Oligomeric Forms of the Metastasis-related Mts1 (S100A4) Protein Stimulate Neuronal Differentiation in Cultures of Rat Hippocampal Neurons

Novitskaya, Vera; Grigorian, Mariam; Kriajevska, Marina; Tarabykina, Svetlana; Bronstein, Igor B.; Berezin, Vladimir; Bock, Elisabeth; Lukanidin, Eugene

doi:10.1074/jbc.m007058200

Cited by 148 publications

(191 citation statements)

References 41 publications

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“…which L is the neurite length in lm, d is the vertical distance between two grid lines, and J is the number of intersections between grid lines and neuritis (Novitskaya et al, 2000).…”

Section: Neural Survival and Neurite Outgrowth Assays In Vitromentioning

confidence: 99%

Effects of Reg‐2 on Survival of Spinal Cord Neurons In Vitro

Fang

Huang

Shao

et al. 2010

The Anatomical Record

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Regeneration gene protein 2 (Reg-2) is a small secreted protein expressed in motor and sensory neurons of spinal cord during developmental stages and following injury of peripheral nerves. Reg-2 appears to act as a neurotrophic factor and protects injured neurons from death during regeneration. To illustrate these potential protective effects in vitro, we investigated the blocking effects of Reg-2 antibodies on the survival of primary cultured spinal cord neurons and astrocytes, as well as on neurite outgrowth. In addition, the effects of Reg-2 in neuron injury models induced by peroxide and mitochondrial poisoning were assessed. Our results showed that Reg-2 antibody markedly reduced survival and neurite outgrowth from neurons, whereas astrocyte survival was unaffected. Addition of Reg-2 into the culture medium had no effect on neuron survival or neurite outgrowth. However, the addition of the Reg-2 into culture media after peroxide treatment or cellular hypoxia insult induced by mitochondrial poisoning can reduce lactate dehydrogenase release levels and cell death. Thus, the data suggests that Reg-2 is essential for the survival and neurite outgrowth of developing spinal cord neurons but not the survival of glial cells, and that Reg-2 plays protective effects on spinal cord neurons against injury in vitro. Anat Rec, 293:464-476, 2010. V V C 2010 Wiley-Liss, Inc.

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“…which L is the neurite length in lm, d is the vertical distance between two grid lines, and J is the number of intersections between grid lines and neuritis (Novitskaya et al, 2000).…”

Section: Neural Survival and Neurite Outgrowth Assays In Vitromentioning

confidence: 99%

Effects of Reg‐2 on Survival of Spinal Cord Neurons In Vitro

Fang

Huang

Shao

et al. 2010

The Anatomical Record

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“…Treatment of 3D cultures of SVEC 4-10 cells with the S100A4 oligomeric protein stimulated the formation of protrusions (Figure 1b and e). The addition of the Y75F mutant of S100A4 that is capable of forming dimers only (Novitskaya et al, 2000) did not stimulate growth of the protrusions (Figure 1c and e). The observed capillary-like growth was also stimulated by tumor necrosis factor-a (TNF-a) and hepatocyte growth factor (HGF), indicating that this assay could be used for analysis of the stimulatory effect of different angiogenic molecules.…”

Section: Stimulation Of Capillary-like Growth Of Microvascular Endothmentioning

confidence: 99%

“…It was shown that extracellular activity of S100A4 is associated with the oligomeric conformation of the protein (Novitskaya et al, 2000;Ambartsumian et al, 2001). This conformation is detected both in vitro, in the conditioned media from the cells secreting S100A4, and in vivo, in the blood serum.…”

Section: Introductionmentioning

confidence: 99%

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Extracellular S100A4(mts1) stimulates invasive growth of mouse endothelial cells and modulates MMP-13 matrix metalloproteinase activity

et al. 2004

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S100A4(mts1) protein expression has been strongly associated with metastatic tumor progression. It has been suggested as a prognostic marker for a number of human cancers. It is proposed that extracellular S100A4 accelerates cancer progression by stimulating the motility of endothelial cells, thereby promoting angiogenesis. Here we show that in 3D culture mouse endothelial cells (SVEC 4-10) respond to recombinant S100A4 by stimulating invasive growth of capillary-like structures. The outgrowth is not dependent on the stimulation of cell proliferation, but rather correlates with the transcriptional modulation of genes involved in the proteolytic degradation of extracellular matrix (ECM). Treatment of SVEC 4-10 with the S100A4 protein leads to the transcriptional activation of collagenase 3 (MMP-13) mRNA followed by subsequent release of the protein from the cells. b-Casein zymography demonstrates enhancement of proteolytic activity associated with MMP-13. This observation indicates that extracellular S100A4 stimulates the production of ECM degrading enzymes from endothelial cells, thereby stimulating the remodeling of ECM. This could explain the angiogenic and metastasis-stimulating activity of S100A4(mts1).

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“…They are also associated with human diseases, including inflammation, brain disorders, cancer, diabetes, heart failure, and pathological conditions of the skin and hair follicle. The basic structural and functional unit of most S100 proteins was previously thought to be a noncovalently associated antiparallel dimer; however, there is increasing evidence that some members assemble into higher order oligomers, thereby conferring their biological function (3)(4)(5)(6)(7).…”

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confidence: 99%

Specific Citrullination Causes Assembly of a Globular S100A3 Homotetramer

Kizawa¹,

Takahara

Troxler

et al. 2008

Journal of Biological Chemistry

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S100A3 is a unique member of the Ca 2؉ -binding S100 protein family with the highest cysteine content and affinity for Zn 2؉ . This protein is highly expressed in the differentiating cuticular cells within the hair follicle and organized into mature hair cuticles. Previous studies suggest a close association of S100A3 with epithelial differentiation, leading to hair shaft formation, but its molecular function is still unknown. By two-dimensional PAGE-Western blot analyses using a modified citrulline antibody, we discovered that more than half of the arginine residues of native S100A3 are progressively converted to citrullines by Ca 2؉ -dependent peptidylarginine deiminases. Confocal immunofluorescent microscopy showed that the cytoplasmic S100A3 within the cuticular layer is mostly co-localized with the type III isoform of peptidylarginine deiminase (PAD3) but not with PAD1. Recombinant PAD1 and PAD2 are capable of converting all 4 arginines in recombinant S100A3, whereas PAD3 specifically converts only Arg-51 into citrulline. Gel filtration analyses showed that either enzymatic conversion of Arg-51 in S100A3 to citrulline or its mutational substitution with alanine (R51A) promotes a homotetramer assembly. Fluorescent titration of R51A suggested that its potential Ca 2؉ binding property increased during tetramerization. A prototype structural model of the globular Ca 2؉ -bound S100A3 tetramer with citrulline residues is presented. High concentrations of S100A3 homotetramer might provide the millimolar level of Ca 2؉ required for hair cuticular barrier formation.

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Oligomeric Forms of the Metastasis-related Mts1 (S100A4) Protein Stimulate Neuronal Differentiation in Cultures of Rat Hippocampal Neurons

Cited by 148 publications

References 41 publications

Effects of Reg‐2 on Survival of Spinal Cord Neurons In Vitro

Effects of Reg‐2 on Survival of Spinal Cord Neurons In Vitro

Extracellular S100A4(mts1) stimulates invasive growth of mouse endothelial cells and modulates MMP-13 matrix metalloproteinase activity

Specific Citrullination Causes Assembly of a Globular S100A3 Homotetramer

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