LBP-p40 Binds DNA Tightly through Associations with Histones H2A, H2B, and H4

Kinoshita, Koichi; Kaneda, Y.; Sato, Manabu; Saeki, Yoshinaga; Wataya‐Kaneda, Mari; Hoffmann, Alexander; Kaneda, Yasufumi

doi:10.1006/bbrc.1998.9699

Cited by 46 publications

(44 citation statements)

References 37 publications

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“…When almost all nuclei displayed ACC (8 h after Fasinduction), these proteins were essentially undetectable in the NMP fraction ( Figure 5, open circles). At that time, a further set of proteins was significantly decreased, including the chromatin-associated proteins LBP-p40, 36 hnRNP C1, E, K, U, 37 MCM2/3, 38 HP-1g, 39 in addition to nucleoporin p62, annexin IV, prohibitin and an abundant, but yet uncharacterized, motor protein ( Figure 5, Table 1). …”

Section: Decrease Of Nuclear Proteins During Accmentioning

confidence: 99%

Proteome analysis of nuclear matrix proteins during apoptotic chromatin condensation

et al. 2002

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The nuclear matrix (NM) is considered a proteinaceous scaffold spatially organizing the interphase nucleus, the integrity of which is affected during apoptosis. Caspasemediated degradation of NM proteins, such as nuclear lamins, precedes apoptotic chromatin condensation (ACC). Nevertheless, other NM proteins remain unaffected, which most likely maintain a remaining nuclear structure devoid of chromatin. We, therefore, screened various types of apoptotic cells for changes of the nuclear matrix proteome during the process of apoptotic ACC. Expectedly, we observed fundamental alterations of known chromatin-associated proteins, comprising both degradation and translocation to the cytosol. Importantly, a consistent set of abundant NM proteins, some (e.g. hNMP 200) of which displaying structural features, remained unaffected during apoptosis and might therefore represent constituents of an elementary scaffold. In addition, proteins involved in DNA replication and DNA repair were found accumulated in the NM fraction before cells became irreversibly committed to ACC, a time point characterized in detail by inhibitor studies with orthovanadate. In general, protein alterations of a consistent set of NM proteins (67 of which were identified), were reproducibly detectable in Fasinduced Jurkat cells, in UV-light treated U937 cells and also in staurosporine-treated HeLa cells. Our data indicate that substantial alterations of proteins linking chromatin to an elementary nuclear protein scaffold might play an intriguing role for the process of ACC.

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Section: Decrease Of Nuclear Proteins During Accmentioning

confidence: 99%

Proteome analysis of nuclear matrix proteins during apoptotic chromatin condensation

et al. 2002

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“…Besides contributing to the key steps of metastasis, it is important to note that LRP/LR also plays crucial roles in the nucleus and cytosol. This includes nuclear structure maintenance and translational processes (10). Hence, with increased levels of total LRP/ LR, cells acquire heightened levels of protein synthesis, which is necessary for processes that are involved in cancer progression and metastasis, such as tumor angiogenesis.…”

Section: Late-stage Colorectal Cancer Cells Exhibit Significantly Higmentioning

confidence: 99%

“…The present study focuses on colorectal cancer, the third most common cancer type, with over 1.4 million new cases diagnosed in 2012, including 600,000 biogenesis (10). Its physiological functions include cellular growth, adhesion, invasion, movement and viability (10).…”

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confidence: 99%

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Anti-LRP/LR-Specific Antibody IgG1-iS18 Significantly Impedes Adhesion and Invasion in Early- and Late-Stage Colorectal Carcinoma Cells

Vania

Chetty

Ferreira

et al. 2016

Mol Med

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Cancer is a highly complex disease that has become one of the leading causes of death globally. Metastasis, a major cause of cancer deaths, requires two crucial events, adhesion and invasion. The 37kDa/67kDa laminin receptor (laminin receptor precursor/high-affinity laminin receptor [LRP/LR]) enhances these two steps, consequently aiding in cancer progression. In this study, the role of LRP/LR in adhesion and invasion of early-stage (SW-480 and HT-29) and late-stage (DLD-1) colorectal cancer cells was investigated. Western blotting revealed that early-and late-stage colorectal cancer cells contained significantly higher total LRP/LR levels compared with poorly invasive MCF-7 breast cancer control cells. Flow cytometry revealed that both stages of colorectal cancer displayed significantly higher cell surface LRP/LR levels. Furthermore, upon treatment of colorectal cancer cells with the anti-LRP/LR-specific antibody IgG1-iS18, adhesion to laminin-1 was significantly reduced in both stages. Each stage's invasive potential was determined using the Matrigel™ invasion assay, showing that invasion was significantly impeded in both colorectal cancer stages when the cells were incubated with IgG1-iS18. In addition, Pearson's correlation coefficients propose that both total and cell surface LRP/LR levels are directly proportional to the adhesive and invasive potential of both stages of colorectal cancer. Hence, these findings indicate potential for use of the IgG1-iS18 antibody as a promising therapeutic tool for colorectal cancer patients at both stages.

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“…the 40S ribosomal subunit and protein synthesis 31,32 and in the nucleus in which it is associated with histones H2A, H2B and H4. 94 LRP/LR is a transmembrane (TM) receptor (TMR) which is located at the cholesterol-rich lipid rafts and may employ HSPGs to mediate its binding interactions. 31,32 Aβ oligomers, as previously stated, have been shown to bind to an array of TM receptors and HSPGs or are alternatively inserted to lipid raft domains of the plasma membrane.…”

Section: Aβ Interactionsmentioning

confidence: 99%