Molecular cloning and characterization of the human budding uninhibited by benomyl (BUB3) promoter

Baek, Won-Ki; Park, Jong Wook; Lim, Jun Hee; Suh, Seong Il; Suh, Min Ho; Gabrielson, Edward; Kwon, Taeg Kyu

doi:10.1016/s0378-1119(02)00827-2

Cited by 22 publications

(12 citation statements)

References 26 publications

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“…BUB3 plays a role in chromosome homeostasis and is a component of the spindle assembly checkpoint complex [23], alterations of which could underlie the aneuploidy that is characteristic of OS [160]. Interestingly, BUB3 is a target of E2F [6]. Primase polypeptide 1 (PRIM1), located at 12q13, is amplified in nine of 22 OS tumors [276].…”

Section: Additional Genetic Changesmentioning

confidence: 99%

Osteosarcoma Development and Stem Cell Differentiation

Tang

Song

Luo

et al. 2008

Clin Orthop Relat Res

317

373

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Osteosarcoma is the most common nonhematologic malignancy of bone in children and adults. The peak incidence occurs in the second decade of life, with a smaller peak after age 50. Osteosarcoma typically arises around the growth plate of long bones. Most osteosarcoma tumors are of high grade and tend to develop pulmonary metastases. Despite clinical improvements, patients with metastatic or recurrent diseases have a poor prognosis. Here, we reviewed the current understanding of human osteosarcoma, with an emphasis on potential links between defective osteogenic differentiation and bone tumorigenesis. Existing data indicate osteosarcoma tumors display a broad range of genetic and molecular alterations, including the gains, losses, or arrangements of chromosomal regions, inactivation of tumor suppressor genes, and the deregulation of major signaling pathways. However, except for p53 and/or RB mutations, most alterations are not constantly detected in the majority of osteosarcoma tumors. With a rapid expansion of our knowledge about stem cell biology, emerging evidence suggests osteosarcoma should be regarded as a differentiation disease caused by genetic and epigenetic changes that interrupt osteoblast differentiation from mesenchymal stem cells. Understanding the molecular pathogenesis of human osteosarcoma could ultimately lead to the development of diagnostic and prognostic markers, as well as targeted therapeutics for osteosarcoma patients.

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Section: Additional Genetic Changesmentioning

confidence: 99%

Osteosarcoma Development and Stem Cell Differentiation

Tang

Song

Luo

et al. 2008

Clin Orthop Relat Res

317

373

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“…Nuclear extract preparation and electrophoretic mobility shift assay (EMSA) Preparation of nuclear extracts from control or drugtreated cells was carried out as described previously (Baek et al, 2002). The sequences of the doublestranded oligonucleotides used to detect the DNAbinding activities of NF-kB, CREB and C/EBP are as follows: NF-kB, 5 0 -AGT TGA GGG GAC TTT CCC AGG C-3 0 ; CREB, 5 0 -AGA GAT TGC CTG ACG TCA GAG AGC TAG-3 0 and C/EBP, 5 0 -TGC AGA TTG CGC AAT CTG CA-3 0 .…”

Section: Article In Pressmentioning

confidence: 99%

Differential inhibitory effects of baicalein and baicalin on LPS-induced cyclooxygenase-2 expression through inhibition of C/EBPβ DNA-binding activity

et al. 2006

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“…Preparation of nuclear extracts from control or drugtreated cells was carried out as described previously [15]. An The whole-cell lysates were analyzed by immunoblot analysis using phosphorylation state-specific Akt antibodies.…”

Section: Nuclear Extract Preparation and Electrophoretic Mobility Shimentioning

confidence: 99%

LY294002 inhibits LPS-induced NO production through a inhibition of NF-κB activation: independent mechanism of phosphatidylinositol 3-kinase

et al. 2005

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Molecular cloning and characterization of the human budding uninhibited by benomyl (BUB3) promoter

Cited by 22 publications

References 26 publications

Osteosarcoma Development and Stem Cell Differentiation

Osteosarcoma Development and Stem Cell Differentiation

Differential inhibitory effects of baicalein and baicalin on LPS-induced cyclooxygenase-2 expression through inhibition of C/EBPβ DNA-binding activity

LY294002 inhibits LPS-induced NO production through a inhibition of NF-κB activation: independent mechanism of phosphatidylinositol 3-kinase

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