Changes in Acidic Chromatin Proteins During Mammary Cell Differentiation

1973 ◽  
Vol 51 (8) ◽  
pp. 1167-1176 ◽  
Author(s):  
Nobuyuki Kadohama ◽  
Roger W. Turkington
Keyword(s):  
Cell Differentiation ◽  
Sodium Dodecyl ◽  
Mammary Epithelial ◽  
Chromatin Protein ◽  
Cell Nuclei ◽  
Culture Studies ◽  
Proposed Model ◽  
Mammary Cell ◽  
Chromatin Proteins ◽  
Prolactin Synthesis

Chromatin was prepared from mouse mammary epithelial cell nuclei and histones were removed by extraction with 2.0 M NaCl, pH 6.0. Electrophoresis of the residual acidic chromatin proteins in polyacrylamide gels containing sodium dodecyl sulfate revealed a heterogeneous banding pattern which was tissue specific. Six or more bands among the proteins present in differentiated, lactational cells were not detectable in undifferentiated, virginal cells.In organ culture studies insulin stimulated the incorporation of 3H-tryptophan or 3H-aspartic acid and 3H-leucine into all electrophoretic components of the mammary acidic chromatin protein. Two peak rates of synthesis, preceding and following the peak rate of DNA synthesis, were observed. Synthesis was unaffected by hydrocortisone or prolactin. Synthesis of the six bands characteristic of the lactational cells was initially undetectable in undifferentiated, virginal cells, but was induced after incubation with insulin for 42 h. These results, taken in correlation with previous studies on this system, are consistent with a proposed model in which new species of acidic chromatin proteins may participate in chromatin reconstitution during mammary cell differentiation.

A Disappearance of a 24-kDa Acid-Soluble Protein from Liver Chromatin of Normal and Starved Hens Following ᴅ-Galactosamine Administration

1985 ◽  
Vol 40 (11-12) ◽  
pp. 798-805 ◽  
Author(s):  
Jan Pałyga
Keyword(s):  
Gel Electrophoresis ◽  
Rna Synthesis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Two Dimensional ◽  
Chromatin Protein ◽  
Ionic Detergent ◽  
Liver Chromatin ◽  
Chromatin Proteins ◽  
Triton X

Abstract Normal and starved adult chickens were injected intraperitoneally with ᴅ-galactosamine hydro­ chloride (0.5 g/kg body weight) and 6 h later liver chromatin acid-soluble proteins were isolated. These proteins were resolved by a two-dimensional polyacrylamide gel electrophoresis in the presence of non-ionic detergent, Triton X-100, in the first dimension and anionic detergent, sodium dodecyl sulfate, in the second dimension. Although spotting patterns of acid-soluble chromatin proteins were remarkably similar between normal and starved control birds and those receiving ᴅ-galactosamine, a disappearance of a 24-kDa protein after administration of this agent was found. Moreover, it was shown that this protein was also completely absent in the chicken erythrocyte chromatin which was known to be inactive in RNA synthesis.It seems that the disappearance of the 24-kDa chromatin protein may be associated with inhibiting of transcription in hen liver after ᴅ-galactosamine administration and during hen erythrocyte maturation.

GENE ACTIVATION IN MAMMARY CELLS

1972 ◽  
Vol 71 (2_Suppla) ◽  
pp. S346-S368 ◽  
Author(s):  
Roger W. Turkington ◽  
Nobuyuki Kadohama
Keyword(s):  
Cell Differentiation ◽  
Gene Transcription ◽  
Hormonal Regulation ◽  
Gene Activation ◽  
Milk Proteins ◽  
Mouse Mammary Gland ◽  
Nuclear Proteins ◽  
Mammary Cells ◽  
Alveolar Cells ◽  
Mammary Cell

ABSTRACT Hormonal activation of gene transcription has been studied in a model system, the mouse mammary gland in organ culture. Transcriptive activity is stimulated in mammary stem cells by insulin, and in mammary alveolar cells by prolactin and insulin. Studies on the template requirement for expression of the genes for milk proteins demonstrate that DNA methylation has an obligatory dependence upon DNA synthesis, but is otherwise independent from hormonal regulation of mammary cell differentiation. Incorporation of 5-bromo-2′deoxyuridine into DNA selectively inhibits expression of the genes for specific milk proteins. Undifferentiated mammary cells activate the synthesis of specific acidic nuclear proteins when stimulated by insulin. Several of these induced acidic nuclear proteins are undetectable in unstimulated undifferentiated cells, but appear to be characteristic components of the nuclei of differentiated cells. These results indicate that mammary cell differentiation is associated with a change in acidic nuclear proteins, and they provide evidence to support the concept that acidic nuclear proteins may be involved in the regulation of gene transcription and of mammary cell differentiation.

