Presence of Atypical Laminin on the Surface of Mouse Lewis Lung Carcinoma Cells.

Abe, Kazuhiko; Murakami, S; Mukae, Nobutaka; Morita, Takashi; Hashimoto, Yukio; Isemura, Mamoru; Shimo-Oka, Tadashi; Kimata, Koji; Narumi, Kunihiro; Satoh, Ken; Nukiwa, Toshihiro

doi:10.1620/tjem.180.33

Cited by 3 publications

(3 citation statements)

References 20 publications

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“…For example, laminin-β1 interacts with malignant cancer cells in tumor progression, and is synthesized and secreted in hepatocellular carcinoma 29 and expressed in lung cancer cells. 30 A growing number of studies targeting cytoskeletal molecules and ECM as anticancer drugs have shown promising outcomes in cancer treatment. 31,32 Therefore, our observation of up-regulated expression of actin, tubulin, or laminin in SCLC suggest that these molecules may be future therapeutic targets.…”

Section: Discussionmentioning

confidence: 99%

Proteomic Analysis of Human Small Cell Lung Cancer Tissues: Up-Regulation of Coactosin-Like Protein-1

Jeong¹,

Kim²,

Cho³

et al. 2011

J. Proteome Res.

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Small cell lung cancer (SCLC) is the leading cause of cancer death, with a high propensity for aggressiveness and metastasis even in an early stage. Thus, identification of biomarkers as early diagnostics and treatment is needed. In this study, we investigated differentially regulated proteins between human SCLC tissues and normal bronchial epithelium by proteomic analysis using two-dimensional electrophoresis (2-DE) and MALDI-TOF mass spectrometry. Seven proteins and protein isoforms, including, γ-actin, tubulin α-1B, laminin B1, coactosin-like protein-1 (COTL-1), ubiquitin carboxyl-terminal esterase L1, ubiquitin-conjugating enzyme E2-25K, and carbonic anhydrase 1, were up-regulated more than 2 fold in SCLC tissues. In particular, up-regulated COTL-1 expression was validated by Western blot analysis, immunohistochemistry, and reverse transcription quantitative polymerase chain reaction (RT-qPCR). Moreover, most SCLC tissues (93%; 28/30) were COTL-1-positive in immunohistochemistry, whereas only 16% (10/64) of nonsmall cell lung cancer (NSLC) tissues were. Taken together, this SCLC proteomic data may help in establishing a human SCLC proteome database. COTL-1 may be a biomarker or a therapeutic target in SCLC patients.

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Section: Discussionmentioning

confidence: 99%

Proteomic Analysis of Human Small Cell Lung Cancer Tissues: Up-Regulation of Coactosin-Like Protein-1

Jeong¹,

Kim²,

Cho³

et al. 2011

J. Proteome Res.

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“…LAMR 67 is considered to be primarily located at the plasma membrane, possibly concentrated in lipid rafts (Fujimura, Yamada & Tachibana, ). This has been sufficiently demonstrated using fluorescent microscopy, membrane fractionation and FACS on unpermeabilized cells (Liotta et al, ; Castronovo et al, ; Landowski et al, ; Abe et al, ).…”

Section: /67‐kda Laminin Receptor Identitymentioning

confidence: 99%

Looking into laminin receptor: critical discussion regarding the non‐integrin 37/67‐kDalaminin receptor/RPSAprotein

2015

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The 37/67-kDa laminin receptor (LAMR/RPSA) was originally identified as a 67-kDa binding protein for laminin, an extracellular matrix glycoprotein that provides cellular adhesion to the basement membrane. LAMR has evolutionary origins, however, as a 37-kDa RPS2 family ribosomal component. Expressed in all domains of life, RPS2 proteins have been shown to have remarkably diverse physiological roles that vary across species. Contributing to laminin binding, ribosome biogenesis, cytoskeletal organization, and nuclear functions, this protein governs critical cellular processes including growth, survival, migration, protein synthesis, development, and differentiation. Unsurprisingly given its purview, LAMR has been associated with metastatic cancer, neurodegenerative disease and developmental abnormalities. Functioning in a receptor capacity, this protein also confers susceptibility to bacterial and viral infection. LAMR is clearly a molecule of consequence in human disease, directly mediating pathological events that make it a prime target for therapeutic interventions. Despite decades of research, there are still a large number of open questions regarding the cellular biology of LAMR, the nature of its ability to bind laminin, the function of its intrinsically disordered C-terminal region and its conversion from 37 to 67 kDa. This review attempts to convey an in-depth description of the complexity surrounding this multifaceted protein across functional, structural and pathological aspects.

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“…When the cells were stained in the presence of 0.5 M methyl -mannoside, a decrease in cell-associated fluorescence was observed (B). Control cells without the biotinylated ACL treatment are shown in C. cording to the method described previously, 10) the cell surfaces were fluorescence-labeled (Fig. 3A).…”

mentioning

confidence: 99%

Stimulation of IL-8 Production byAralia cordateLectin in Human Colon Carcinoma Caco-2 Cells

Koyama

Suzuki

Kajiya

et al. 2005

Bioscience, Biotechnology, and Biochemistry

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Presence of Atypical Laminin on the Surface of Mouse Lewis Lung Carcinoma Cells.

Cited by 3 publications

References 20 publications

Proteomic Analysis of Human Small Cell Lung Cancer Tissues: Up-Regulation of Coactosin-Like Protein-1

Proteomic Analysis of Human Small Cell Lung Cancer Tissues: Up-Regulation of Coactosin-Like Protein-1

Looking into laminin receptor: critical discussion regarding the non‐integrin 37/67‐kDalaminin receptor/RPSAprotein

Stimulation of IL-8 Production byAralia cordateLectin in Human Colon Carcinoma Caco-2 Cells

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