Protocadherin of the Liver, Kidney, and Colon Associates with Detergent-resistant Membranes during Cellular Differentiation

Krahn, Michael P.; Rizk, Sandra; Alfalah, Marwan; Behrendt, Marc; Naim, Hassan Y.

doi:10.1074/jbc.m109.080051

Cited by 8 publications

(17 citation statements)

References 41 publications

(33 reference statements)

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“…Figure 1C shows that most of the YFP signalrefl ecting the total CDHR24 protein -and the plasma membrane CDHR24 signal overlap, i.e., CDHR24 is predominantly located at the cell surface. To further confi rm the results from Figure 1C, we followed a biochemical approach and performed a cell trypsinization assay that has been described to be appropriate for CDHR24 (Krahn et al , 2010 ). The results show that after cleavage of proteins localized at the cell surface by trypsin, most of CDHR24 is reduced in size, verifying that most of the protein is localized at the cell surface at steady state ( Figure 1D).…”

supporting

confidence: 56%

“…Therefore, CDHR24 is supposed to act as a switch for intracellular signaling. Our group ' s previous work showed that CDHR24 expression is associated with the polarization of epithelial cells (Krahn et al , 2010 ). This associative role depends on its O-linked glycosylation as well as its association with specifi c membrane microdomains.…”

mentioning

confidence: 98%

“…CDHR24 is endogenously expressed in liver, kidney, and colon epithelia (Okazaki et al , 2002 ), where it is located apically as well as laterally (Okazaki et al , 2002 ;Krahn et al , 2010 ). To investigate if the morphological changes induced by CDHR24 expression and observed in the xy-direction also affected the morphology in the xz-direction, we examined the subcellular distribution of CDHR24 in CHO-CDHR24-YFP cells and compared it with that of APN.…”

mentioning

confidence: 99%

“…To analyze the intracellular distribution and processing of CDHR24 in nonpolarizing cells, a YFP-tagged version of CDHR24 (Krahn et al , 2010 ) was expressed in different cell lines. Chinese hamster ovarian (CHO) cells representing nonpolarized cells were stably transfected with pEYFP-CDHR24.…”

mentioning

confidence: 99%

“…Scale bars, 20 μ m. (C) CHO-CDHR24-YFP cells grown on cover slips were fi xed with paraformaldehyde, nuclei were stained with DAPI (Molecular Probes, Karlsruhe, Germany), cell surface CDHR24 (plasma membrane) with anti-CDHR24 (HPA012569; Sigma Chemical Co., Deisenhofen, Germany) and anti-rabbit-Alexa568 (Molecular Probes, Karlsruhe, Germany) followed by confocal analysis. (D) Cell surface trypsinization assay with CHO-CDHR24-YFP cells was essentially performed as described previously (Krahn et al , 2010 ). Total protein (50 μ g) from treated and untreated cells, respectively, were loaded on a 6 % SDS gel and blotted.…”

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confidence: 99%

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Cadherin-related protein 24 induces morphological changes and partial cell polarization by facilitating direct cell-cell interactions

Behrendt

Krahn

Al-Bayati

et al. 2012

Biological Chemistry

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Cadherin-related protein 24 (CDHR24) is a potential tumor suppressor located apically as well as laterally in polarized cells. Here, the role of CDHR24 in contributing to cell morphology and polarity is examined. CDHR24 was predominantly localized at the nonattached part of nonpolarizing cells while another apically sorted protein, aminopeptidase N, was equally distributed over the plasma membrane. Furthermore, CDHR24 expression induced cell aggregation capacity, indicating direct cell-cell interaction. The transepithelial resistance, however, was elevated in polarized MDCK cells, but not in nonpolarizing CHO cells. Our data propose a model in which CDHR24 is directly involved in cell and tissue morphogenesis.