Late gestational hyperprolactinemia accelerates mammary epithelial cell differentiation that leads to increased milk yield1

2013 ◽  
Vol 91 (3) ◽  
pp. 1102-1111 ◽  
Author(s):  
M. K. VanKlompenberg ◽  
R. Manjarin ◽  
J. F. Trott ◽  
H. F. McMicking ◽  
R. C. Hovey
Keyword(s):  
Cell Differentiation ◽  
Epithelial Cell ◽  
Mammary Epithelial Cell ◽  
Mammary Epithelial ◽  
Epithelial Cell Differentiation

Covalent guanylyl intermediate formed by HeLa cell mRNA capping enzyme

1982 ◽  
Vol 2 (8) ◽  
pp. 993-1001
Author(s):  
D Wang ◽  
Y Furuichi ◽  
A J Shatkin
Keyword(s):  
Sodium Dodecyl Sulfate ◽  
Hela Cell ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Polyacrylamide Gel ◽  
Enzyme Complex ◽  
Cell Nuclei ◽  
Dodecyl Sulfate ◽  
Enzyme Intermediate

Guanylyltransferase, an enzyme that catalyzes formation of mRNA 5'-terminal caps, was isolated from HeLa cell nuclei. The partially purified preparation, after incubation with [alpha-32P]GTP, yielded a single radiolabeled polypeptide by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The guanylylated product was stable at neutral and alkaline pHs and had a pI of 4 by isoelectric focusing. An apparent molecular weight of approximately 68,000 was estimated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis under reducing conditions. The formation of a covalently linked, radiolabeled GMP-protein complex and the associated release of PPi required the presence of [alpha-32P]GTP and divalent cations and incubation between pH 7 and 9. Reaction with [beta-32P]GTP, [alpha-32P]CTP, [alpha-32P]UTP, or [alpha-32P]ATP did not label the approximately 68,000-dalton polypeptide. Phosphoamide linkage of the GMP-enzyme complex was indicated by its sensitivity to cleavage by acidic hydroxylamine or HCl and not by NaOH or alkaline phosphatase. Both formation of the GMP-enzyme intermediate and synthesis of cap structures of type GpppApG from GTP and ppApG were remarkably temperature independent; the rates of enzyme activity at 0 to 4 degrees C were 30% or more of those obtained at 37 degrees C. Radiolabeled GMP-enzyme complex, isolated by heparin-Sepharose chromatography from reaction mixtures, functioned effectively as a GMP donor for cap synthesis with 5'-diphosphorylated oligo- and polynucleotide acceptors. Alternatively, protein-bound GMP could be transferred to PPi to form GTP. The formation of a guanylylated enzyme intermediate appears to be characteristic of viral and cellular guanylyltransferases that modify eucaryotic mRNA 5' termini.

scholarly journals Image-based evaluation of the molecular events underlying HC11 mammary epithelial cell differentiation

2008 ◽  
Vol 382 (2) ◽  
pp. 122-128 ◽  
Author(s):  
Liang Shan ◽  
Renshu Zhang ◽  
Wanghai Zhang ◽  
Edward Lee ◽  
Rajagopalan Sridhar ◽  
...  
Keyword(s):  
Cell Differentiation ◽  
Epithelial Cell ◽  
Mammary Epithelial Cell ◽  
Mammary Epithelial ◽  
Epithelial Cell Differentiation ◽  
Molecular Events

Autocrine regulation of mammary cell differentiation

PROTOPLASMA ◽  
1990 ◽  
Vol 159 (2-3) ◽  
pp. 112-117 ◽  
Author(s):  
C. J. Wilde ◽  
C. H. Knight ◽  
C. V. P. Addey ◽  
D. R. Blatchford ◽  
M. Travers ◽  
...  
Keyword(s):  
Cell Differentiation ◽  
Autocrine Regulation ◽  
Mammary Cell
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