scholarly journals Immunolocalization in three dimensions: immunogold staining of cytoskeletal and nuclear matrix proteins in resinless electron microscopy sections.

1990 ◽  
Vol 87 (6) ◽  
pp. 2259-2263 ◽  
Author(s):  
J. A. Nickerson ◽  
G. Krockmalnic ◽  
D. C. He ◽  
S. Penman
Keyword(s):  
Electron Microscopy ◽  
Nuclear Matrix ◽  
Three Dimensions ◽  
Matrix Proteins ◽  
Immunogold Staining ◽  
Nuclear Matrix Proteins

scholarly journals Ultrastructural localization of nuclear matrix proteins in HeLa cells using silver-enhanced ultra-small gold probes.

1991 ◽  
Vol 39 (8) ◽  
pp. 1035-1045 ◽  
Author(s):  
A de Graaf ◽  
P M van Bergen en Henegouwen ◽  
A M Meijne ◽  
R van Driel ◽  
A J Verkleij
Keyword(s):  
Hela Cells ◽  
Nuclear Matrix ◽  
Matrix Protein ◽  
Ultrastructural Localization ◽  
Matrix Proteins ◽  
Cell Permeabilization ◽  
Immunogold Staining ◽  
Thin Sections ◽  
Nuclear Matrix Proteins ◽  
Dna And Rna

We describe a method for immunogold staining of nuclear matrix proteins using ultra-small gold particles. The nuclear matrix of HeLa cells is obtained by two fractionation steps: (a) cell permeabilization with Triton X-100 to isolate the cytoskeleton, and (b) nuclease digestion followed by an incubation in 0.25 M ammonium sulfate to isolate the nuclear matrix. To prevent redistribution of internal matrix proteins during nuclear matrix preparation, pre-fixation with 0.1% acrolein was performed. Under this condition up to 80% of protein and 90% of DNA and RNA could be removed on nuclear matrix isolation, without redistribution of internal nuclear matrix proteins. For immunogold labeling, 1-nm gold probes appeared to be required to obtain optimal penetration into the nucleus. These particles can be visualized after silver enhancement. After gold labeling the matrices are stained, embedded in Epon, and ultra-thin sections are prepared for examination in the electron microscope. The applicability of this method is examplified by the localization of a 125 KD internal nuclear matrix protein and the lamins A and C in nuclear matrix preparations of HeLa cells.

Progress in ultrastructural and molecular analysis of the nuclear matrix

1992 ◽  
Vol 50 (1) ◽  
pp. 508-509
Author(s):  
Edward G. Fey
Keyword(s):  
Electron Microscopy ◽  
Nuclear Matrix ◽  
Structure And Function ◽  
Matrix Proteins ◽  
Rna Transcription ◽  
Nuclear Matrix Proteins ◽  
The Past ◽  
And Function

In the past few years, considerable advances have been made regarding the structure and function of the nuclear matrix. In the first half of this presentation, the field of nuclear matrix research will be summarized. Emphasis will be placed on those studies where molecular interactions are demonstrated in situ utilizing high resolution light and/or electron microscopy. Studies demonstrating the role of the nuclear matrix in DNA synthesis and replication, RNA transcription and processing, and the binding of matrix attachment regions to specific nuclear matrix proteins will be summarized.

Differentiation-Specific Nuclear Matrix Proteins Cross-linked to DNA bycis-Diammine Dichloroplatinum

1998 ◽  
Vol 238 (1) ◽  
pp. 216-219 ◽  
Author(s):  
Elena Mattia ◽  
Margherita Eufemi ◽  
Silvia Chichiarelli ◽  
Mara Ceridono ◽  
Anna Ferraro
Keyword(s):  
Nuclear Matrix ◽  
Matrix Proteins ◽  
Nuclear Matrix Proteins

scholarly journals Interactions of rat repetitive sequence MspI8 with nuclear matrix proteins during spermatogenesis.

1996 ◽  
Vol 43 (2) ◽  
pp. 319-324
Author(s):  
J Rogoliński ◽  
P Widłak ◽  
J Rzeszowska-Wolny
Keyword(s):  
Nuclear Matrix ◽  
Blot Analysis ◽  
Repetitive Sequence ◽  
Matrix Proteins ◽  
Velocity Sedimentation ◽  
Nuclear Matrix Proteins ◽  
Rat Testis ◽  
Sedimentation Technique

Using the Southwestern blot analysis we have studied the interactions between rat repetitive sequence MspI8 and the nuclear matrix proteins of rat testis cells. Starting from 2 weeks the young to adult animals showed differences in type of testis nuclear matrix proteins recognizing the MspI8 sequence. The same sets of nuclear matrix proteins were detected in some fractions enriched in spermatocytes and spermatides and obtained after fractionation of testis cells of adult animals by the velocity sedimentation technique.

scholarly journals DNA and proteins of the nuclear matrix are the main targets of benzo[a]pyrene's action in rat hepatocytes.

1993 ◽  
Vol 40 (4) ◽  
pp. 559-562 ◽  
Author(s):  
P Widłak ◽  
J Rzeszowska-Wolny
Keyword(s):  
Molecular Weight ◽  
Dna Adducts ◽  
Dna Sequences ◽  
Nuclear Matrix ◽  
Rat Hepatocytes ◽  
The Other ◽  
Matrix Proteins ◽  
Nuclear Matrix Proteins ◽  
Cultured Rat Hepatocytes ◽  
High Molecular Weight Proteins

The binding of [14C]benzo[a]pyrene (B[a]P) to DNA and proteins in total nuclei and subnuclear fractions of cultured rat hepatocytes was compared. The main targets of B[a]P were non-histone high molecular weight proteins of the nuclear matrix and DNA sequences attached to this structure. Following 24 h exposure to B[a]P the amounts of adducts in the nuclear matrix DNA and proteins were twice as high as in total nuclei. After withdrawal of the carcinogen containing medium the level of B[a]P-induced adducts gradually decreased but always remained the highest in the nuclear matrix proteins. Removal of adducts from the nuclear matrix DNA was more efficient than from the other DNA fractions, and 72 h after exposure to the carcinogen the level of DNA adducts in this fraction was similar to that in total nuclei.

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