Changes in the Cytoskeletal and Nuclear Matrix Proteins in Rat Hepatocyte Neoplastic Nodules in Their Relation to the Process of Transformation

Barboro, Paola; Alberti, Ingles; Sanna, Paola; Parodi, Silvio; Balbi, Cecilia; Allera, Caterina; Patrone, Eligio

doi:10.1006/excr.1996.0182

Cited by 28 publications

(19 citation statements)

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“…Aberrant nuclear and cellular structures are indicators for malignant transformation. Changes in the shape of the nucleus and the cytoskeleton perturb the nuclear matrix (Barboro et al 1996). These alterations in nuclear shape contribute to changes in DNA synthesis and gene expression (Benecke et al 1978;Gospodarowicz et al 1978).…”

Section: Nuclear Matrixmentioning

confidence: 96%

Subcellular localization of protein kinase CK2

Faust

Montenarh

2000

Cell and Tissue Research

219

168

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More than 46 years ago, Burnett and Kennedy first described protein kinase CK2 (formerly known as casein kinase 2) in liver extracts. Since then, protein kinase CK2 has been investigated in many organisms from yeast to man. It is now well established that protein kinase CK2 is a pleiotropic and ubiquitous serine or threonine kinase, which is highly conserved during evolution. A great number of studies deal with substrates of CK2, but the fact that over 160 substrates exist is more confusing than elucidatory. The holoenzyme is composed of two regulatory beta-subunits and two catalytic alpha- or alpha'-subunits. There is now increasing evidence for individual functions of the subunits that are different from their functions in the holoenzyme. Furthermore, more and more studies describe interacting partners of the kinase that may be decisive in the regulation of this enzyme. A big step forward has been the determination of the crystal structure of the two subunits of protein kinase CK2. Now the interactions of the catalytic subunit of CK2 with ATP as well as GTP and the interaction between the regulatory subunits can be explained. However, cellular functions of protein kinase CK2 still remain unclear. In the present review we will focus our interest on the subcellular localization of protein kinase CK2. Protein kinase CK2 is found in many organisms and tissues and nearly every subcellular compartment. There is ample evidence that protein kinase CK2 has different functions in these compartments and that the subcellular localization of protein kinase CK2 is tightly regulated. Therefore studying the subcellular localization of protein kinase CK2 may be a key to its function.

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Section: Nuclear Matrixmentioning

confidence: 96%

Subcellular localization of protein kinase CK2

Faust

Montenarh

2000

Cell and Tissue Research

219

168

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“…It is widely accepted that expression of CK18 affects nuclear organization then further impacts the integrity and stability of HCC cell nuclei. Reorganization of cytoskeleton perturbing the function of nuclear matrix was the suggested mechanism since Barboro et al reported that dramatic changes in the expression of both the nuclear matrix and IF proteins occur during transformation of rat hepatocyte nodules (20). Our latest study also showed that nuclear pleomorphism of hepatoma cells is correlated with the cytoplasmic disorganization of cytoskeleton caused by plectin deficiency; irregular nuclear shape resembled pleomorphic nuclei in cancer cells were observed in the plectin-knockdown liver cells (21).…”

Section: Histone H3 Co-immunoprecipitated With Ck18 In Human Hccmentioning

confidence: 74%

Cytokeratin 18-associated Histone 3 Modulation in Hepatocellular Carcinoma: A Mini Review

Lai

Cheng

Lai

et al. 2017

CGP

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Abstract.Hepatocellular carcinoma (HCC) is a cancer with high incidence and mortality in Taiwan. HCC cells exhibit different morphological features in divergent shapes and having pleomorphic nuclei from normal liver cells. Microtubules (MTs), intermediate filaments (IFs), and microfilaments (MFs) are major components of the cytoskeleton that are essential to maintain the integrity of eukaryotic cells (1). Proper cross-linking structures among these cytoskeletal proteins are crucial for intracellular architectures and normal cellular morphology. Plectin exhibits the binding sites accessible to IFs, MTs and MFs rendering the interaction with a variety of cytoskeletal components to maintain the integrity of the cytoskeletal network (2). The rope-like IFs have a mean diameter of 10 nm and mainly play a role in maintaining the shape and mechanical integrity of a cell (3). In human hepatocytes, a cytokeratin (CK) pair composed of CK8 (type II, 52 kD) and CK18 (type I, 45 kD) renders IFs (4). CKs are required for maintaining the integrity of hepatocytes (5). Altered expression of keratin genes were associated with chronic hepatitis, increased hepatocyte fragility and decreased bile secretion (6).In eukaryotic nucleus, the organization and packaging of DNA are achieved by addition of histone proteins to form chromatin. Post-translational modifications of histones, such as acetylation, phosphorylation, methylation and ADPribosylation, frequently alter the structure of chromatin (7). Epigenetic modifications of histone, especially acetylation status, altering the chromatin structure are involved in gene expression and further intervened in the pathogenesis of cancer. Two types of enzymes, including histone acetyltransferases (HATs) and histone deacetylases (HDACs), affect the acetylation status of histones. Recently it was reported that alterations in the activities of HDACs, as well as aberrant acetylation of histone, lead to diseases including cancer (8). HDACs catalyze histone deacetylation and repress transcription of specific genes, such as p21, resulting in cell-cycle activation and cell proliferation (9).The investigation of histones in our laboratory originated in a study of CK18, in which we found that CK18 was coimmunoprecipitated with histone H3 in human HCC, but not in normal liver. We speculated that both histone H3 and CK18 were modulated in HCC, which was shown in the co-219

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“…When some extractions or enzyme treatments are omitted, the composition and structure of the resulting product are modified, but not drastically. Many modifications of the original protocol have been proposed (Barboro et al, 1996;Kaufmann and Shaper, 1984;Kaufmann et al, 1981;Staufenbiel and Deppert, 1984), for example extraction of nuclei with 250 mM ammonium sulfate and presence of vanadyl ribonucleoside complexes in the reaction mixtures (Fey et al, 1984;Gerner et al, 1998). The presence of reducing or chelating agents usually decreases the number of proteins co-purifying with the nuclear matrix, but bivalent ions increase it (Kaufmann and Shaper, 1984;Kaufmann et al, 1981).…”

Section: Methods Of Nuclear Matrix Isolationmentioning

confidence: 98%