1996).…”

Section: Introductionmentioning

confidence: 99%

Developmental expression and characterization of the 2,8-polysialyltransferase activity in embryonic chick brain

Sevigny

Kitazume-Kawaguchi

et al. 1998

Glycobiology

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The α2,8-polysialyltransferases (polySTs) from embryonic chick brain catalyze the α2,8-specific polysialylation of endogenous neural cell adhesion molecules (N-CAMs). This posttranslation glycosylation decreases N-CAM-dependent cell adhesion and migration. The enzymatic properties of the membrane-bound form of the polyST activity was investigated in vitro. Our results show that the polyST activity was developmentally expressed with maximum specific activity appearing about 12 days after fertilization. This time shortly precedes maximal expression of the cognate polysialylated N-CAMs. Kinetic studies showed the K M and V max for CMPNeu5Ac were 133 µM and 0.13 µM/h, respectively, at pH 6.1, 33_C. CMP-Neu5Gc was not a donor substrate. PolyST activity was increased 5-to 6-fold in the presence of 10 mM MnCl 2, the preferred divalent cation, and 1 mM dithiothreitol (DTT). Heparin (3 kDa) was a noncompetitive inhibitor of polysialylation with a K i of 9 µM. Based on the affinity of the enzyme for heparin, the polyST activity was partially purified (∼30-fold) by heparin-Sepharose affinity chromatography, after differential solubilization with the zwitterionic detergent, CHAPS. DTT and chemical modification studies using the thiol-directed alkylating reagents, N-ethylmaleimide (NEM) and iodoacetamide (IAA), were used to show that at least one cysteinyl residue in the polyST was of critical importance for polysialylation, but of lesser importance for monosialylation, catalyzed by the α2,3-, α2,6-, and α2,8-monosialyltransferases (monoSTs). A sulfhydryl residue is implicated in chain initiation. Two important structural differences between the mono-and polySTs were revealed by sequence analyses. First, the polySTs contain heparin-like, positively charged amino acid clusters upstream of both sialylmotif L and S. Second, the polySTs contain a uniquely extended basic amino acid region (pI 11.6-12.0) of 31 residues immediately upstream of sialylmotif S. This extended, positively charged region may function in the processive mechanism of polymerization by allowing nascent polySia chains to remain bound to the polyST during the repetitive addition of each new Sia residue to the nonreducing termini of the growing chain. The importance of these studies is that they provide new information on the enzymatic basis of polysialylation. They also reveal that sulfhydryl residues and extended basic amino acid domains are two structural features unique to polysialylation, in contrast to monosialylation. Both may be important distinguishing features between the classes of distributive (monoSTs) and processive polysialyltransferases, which have not been previously described.

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Expression of NCAM and its polysialylated isoforms during mdx mouse muscle regeneration and in vitro myogenesis

Cited by 45 publications

References 36 publications

Secreted Protein Acidic and Rich in Cysteine (SPARC) in Human Skeletal Muscle

Secreted Protein Acidic and Rich in Cysteine (SPARC) in Human Skeletal Muscle

Myogenesis in human denervated muscle biopsies

Developmental expression and characterization of the 2,8-polysialyltransferase activity in embryonic chick brain

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