Immunolocalization of protein 4.1B/DAL-1 during neoplastic transformation of mouse and human intestinal epithelium

Ohno, Nobuhiko; Terada, Nobuo; Murata, Shin Ichi; Yamakawa, Hisashi; Newsham, Irene; Katoh, Ryohei; Ohara, Osamu; Ohno, Shinichi

doi:10.1007/s00418-004-0716-7

Cited by 28 publications

(20 citation statements)

References 47 publications

(44 reference statements)

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“…For instance, 4.1B has been reported to be lost in Յ60% of sporadic meningiomas (27), whereas allelic loss of region 18p11.3, where the 4.1B gene resides, was detected in 55% of ductal carcinomas in situ, as well as in 67% of invasive and metastatic breast cancers (28). In addition, 4.1B protein expression has been observed to be downregulated during tumorigenesis in spontaneous mouse models of pancreatic and intestinal cancer (29,30). Consistent with these findings, we have observed that 4.1B expression is significantly reduced in four studies of human clinical prostate cancer.…”

Section: Discussionmentioning

confidence: 99%

Protein 4.1B suppresses prostate cancer progression and metastasis

Wong

Haack

Kissil

et al. 2007

Proc. Natl. Acad. Sci. U.S.A.

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Protein 4.1B is a 4.1/ezrin/radixin/moesin domain-containing protein whose expression is frequently lost in a variety of human tumors, including meningiomas, non-small-cell lung cancers, and breast carcinomas. However, its potential tumor-suppressive function under in vivo conditions remains to be validated. In a screen for genes involved with prostate cancer metastasis, we found that 4.1B expression is reduced in highly metastatic tumors. Downregulation of 4.1B increased the metastatic propensity of poorly metastatic cells in an orthotopic model of prostate cancer. Furthermore, 4.1B-deficient mice displayed increased susceptibility for developing aggressive, spontaneous prostate carcinomas. In both cases, enhanced tumor malignancy was associated with reduced apoptosis. Because expression of Protein 4.1B is frequently downregulated in human clinical prostate cancer, as well as in a spectrum of other tumor types, these results suggest a more general role for Protein 4.1B as a negative regulator of cancer progression to metastatic disease.

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Section: Discussionmentioning

confidence: 99%

Protein 4.1B suppresses prostate cancer progression and metastasis

Wong

Haack

Kissil

et al. 2007

Proc. Natl. Acad. Sci. U.S.A.

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“…Cryosections for immunoXuorescence-staining were incubated with 2% bovine serum albumin in PBS for 1 h. Then they were immunostained with each primary antibody at 4°C overnight, and with the secondary antibodies at room temperature for 1 h. The immunostained cryosections were observed with a confocal laser scanning microscope (TCS4D; Leica, Bensheim, Germany), as described before (Ohno et al 2005b). The biotinylated secondary antibody was visualized as described previously (Ohno et al 2004b). The immunostained sections were counterstained with methylgreen, embedded in glycerol, and observed with a light microscope (BX-61; Olympus, Tokyo, Japan).…”

Section: Preparation Of Sections For Observation By Light or Electronmentioning

confidence: 99%

Histochemical analyses of living mouse liver under different hemodynamic conditions by “in vivo cryotechnique”

Ohno

Terada

Ohno

2006

Histochem Cell Biol

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Although the morphology and molecular distribution in animal liver tissues have been examined using conventional preparation methods, the findings are always affected by the technical artifacts caused by perfusion-fixation and tissue-resection. Using "in vivo cryotechnique" (IVCT), we have examined living mouse livers with histochemical, immunohistochemical and ultrastructural analyses. In samples prepared by IVCT, widely open sinusoids with many flowing erythrocytes were observed under normal blood circulation, and their collapse or blood congestion was seen in ischemic or heart-arrested mice. In contrast, the sinusoidal cavities were artificially dilated by perfusion-fixation, and collapsed by immersion-fixation and quick-freezing (QF) methods of resected tissues. The immunoreactivity of serum albumin and immunoglobulin G and intensity of periodic acid-Schiff-staining in hepatocytes were well preserved with the QF method and IVCT. Furthermore, following tissue resection, serum proteins were rapidly translocated into hepatocytes as demonstrated by immunoreactions on QF tissues frozen 1 or 5 min after resection. Translocation was not observed in IVCT samples, indicating that IVCT could be useful to examine cell membrane permeability of hepatocytes under different pathological conditions. Both dynamic morphology and immunodistribution of soluble components in living mouse livers, reflecting their physiological and pathological states, can be precisely examined by IVCT with higher time-resolution.

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“…Recent studies from our laboratory and others have implicated another member of the protein 4.1 superfamily, protein 4.1B, in the molecular pathogenesis of a wide variety of diverse human cancers (10)(11)(12)(13), including meningiomas (10,14,15). In these reports, protein 4.1B loss has been observed in human meningiomas at the DNA level by fluorescence in situ hybridization and PCR-based loss of heterozygosity (14).…”

Section: Introductionmentioning

confidence: 98%

Protein 4.1B/Differentially Expressed in Adenocarcinoma of the Lung-1 Functions as a Growth Suppressor in Meningioma Cells by Activating Rac1-Dependent c-Jun-NH2-kinase Signaling

2006

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Meningiomas are the second most common brain tumor in adults, yet comparatively little is presently known about the dysregulated growth control pathways involved in their formation and progression. One of the most frequently observed genetic changes in benign meningioma involves loss of protein 4.1B expression. Previous studies from our laboratory have shown that protein 4.1B growth suppression in meningioma is associated with the activation of the c-Jun-NH 2 -kinase (JNK) pathway and requires localization of a small unique region (U2 domain) of protein 4.1B to the plasma membrane. To define the relationship between protein 4.1B expression and JNK activation, as well as to determine the mechanism of JNK activation by protein 4.1B, we used a combination of genetic and pharmacologic approaches. In this report, we show that protein 4.1B/differentially expressed in adenocarcinoma of the lung-1 (DAL-1) expression in meningioma cells in vitro results in JNK activation, which requires the sequential activation of Src, Rac1, and JNK. In addition, inhibition of Rac1 or JNK activation abrogates protein 4.1B/DAL-1 growth suppression and cyclin A regulation. Last, protein 4.1B/DAL-1 regulation of this critical growth control pathway in meningioma cells requires the presence of the U2 domain. Collectively, these observations provide the first mechanistic insights into the function of protein 4.1B as a growth regulator in meningioma cells.

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Immunolocalization of protein 4.1B/DAL-1 during neoplastic transformation of mouse and human intestinal epithelium

Cited by 28 publications

References 47 publications

Protein 4.1B suppresses prostate cancer progression and metastasis

Protein 4.1B suppresses prostate cancer progression and metastasis

Histochemical analyses of living mouse liver under different hemodynamic conditions by “in vivo cryotechnique”

Protein 4.1B/Differentially Expressed in Adenocarcinoma of the Lung-1 Functions as a Growth Suppressor in Meningioma Cells by Activating Rac1-Dependent c-Jun-NH2-kinase Signaling

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