Anti-sense RNA of 32-kDa laminin-binding protein inhibits attachment and invasion of a human colon carcinoma cell line

Mafune, Ken–ichi; Ravikumar, T. S.

doi:10.1016/0022-4804(92)90113-e

Cited by 31 publications

(17 citation statements)

References 23 publications

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“…In the present study, cell lines expressing reduced M r 67,000 laminin receptor demonstrated a significantly reduced ability to attach to laminin and to traverse Matrigel-coated filters compared with parental cells and sense-transfected cells. These findings are in agreement with other studies demonstrating the role of the M r 67,000 laminin receptor in attachment to laminin and invasion of tumor cells (20,24) and confirm the importance of the receptor in these processes.…”

Section: Discussionsupporting

confidence: 93%

“…In addition to its physiological roles (18,19), expression of the M r 67,000 laminin receptor has been shown to be upregulated in neoplastic cells compared with their normal counterparts and to directly correlate with an enhanced invasive and metastatic potential in many malignancies (14, 20 -22). The receptor has been implicated in laminin-induced tumor cell attachment (20,23,24) and migration (25), as well as in tumor angiogenesis (26), growth, invasion, and metastasis (2,20,24).…”

Section: Introductionmentioning

confidence: 99%

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Laminin-Induced Signaling in Tumor Cells

2004

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The expression of the M r 67,000 laminin receptor, a nonintegrin laminin receptor, was found to be up-regulated in neoplastic cells and to directly correlate with invasion and metastatic potential. In the present study, we investigated the role of laminin receptor in mediating laminin effects and the involvement of the mitogen-activated protein kinases (MAPK) cascades and dual-specificity phosphatases in laminin signaling in human melanoma cells. Using stable transfection of A375SM melanoma cells, we established lines expressing reduced or elevated laminin receptor. The antisense-transfected cells demonstrated reduced attachment to laminin and reduced invasion through Matrigel-coated filters. In addition, both matrix metalloproteinase-2 (MMP-2) mRNA expression and activity were significantly reduced in the antisense-transfected cells. Antisensetransfected cells showed a reduction in mRNA level of the ␣6B integrin subunit isoform, whereas no change in the mRNA level of the ␣6A isoform was observed. We found that exogenous laminin reduced the phosphorylated (active) form of extracellular signal-regulated kinase, c-Jun NH 2 -terminal protein kinase, and p38 in all of the cells, irrespective of the expression of the laminin receptor. Furthermore, the phosphorylation of extracellular signal-regulated kinase, c-Jun NH 2 -terminal protein kinase, and p38 was significantly higher in the cell lines expressing reduced laminin receptor, regardless of the exposure to exogenous laminin. This increase of MAPK phosphorylation was accompanied by a significant reduction in MKP-1 phosphatase mRNA level and a significant increase in PAC-1 phosphatase mRNA level. In conclusion, our results confirm the involvement of the laminin receptor in different mechanisms related to tumor dissemination and provide first evidence of the involvement of MAPK and dual-specificity phosphatases in its signal transduction pathway.

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Section: Discussionsupporting

confidence: 93%

Section: Introductionmentioning

confidence: 99%

Laminin-Induced Signaling in Tumor Cells

2004

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“…In addition to its physiological roles [12,13] , expression of the 67LR has been shown to be upregulated in neoplastic cells compared with their normal counterparts and to directly correlate with an enhanced invasive and metastatic potential in many malignancies [14][15][16][17] . The receptor has been implicated in laminin-induced tumor cell attachment [18,19] and migration [20] , as well as in tumor angiogenesis [21] , growth, invasion, and metastasis [15,19] .…”

Section: Discussionmentioning

confidence: 99%

67-kDa Laminin Receptor in Human Bile Duct Carcinoma

Chen

Gao

et al. 2009

Eur Surg Res

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Background/Aim: Abnormal interaction of epithelial cells with laminin component of basement membrane may account for altered biological behavior of cells, influencing proliferation, adhesion, and motility. In the current study, we investigated the role of 67-kDa laminin receptor (67LR), a high affinity receptor for laminin, in aggressiveness of bile duct carcinoma. Methods: Fifty-two paraffin-embedded specimens and 22 fresh tissues of patients with bile duct carcinoma were analyzed using immunohistologic and real-time polymerase chain reaction techniques, respectively. Expression of 67LR on the bile duct carcinoma QBC939 cells was examined by flow cytometry. The effects of 67LR on the adhesive and invasive abilities of QBC939 cells were determined by adhesion and invasion assay in vitro. Results: Both at the mRNA and protein level, bile duct carcinoma cells expressed a higher level of 67LR than normal epithelial cells (p < 0.01). The expression of 67LR was correlated inversely with differentiation extent of tumor (p < 0.05). The 67LR level was significantly increased in patients with lymph node metastases than in patients without lymph node involvement (p < 0.01). Flow cytometry showed that 69.9 ± 1.1% of QBC939 cells expressed 67LR. Expression of 67LR increased the adhesion and invasion of QBC939 cells. 60 and 120 min of incubation of 67LR antibodies, MLuC5, induced 46.3 ± 2.2 and 61.3 ± 2.1% inhibition of adhesion, respectively. The invasive ability of QBC939 cells to Matrigel was also reduced by 67LR antibodies, MLuC5. Conclusions: Overexpressing 67LR on bile duct carcinoma was associated with invasion and metastasis of bile duct carcinoma. Blockage of 67LR suppressed adhesion and invasion of bile duct carcinoma.

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“…It promotes lamellipodia formation and the turnover of focal adhesions both of which stimulate cell migration 54, 55 . Studies show that LamR plays a role in cell migration 40, 56, 57 and localizes to lamellipodia structures in migrating cells 27 . The LamR-β-PIX interaction may be important for regulating the dynamics of focal contacts and facilitating cell movement.…”

Section: Resultsmentioning

confidence: 99%

Comprehensive Proteomic Analysis of Nonintegrin Laminin Receptor Interacting Proteins

Venticinque

Meruelo

2012

J. Proteome Res.

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Human non-integrin laminin receptor is a multifunctional protein acting as an integral component of the ribosome and a cell surface receptor for laminin-1. Laminin receptor is overexpressed in several human cancers and is also the cell surface receptor for several viruses and pathogenic prion protein, making it a pathologically significant protein. This study focused on the proteomic characterization of laminin receptor interacting proteins from mus musculus. The use of affinity chromatography with immobilized recombinant laminin receptor coupled with mass spectrometry analysis identified 45 proteins with high confidence. Following validation through co-immunoprecipitation, the proteins were classified based on predicted function into ribosomal, RNA processing, signal transduction/ metabolism, protein processing, cytoskeleton/ cell anchorage, DNA/ chromatin and unknown functions. A significant portion of the identified proteins is related to functions or localizations previously described for laminin receptor. This work represents a comprehensive proteomic approach to studying laminin receptor, and provides an essential stepping-stone to a better mechanistic understanding of this protein’s diverse functions.

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Anti-sense RNA of 32-kDa laminin-binding protein inhibits attachment and invasion of a human colon carcinoma cell line

Cited by 31 publications

References 23 publications

Laminin-Induced Signaling in Tumor Cells

Laminin-Induced Signaling in Tumor Cells

67-kDa Laminin Receptor in Human Bile Duct Carcinoma

Comprehensive Proteomic Analysis of Nonintegrin Laminin Receptor Interacting Proteins

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