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Nuclear matrix proteins

Khanuja PS, Lehr JE, Soule HD, Gehani SK, Noto AC, Choudhury S, Chen R, Pienta KJ (1993) Nuclear matrix proteins in normal and breast cancer cells. Cancer Res 53(14) 3394-3398 Konety BR, Nangia AK, Nguyen T.S, Veitmeier BN, Dhir R, Acierno JS, Becich MJ, Hrebinko RL, Getzenberg RH (1998) Identification of nuclear matrix protein alterations associated with renal cell carcinoma. J Urol 159(4) 1359-1363... [Pg.227]

Raziuddin A, Court D, Sarkar FH, Liu YL, Kung H, Raziuddin R (1997) A c-erbB-2 promoter-specific nuclear matrix protein from human breast tumor tissues mediates NF-kappaB DNA binding activity. / Biol Chem 272(25) 15715-15720... [Pg.228]

Zhu Q, Gregg K, Lozano M, Liu J, Dudley JP (2000) CDP is a repressor of mouse mammary tumor virus expression in the mammary gland. J Virol 74(14) 6348-6357 Zweyer M, Riederer BM, Ochs RL, Fackelmayer FO, Kohwi-Shigematsu T, Bareggi R, Narducci P, Martelli AM (1997) Association of nuclear matrix proteins with granular and threaded nuclear bodies in cell lines undergoing apoptosis. Exp Cell Res 230(2) 325-336... [Pg.230]

Hrebinko, R. L, Getzenberg, R. H. (1998). Identification of nuclear matrix protein alterations associated with renal cell carcinoma./. Urol. 159, 1359-1363. [Pg.236]

Germain-Desprez, D., Bazinet, M., Bouvier, M. and Aubry, M. (2003) Oligomerization of transcriptional intermediary factor 1 regulators and interaction with ZNF74 nuclear matrix protein revealed by bioluminescence resonance energy transfer in living cells. J. Biol. Chem. 278, 22367-22373. [Pg.176]

Nuclear matrix proteins (NMPs) make up the internal structure of the nucleus. Their function has been associated with regulating key reactions in the nucleus, such as DNA reph-cation and RNA synthesis. The NMPs released by the cancer cell may be different from the normal cell. Furthermore, different types of cells may have different NMPs. Soluble NMPs could be detected in the sera of cancer patients in higher concentrations than the sera from normal subjects. In a multicenter foUow-up study (125 cystoscopies) of 90 patients with 33 pathologically confirmed TCC of the urinary tract, 70% of the 33 recurrences had urinary NMP greater than lOU/mL. Of the patients with NMP less than lOU/mL, 86% had no malignancy at subsequent cystoscopy. ... [Pg.775]

Eissa S, SweUam M, Sadek M, et al. Comparative evaluation of the nuclear matrix protein, fibronectin, urinary bladder cancer antigen and voided urine cytology in the detection of bladder tumors. J Urol 2002 168 465-69. [Pg.788]

Partin AW, Getzenherg RH, Carmichael MJ, et al. Nuclear matrix protein patterns in human benign prostatic hyperplasia and prostate cancer. Cancer Res 1993 53 744-49. [Pg.792]

The effector caspases (caspase-3, caspase-6, caspase-7) are responsible for the morphological and biochemical changes that mark apoptosis. Activation of the effector caspases occurs via cleavage of the proform by activated initiator caspases and often marks the point of no return for cell death. Substrates for effector caspases include the caspases themselves (autoactivation), cytoskeletal components (i.e., actin, fodrin, and cytokeratins), poly (ADP-ribose) polymerase (PARP), and nuclear matrix proteins like Lamin B. Detection of caspase-3 expression by immunohistochemistry has been studied extensively due to its apical position in the effector caspase cascade (7-9,11-16). As with the initiator caspases, it is important to determine which form of the enzyme is recognized by the spe-... [Pg.64]

The nuclear matrix. The lipid bilayers, the histones and other soluble proteins, and the DNA can all be removed from nuclei by exfracfion and enzymatic digestion. An insoluble residue, the nuclear matrix, is left. Largely protein in nature, this matrix is spread throughout the nucleus. Remnants of the membranes remain in the form of profeins that were in or along the bilayer. The nucleolus is clearly defined. The DNA appears to be bound to the nuclear matrix proteins. A specific 320-kb piece of a Drosophila chromosome has been mapped and used fo locate nontran-scribed scaffold (or mafrix) affachmenf regions of DNA bound to matrix proteins. These were found af intervals of 26-112 kb, fhe infervening loops confain-ing up to five or more A 120-kDa... [Pg.622]

Brotherton, T., Zenk, D., Kahanic, S. Reneker, J. (1991). Avian nuclear matrix proteins bind very tightly to cellular DNA of jS-globin gene enhancer in a tissue-specific fashion. Biochemistry, 30, 5845—50. [Pg.234]

Sun, J.-M., Hendzel, M.J. Davie, J.R. (1992). Nuclear matrix proteins bind very tightly to specific regions of the chicken histone H5 gene. Biochem. Cell Biol., 70, 822-9. [Pg.260]

Malanga M, Farina B. Noncovalent binding of poly(ADP-tibose) to nuclear matrix proteins Developmental changes and tissue specificity. Biol Chem 2000 381 1047-1053. [Pg.49]

Malanga M, Kleczkowska HE, Althaus FR. Selected nuclear matrix proteins are targets for poly(ADP-ribose)-binding. J Cell Biochem 1998 70 596-603. [Pg.49]

ADP-Ribosylation of Nuclear Matrix Proteins. Association of Poly(ADP-Ribose) Synthetase with the Nuclear Matrix... [Pg.222]

Fig. 3. Boronate-bound fraction of nuclear matrix proteins. Cells were labeled by 24 h incubation with methionine. PAGE as in Fig. 2. 1 Coomassie blue staining 2 autoradiography... Fig. 3. Boronate-bound fraction of nuclear matrix proteins. Cells were labeled by 24 h incubation with methionine. PAGE as in Fig. 2. 1 Coomassie blue staining 2 autoradiography...
A comparison of the data resulting from the labeling experiments with permeabilized cells with the data obtained by analysis of the boronate-binding fraction suggests the existence of several ADP-ribosylated nuclear matrix proteins. Beginning with a weak, but distinct electrophoretic band at approximately 300 kD, there are modified proteins at 300,220,140,116,73,69,64,60,51,46,43,41 kD. [Pg.227]

At this point, reference to the modification of nuclear matrix proteins by phosphorylation may be of interest. Gerace and Blobel [13] observed the phosphorylation of lamins in the course of the reversible depolymerization of the lamina during cell division. Henry and Hodge [14] reported the occurrence in the matrix of HeLa cells of about ten proteins with mol. wts. between 200 and 19 kD which could be phos-phorylated in vivo and in vitro. [Pg.227]


See other pages where Nuclear matrix proteins is mentioned: [Pg.611]    [Pg.220]    [Pg.222]    [Pg.223]    [Pg.225]    [Pg.225]    [Pg.226]    [Pg.228]    [Pg.1535]    [Pg.229]    [Pg.258]    [Pg.47]    [Pg.775]    [Pg.2287]    [Pg.618]    [Pg.44]    [Pg.3117]    [Pg.223]    [Pg.224]    [Pg.225]    [Pg.227]    [Pg.229]    [Pg.177]    [Pg.187]    [Pg.186]    [Pg.357]   
See also in sourсe #XX -- [ Pg.775 , Pg.2287 ]




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