Expression of the Rho‐family GTPase gene <i>RHOF</i> in lymphocyte subsets and malignant lymphomas

Gouw, Launce; Reading, N. Scott; Jenson, Stephen D.; Lim, Megan S.; Elenitoba-Johnson, Kojo S.J.

doi:10.1111/j.1365-2141.2005.05481.x

Cited by 39 publications

(22 citation statements)

References 10 publications

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“…16) And the Rho GTPases have been reported to regulate the unlimited proliferation, invasion, and metastasis in some human tumors. 13,15) The RhoA signaling has been reported to be activated in the invasion or metastasis including, but not limited to, colorectal cancer, breast cancer, and prostate cancer. [28][29][30] In order to explore its pro-oncogenic role in cervical carcinoma, we manipulated the RhoA level in Hela cells by overexpressing or knockdowning RhoA.…”

Section: Discussionmentioning

confidence: 99%

“…Several Rho GTPases are upregulated in some human tumors, including RhoA, RhoC, Rac1, and so on. [13][14][15] And the upregulated Rho GTPases play their pro-oncogenic roles via stimulating cell cycle progression and regulating gene transcription, for example, in promoting Ras-induced transformation. 16) The induction of tumor vascularization is essential for tumors to grow beyond a certain size, and malignant cells release factors that promote angiogenesis from nearby pre-existing blood vessels.…”

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confidence: 99%

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Overexpression of RhoA promotes the proliferation and migration of cervical cancer cells

Liu

Chen

2014

Bioscience, Biotechnology, and Biochemistry

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The pro-oncogenic role of RhoA has been well identified in other cancers, but rarely in cervical cancer (CC), one of the main causes of cancer-related death in women. In the present study, we identified the overexpression of RhoA and its downstream effectors, ROCK-1 and ROCK-II, in CC specimens using western blotting. Then, we determined the effect of RhoA on the proliferation and migration of Hela cells, one of CC cell lines, by upregulating or downregulating the RhoA expression in Hela cells. We found that there was an overexpression of RhoA, ROCK-I/II in CC, which was associated with the progression of CC. And we confirmed that RhoA promoted the proliferation and migration of CC cells. In conclusion, we found a positive correlation among RhoA with the progression of CC by in vivo and in vitro evidences. A high RhoA expression in CC may predict a high metastatic potential of CC.

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Section: Discussionmentioning

confidence: 99%

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confidence: 99%

Overexpression of RhoA promotes the proliferation and migration of cervical cancer cells

Liu

Chen

2014

Bioscience, Biotechnology, and Biochemistry

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“…These include NF-kB, 18 BCL-11A, 19 BALassociated protein, 20 and RhoF. 21 Importantly, many proteins previously unknown to be expressed in tFL such as ribosomal S6 kinase, Wnt2 protein, betacatenin like protein1, and the eta (Z) isoform of protein kinase C (PKC) were identified in the FFPE sample.…”

Section: Discussionmentioning

confidence: 99%

Identification of proteins from formalin-fixed paraffin-embedded cells by LC-MS/MS

Crockett

Lin

Vaughn

et al. 2005

Laboratory Investigation

143

140

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There exists a need for robust approaches for tandem mass spectrometry (MS/MS)-based identification of proteins in formalin-fixed paraffin-embedded (FFPE) material. We demonstrate herein the identification of proteins in FFPE material using enzymatic cleavage for extraction of peptides from the FFPE specimen and liquid chromatography (LC) followed by MS/MS. We identified 324 proteins from a 3-year-old FFPE cell-block of a human lymphoma cell line. The identified proteins were assigned to the membrane, cytosol and nucleus, with diverse cellular functions. The results were comparable to those obtained with lysates from a fresh specimen of the lymphoma cell line. Western blotting analysis and immunofluorescence microscopy confirmed the expression of selected proteins. The functional significance of one protein (PKC g) was validated using a PKC inhibitory peptide which resulted in lymphoma cell death in vitro. The ability to identify proteins from FFPE specimens has significant implications for MS/MS-based proteomics of vast repositories of archival primary tissue samples for disease-related discovery research. Laboratory Investigation ( Keywords: bottom-up proteomics; formalin fixed; paraffin embedded; tandem mass spectrometry Formalin fixation and tissue embedding in paraffin wax is a universal approach for tissue processing prior to light microscopic evaluation. A major advantage afforded by formalin-fixed paraffin-embedded (FFPE) specimens is the preservation of cellular and architectural morphologic detail in tissue sections. 1 The standard buffered formalin fixative in which biopsy specimens are processed is an aqueous solution containing 37% formaldehyde and 10-15% methyl alcohol. Formaldehyde is a highly reactive dipolar compound that results in the formation of protein-nucleic acid and proteinprotein crosslinks in vitro. [1][2][3][4][5] FFPE specimens have not been routinely used for global mass spectrometry-based proteomic studies. This relates to the fact that formaldehyde-induced crosslinking also renders proteins relatively insoluble and unsuitable for routine biochemical extraction and analysis. This crosslinking effect has precluded protein extraction from FFPE for routine Western blotting analysis of protein expression. 2 Thus, while recently developed enzymatic and heatinduced antigen retrieval methods have facilitated the immunohistologic detection of proteins in tissue, many proteins are still not detectable using these approaches. 6,7 In addition, proteins lacking widely available antibodies to their formalin-resistant epitopes are largely undetectable by immunohistochemistry. Although recent advances in molecular biotechnology have permitted the global analysis of proteins expressed in various cellular and tissue systems, the diminished capacity to extract intact proteins has largely precluded the proteomic analysis of FFPE samples with definitive identification of the proteins present within cells and tissues in biopsy material.The development of strategies to permit utilization of the universa...

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“…Some studies demonstrated that Rif is up-regulated in a subset of transformed FLs (follicular lymphomas), and a significant percentage of FLs transformed to an aggressive DLBCL (diffuse large Bcell lymphoma) [27]. Other research has revealed that Rif is deleted in early-stage mycosis fungoides, which is the most frequent form of cutaneous T-cell lymphoma [28].…”

Section: Rif and Lymphocyte Morphologymentioning

confidence: 98%

The small Rho GTPase Rif and actin cytoskeletal remodelling

Fan

Mellor

2012

Biochemical Society Transactions

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The Rif GTPase is a recent addition to small Rho GTPase family; it shares low homology with other members in the family and evolutionarily parallels with the development of vertebrates. Rif has the conserved Rho GTPase domain structures and cycles between a GDP-bound inactive form and a GTP-bound active form. In its active form, Rif signals through multiple downstream effectors. In the present review, our aim is to summarize the current information about the Rif effectors and how Rif remodels actin cytoskeleton in many aspects.

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Expression of the Rho‐family GTPase gene RHOF in lymphocyte subsets and malignant lymphomas

Cited by 39 publications

References 10 publications

Overexpression of RhoA promotes the proliferation and migration of cervical cancer cells

Overexpression of RhoA promotes the proliferation and migration of cervical cancer cells

Identification of proteins from formalin-fixed paraffin-embedded cells by LC-MS/MS

The small Rho GTPase Rif and actin cytoskeletal remodelling

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