Origin and Roles of Nuclear Matrix Proteins. Specific Functions of the MAR-Binding Protein MeCP2/ARBP

1999 ◽  
Vol 9 (3-4) ◽  
pp. 311-318 ◽  
Author(s):  
Wolf H. Stratling ◽  
Fang Yu
Keyword(s):  
Nuclear Matrix ◽  
Binding Protein ◽  
Matrix Proteins ◽  
Nuclear Matrix Proteins ◽  
Protein Mecp2

scholarly journals Developmental association of the beta-galactoside-binding protein galectin-1 with the nuclear matrix of rat calvarial osteoblasts

1998 ◽  
Vol 111 (20) ◽  
pp. 3035-3043 ◽  
Author(s):  
J.Y. Choi ◽  
A.J. van Wijnen ◽  
F. Aslam ◽  
J.D. Leszyk ◽  
J.L. Stein ◽  
...  
Keyword(s):  
Nuclear Matrix ◽  
Osteoblast Differentiation ◽  
Matrix Protein ◽  
Binding Protein ◽  
Protein Composition ◽  
Matrix Proteins ◽  
Specific Gene ◽  
Two Dimensional Gel Electrophoresis ◽  
Nuclear Matrix Proteins ◽  
Differential Retention

The protein composition of the nuclear matrix changes significantly as the osteoblast matures from a proliferating pre-osteoblast to an osteocyte embedded in a mineralized matrix. These matrix protein are the result of developmental stage-specific gene expression during osteoblast differentiation. To isolate nuclear matrix proteins unique to the bone phenotype we analyzed nuclear matrix preparations from cultures of rat calvarial osteoblasts by high resolution two-dimensional gel electrophoresis at two different stages: proliferation (day 3) and differentiation (day 18, mineralized). We characterized one protein (14 kDa; pI 5.0), that was detectable only in the nuclear matrix of differentiated osteoblasts. By mass spectrometry and microsequencing, this protein was identified as the beta -galactoside-binding protein galectin-1. Both immunofluorescence staining of nuclear matrix preparations with the galectin-1 antibody and western blot analysis of subcellular fractions confirmed that galectin-1 is only associated with the nuclear matrix in differentiated osteoblasts as the result of differential retention. Galectin-1 protein and mRNA are present throughout osteoblast differentiation. Galectin-1 is present in the cytoplasmic and nuclear fractions in both proliferating and differentiated osteoblasts. However, its only stable binding is to the nuclear matrix of the differentiated osteoblast; but, in proliferating osteoblasts, galectin-1 is not retained in the nuclear matrix. Taken together, our results suggest that developmental association of galectin-1 with the nuclear matrix reflects differential subnuclear binding of galectin-1 during osteoblast differentiation.

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

Nuclear matrix proteins as biomarkers for breast cancer

2002 ◽  
Vol 2 (1) ◽  
pp. 23-31 ◽  
Author(s):  
Diana Lüftner ◽  
Kurt Possinger
Keyword(s):  
Breast Cancer ◽  
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.

Identification of nuclear matrix proteins tightly bound to soluble simian virus 40 chromosomes

Virology ◽  
1984 ◽  
Vol 134 (2) ◽  
pp. 406-420 ◽  
Author(s):  
Barry I. Milavetz ◽  
Tracy Hopkins-Davis ◽  
Cheryl M. Payne
Keyword(s):  
Nuclear Matrix ◽  
Simian Virus 40 ◽  
Simian Virus ◽  
Matrix Proteins ◽  
Nuclear Matrix Proteins
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