Isolation of a YAC clone covering a cluster of nine S100 genes on human chromosome 1q21: rationale for a new nomenclature of the S100 calcium-binding protein family

Schäfer, Beat W.; Wicki, Roland; Engelkamp, Dieter; Matteï, Marie‐Geneviève; Heizmann, Claus W.

doi:10.1016/0888-7543(95)80005-7

Cited by 313 publications

(193 citation statements)

References 27 publications

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“…1, 7, and 8), giant myosin-associated twitchin kinase (9), and the SR Ca 2ϩ release channel (both S100A1) (10). Thirteen S100 genes were found to be localized in a cluster on human chromosome 1q21 (11)(12)(13). Contrary to calmodulin, the expression of S100 proteins is cell-and tissue-specific.…”

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confidence: 93%

Binding of Ca2+ and Zn2+ to Human Nuclear S100A2 and Mutant Proteins

Franz¹,

Durussel²,

Cox³

et al. 1998

Journal of Biological Chemistry

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confidence: 93%

Binding of Ca2+ and Zn2+ to Human Nuclear S100A2 and Mutant Proteins

Franz¹,

Durussel²,

Cox³

et al. 1998

Journal of Biological Chemistry

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“…The S100A4 gene encodes an acidic 101 amino acid protein containing two EFhand motifs. The mouse S100A4 gene is located on chromosome 3 and the human gene on 1q21, both as a cluster with calcyclin (CACY/S100A6) and several other S100-related protein genes (SchaÈ fer et al, 1995). The S100A4 gene was independently cloned from various sources based on di erent interests, and the gene product has been implicated to play important roles in many biological phenomena such as cell immortalization (Goto et al, 1988), cell growth (Jackson-Grusby et al, 1987), di erentiation of mammary epithelial stem cells to myoepithelial-like cells (Barraclough et al, 1987), and ®brogenesis (Strutz et al, 1995).…”

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Expression of antisense RNA to S100A4 gene encoding an S100-related calcium-binding protein suppresses metastatic potential of high-metastatic Lewis lung carcinoma cells

1997

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S100A4 (also known as pEL98/mts1/p9Ka/18A2/42A/ calvasculin/FSP1/CAPL), a member of S100-related calcium-binding proteins, has been implicated to play a role in metastasis. In the present study, we examined the e ect of antisense S100A4 RNA on metastatic potential of Lewis lung carcinoma (LLC) cells. High-metastatic A11 cells were transfected with the expression vector containing S100A4 cDNA in an inverted (antisense) orientation under the transcriptional control of the mouse metallothionein promoter. Treatment of a stably transfected clone (AS10 cells) with Zn 2+ resulted in the suppression of the experimental metastatic ability, which was accompanied with the expression of antisense S100A4 RNA and the suppression of the S100A4 expression at both the mRNA and the protein levels. To further con®rm the e ect of antisense S100A4 RNA, we established several clones after retroviral transduction with an antisense S100A4 construct. Notably, reduced metastatic potential was also evident in these clones. In the antisense S100A4 RNA-expressing cells, cell motility and in vitro invasiveness were found to be suppressed.

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“…7) Therefore, the terms S100A8 and S100A9 are now common, 12) although the names MRP8 and 14, or calgranulin A and B, are still often used.…”

Section: Introductionmentioning

confidence: 99%

Calprotectin (S100A8/S100A9), an Inflammatory Protein Complex from Neutrophils with a Broad Apoptosis-Inducing Activity

Yui

Nakatani

Mikami

2003

Biological & Pharmaceutical Bulletin

283

211

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Calprotectin, a complex of two calcium-binding proteins that belong to the S100 protein family, is abundant in the cytosolic fraction of neutrophils. A high level of calprotectin reportedly exists in extracellular fluid during various inflammatory conditions, such as rheumatoid arthritis, cystic fibrosis and abscesses. However, the exact biological role(s) of the factor is now under investigation. We recently observed that neutrophils contain a factor that shows growth-inhibitory and apoptosis-inducing activities against various cell types including tumor cells and normal fibroblasts, and we identified that factor as calprotectin. The findings suggest that calprotectin exerts a regulatory activity in inflammatory processes through its effect on the survival or growth states of cells participating in the inflammatory reaction. It is also possible that calprotectin, at a high concentration, might have a deleterious effect on fibroblasts and influence the recovery of inflammatory tissue. Therefore, the protein factor may be a new drug target to control inflammatory reactions. We found that a few of the Amaryllidaceae alkaloids effectively inhibited the growth-inhibitory and apoptosis-inducing activities of calprotectin. In this article, we focus on the biological functions of calprotectin in extracellular fluids, focusing on its apoptosis-inducing activity.

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Isolation of a YAC clone covering a cluster of nine S100 genes on human chromosome 1q21: rationale for a new nomenclature of the S100 calcium-binding protein family

Cited by 313 publications

References 27 publications

Binding of Ca2+ and Zn2+ to Human Nuclear S100A2 and Mutant Proteins

Binding of Ca2+ and Zn2+ to Human Nuclear S100A2 and Mutant Proteins

Expression of antisense RNA to S100A4 gene encoding an S100-related calcium-binding protein suppresses metastatic potential of high-metastatic Lewis lung carcinoma cells

Calprotectin (S100A8/S100A9), an Inflammatory Protein Complex from Neutrophils with a Broad Apoptosis-Inducing Activity

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