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confidence: 56%

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confidence: 98%

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confidence: 99%

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confidence: 99%

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confidence: 99%

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Cadherin-related protein 24 induces morphological changes and partial cell polarization by facilitating direct cell-cell interactions

Behrendt

Krahn

Al-Bayati

et al. 2012

Biological Chemistry

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Long range epigenetic silencing is a trans‐species mechanism that results in cancer specific deregulation by overriding the chromatin domains of normal cells

et al. 2013

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DNA methylation and chromatin remodeling are frequently implicated in the silencing of genes involved in carcinogenesis. Long Range Epigenetic Silencing (LRES) is a mechanism of gene inactivation that affects multiple contiguous CpG islands and has been described in different human cancer types. However, it is unknown whether there is a coordinated regulation of the genes embedded in these regions in normal cells and in early stages of tumor progression. To better characterize the molecular events associated with the regulation and remodeling of these regions we analyzed two regions undergoing LRES in human colon cancer in the mouse model. We demonstrate that LRES also occurs in murine cancer in vivo and mimics the molecular features of the human phenomenon, namely, downregulation of gene expression, acquisition of inactive histone marks, and DNA hypermethylation of specific CpG islands. The genes embedded in these regions showed a dynamic and autonomous regulation during mouse intestinal cell differentiation, indicating that, in the framework considered here, the coordinated regulation in LRES is restricted to cancer. Unexpectedly, benign adenomas in Apc(Min/+) mice showed overexpression of most of the genes affected by LRES in cancer, which suggests that the repressive remodeling of the region is a late event. Chromatin immunoprecipitation analysis of the transcriptional insulator CTCF in mouse colon cancer cells revealed disrupted chromatin domain boundaries as compared with normal cells. Malignant regression of cancer cells by in vitro differentiation resulted in partial reversion of LRES and gain of CTCF binding. We conclude that genes in LRES regions are plastically regulated in cell differentiation and hyperproliferation, but are constrained to a coordinated repression by abolishing boundaries and the autonomous regulation of chromatin domains in cancer cells.

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Characterization of protocadherin‐1 expression in primary bronchial epithelial cells: association with epithelial cell differentiation

et al. 2011

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Protocadherin-1 (PCDH1) is a novel susceptibility gene for asthma that is expressed in airway epithelium. We aimed to characterize PCDH1 mRNA transcripts and protein expression in primary bronchial epithelial cells and to determine regulation of PCDH1 during mucociliary differentiation. Total RNA and protein were isolated from human primary bronchial epithelial cells. PCDH1 transcripts were characterized by rapid amplification of cDNA ends in bronchial epithelial cells of 4 subjects. PCDH1 expression was quantified by quantitative RT-PCR and Western blotting in bronchial epithelial cells directly ex vivo and after air liquid interface (ALI) or submerged culture. We identified 5 novel exons on the 5' end and 1 exon on the 3' end of PCDH1. Novel transcripts showed major variation in expression of intracellular conserved motifs. Expression levels of PCDH1 transcripts encoding exon 1-2 were 4-fold higher, and transcripts encoding exon 3-4 were 15-fold higher in freshly isolated bronchial epithelial cells than in submerged cultures. PCDH1 mRNA (3- to 8-fold) and protein levels (2- to 3-fold) were strongly up-regulated during mucociliary differentiation of primary bronchial epithelial cells in ALI cultures. In summary, PCDH1 transcripts display remarkable variability in expression of conserved intracellular signaling domains. Enhanced PCDH1 expression levels strongly correlate with differentiation of bronchial epithelial cells.

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Protocadherin of the Liver, Kidney, and Colon Associates with Detergent-resistant Membranes during Cellular Differentiation

Cited by 8 publications

References 41 publications

Cadherin-related protein 24 induces morphological changes and partial cell polarization by facilitating direct cell-cell interactions

Cadherin-related protein 24 induces morphological changes and partial cell polarization by facilitating direct cell-cell interactions

Long range epigenetic silencing is a trans‐species mechanism that results in cancer specific deregulation by overriding the chromatin domains of normal cells

Characterization of protocadherin‐1 expression in primary bronchial epithelial cells: association with epithelial cell differentiation

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