Design of Inhibitors for S100B

Markowitz, Joseph; MacKerell, Alexander D.; Charpentier, Thomas H.; Weber, David J.

doi:10.2174/156802605774370865

Cited by 31 publications

(25 citation statements)

References 137 publications

(200 reference statements)

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“…Markowitz et al developed a drug discovery approach to identify chemical compounds disrupting the interaction between S100B and p53 [153]. Because protein-target interactions significantly modify the conformation of S100B protein, the screening procedure was performed by combination of biophysical methods in vitro.…”

Section: S100a4: Perspectives For Therapeutic Interven-tionmentioning

confidence: 99%

Metastasis-Associated Protein S100A4: Spotlight on its Role in Cell Migration

Tarabykina

Griffiths

Tulchinsky

et al. 2007

CCDT

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S100A4 (also known as Mts1, metastasin, p9Ka, pEL98, CAPL, calvasculin, Fsp-1, placental calcium-binding protein) belongs to the family of EF-hand calcium-binding proteins, whose expression is elevated in a number of pathological conditions. Although it is well documented that S100A4 is expressed in cancer cells and contributes to tumor cell motility and metastatic progression, the exact underlying mechanisms remain elusive. An important characteristic feature of S100 proteins is their dual function, inside and outside the cell. In this review, we focus on the intracellular function of S100A4. The review contains structural analysis of S1004 in comparison with other members of S100 proteins. Possible modes of the interaction of S100 proteins with targets are described. Several examples of best-studied molecular interactions involving S100A4 with heavy chain of nonmuscle myosin IIA, LAR-interacting protein liprin beta1 and tumor suppressor protein p53 are provided. We suggest that the binding of S100A4 to these molecules is critical for the S100A4 function. Further studies of the implications of these interactions in different molecular pathways may shed additional light on the role of S100A4 protein in the control of tumor cell motility and migration. We discuss the approaches for down-regulation of S100A4 expression and their potential for application in the clinics.

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Section: S100a4: Perspectives For Therapeutic Interven-tionmentioning

confidence: 99%

Metastasis-Associated Protein S100A4: Spotlight on its Role in Cell Migration

Tarabykina

Griffiths

Tulchinsky

et al. 2007

CCDT

View full text Add to dashboard Cite

show abstract

“…One of the structures involves binding to Ca 2+ -loaded dimeric S100B(ββ), which blocks access to several phosphorylation and acetylation sites in p53-NRD and thus inhibits p53 oligomerization and transcriptional activity 28 . The level of S100B protein is correlated with malignant melanoma, and is often used as a diagnostic cancer marker 29 .…”

Section: Introductionmentioning

confidence: 99%

Potential Conformational Heterogeneity of p53 Bound to S100B(ββ)

McDowell

Chen

2013

Journal of Molecular Biology

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“…The determination of S100B protein in cerebrospinal fluid (CSF) is very important in patients with metastatic carcinoma in CNS, such as determining the degree of brain injury, evaluating the therapeutic effect and prognosis, and so on [11]. S100B can also interact with the p53 protein in a calcium-dependent manner and downregulates its function as a tumor suppressor, which lead to genesis and metastasis of neoplastic cells [27].…”

Section: Discussionmentioning

confidence: 99%

Biological characteristics of a specific brain metastatic cell line derived from human lung adenocarcinoma

Zhang

Zhu

et al. 2009

Med Oncol

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To study the expression of VEGF, MMP-9, EGFR, and S100B in a highly brain metastases sub-clone cell line, PC14/B. The in vitro metastases-related behaviors of PC14 /B cells, such as adhesion to extracellular matrix (ECM), migration, and invasion were determined and compared with primary PC14 cells and A549 cells that do not metastasize to brain. The expression of vascular epithelial growth factor (VEGF), matrix metalloproteinase 9 (MMP-9), S100B, and epidermal growth factor receptor (EGFR) in the above three cell lines were measured by immunohistochemical staining and Western blot assay.The PC14/B cells have enhanced abilities of adhesion, migration, and invasion than PC14 cells and A549 cells. The expression levels of VEGF and MMP-9 in PC14/B cells are much higher than in PC14 and A549 cells. Two protein polymers of S100B are expressed specially in PC14/B cells. The expression of EGFR has a significant lower level in PC14 cells than in the other two cell lines. The increased expression of VEGF and MMP-9 may lead to the enhancement of adhesion, migration, and invasion of PC14/B cells. The expression of EGFR in PC14/B cells may have negative correlation with their capacities of metastasizing to brain. The specific expression of S100B in PC14/B cells strongly suggest that S100B might be a potential target for developing new therapy to brain metastases of lung cancer.

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Design of Inhibitors for S100B

Cited by 31 publications

References 137 publications

Metastasis-Associated Protein S100A4: Spotlight on its Role in Cell Migration

Metastasis-Associated Protein S100A4: Spotlight on its Role in Cell Migration

Potential Conformational Heterogeneity of p53 Bound to S100B(ββ)

Biological characteristics of a specific brain metastatic cell line derived from human lung adenocarcinoma

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