Maternal mRNA Expression in Early Development: Regulation at the 3' End

Enzyme ◽  
1990 ◽  
Vol 44 (1-4) ◽  
pp. 129-146 ◽  
Author(s):  
Jeannie Paris ◽  
L. Lynn McGrew ◽  
Joel D. Richter
Keyword(s):  
Mrna Expression ◽  
Early Development ◽  
Maternal Mrna ◽  
Development Regulation

Synthesis and phosphorylation of uvomorulin during mouse early development

Development ◽  
1992 ◽  
Vol 115 (1) ◽  
pp. 313-318 ◽  
Author(s):  
M. Sefton ◽  
M.H. Johnson ◽  
L. Clayton
Keyword(s):  
Cell Adhesion ◽  
Early Development ◽  
Adhesion Molecule ◽  
Cell Adhesion Molecule ◽  
Blastocyst Stage ◽  
Embryonic Stage ◽  
Cell Stage ◽  
Mouse Oocytes ◽  
Maternal Mrna ◽  
Embryonic Genome

The cell adhesion molecule, uvomorulin, is synthesised in both the 135 × 10(3) M(r) precursor and 120 × 10(3) M(r) mature forms on maternal mRNA templates in unfertilized and newly fertilized mouse oocytes. Synthesis on maternal message ceases during the 2-cell stage to resume later on mRNA encoded presumptively by the embryonic genome. Uvomorulin is detectable by immunoblotting at all stages upto the blastocyst stage, but shows variations in its total amount and processing with embryonic stage. Whilst only trace levels of phosphorylated uvomorulin are detectable in early and late 4-cell embryos, uvomorulin in 8-cell embryos is phosphorylated.

Analysis of differential maternal mRNA expression in developmentally competent and incompetent bovine two-cell embryos

2003 ◽  
Vol 67 (2) ◽  
pp. 136-144 ◽  
Author(s):  
Trudee Fair ◽  
Madeline Murphy ◽  
Dimitrios Rizos ◽  
Catherine Moss ◽  
Finian Martin ◽  
...  
Keyword(s):  
Mrna Expression ◽  
Maternal Mrna

scholarly journals Differential accumulation of ribonucleotide reductase subunits in clam oocytes: the large subunit is stored as a polypeptide, the small subunit as untranslated mRNA.

1986 ◽  
Vol 103 (6) ◽  
pp. 2129-2136 ◽  
Author(s):  
N Standart ◽  
T Hunt ◽  
J V Ruderman
Keyword(s):  
Enzyme Activity ◽  
Early Development ◽  
Ribonucleotide Reductase ◽  
Reductase Activity ◽  
Large Subunit ◽  
Small Subunit ◽  
Maternal Mrna ◽  
Molecular Masses ◽  
Maternal Mrnas ◽  
Ribonucleotide Reductase Activity

Within minutes of fertilization of clam oocytes, translation of a set of maternal mRNAs is activated. One of the most abundant of these stored mRNAs encodes the small subunit of ribonucleotide reductase (Standart, N. M., S. J. Bray, E. L. George, T. Hunt, and J. V. Ruderman, 1985, J. Cell Biol., 100:1968-1976). Unfertilized oocytes do not contain any ribonucleotide reductase activity; such activity begins to appear shortly after fertilization. In virtually all organisms, this enzyme is composed of two dissimilar subunits with molecular masses of approximately 44 and 88 kD, both of which are required for activity. This paper reports the identification of the large subunit of clam ribonucleotide reductase isolated by dATP-Sepharose chromatography as a relatively abundant 86-kD polypeptide which is already present in oocytes, and whose level remains constant during early development. The enzyme activity of this large subunit was established in reconstitution assays using the small subunit isolated from embryos by virtue of its binding to the anti-tubulin antibody YL 1/2. Thus the two components of clam ribonucleotide reductase are differentially stored in the oocyte: the small subunit in the form of untranslated mRNA and the large subunit as protein. When fertilization triggers the activation of translation of the maternal mRNA, the newly synthesized small subunit combines with the preformed large subunit to generate active ribonucleotide reductase.

scholarly journals Maternal mRNA expression levels of H19 are inversely associated with risk of macrosomia

2014 ◽  
Vol 3 ◽  
pp. 525-530 ◽  
Author(s):  
Hua Jiang ◽  
Yang Yu ◽  
Pengcheng Xun ◽  
Jun Zhang ◽  
Guanghua Luo ◽  
...  
Keyword(s):  
Mrna Expression ◽  
Expression Levels ◽  
Maternal Mrna ◽  
Mrna Expression Levels

GAP-43 mRNA expression in early development of human nervous system

1996 ◽  
Vol 38 (1) ◽  
pp. 145-155 ◽  
Author(s):  
Selma Kanazir ◽  
Sabera Ruzdijic ◽  
Slobodanka Vukosavic ◽  
Sanja Ivkovic ◽  
Ana Milosevic ◽  
...  
Keyword(s):  
Nervous System ◽  
Mrna Expression ◽  
Early Development ◽  
Human Nervous System

Developmental expression of the creatine kinase isozyme system of Xenopus: maternally derived CK-IV isoform persists far beyond the degradation of its maternal mRNA and into the zygotic expression period

Development ◽  
1990 ◽  
Vol 108 (3) ◽  
pp. 507-514
Author(s):  
J. Robert ◽  
J. Wolff ◽  
H. Jijakli ◽  
J.D. Graf ◽  
F. Karch ◽  
...  
Keyword(s):  
Creatine Kinase ◽  
Differential Expression ◽  
Early Development ◽  
Developmental Expression ◽  
Developmental Profile ◽  
Maternal Mrna ◽  
Skeletal Musculature ◽  
Adult Pattern ◽  
Specific Manner ◽  
Isozyme System

The differential expression of the multilocus CK isozyme system throughout development of the two Xenopus species X. laevis and X. borealis was investigated. A cDNA containing the nearly complete coding sequence of the CK-IV subunit of X. laevis was isolated and sequenced. Early development of X. laevis proceeds with a stock of maternally derived CK-IV/IV isozyme. While the mRNA declines rapidly after fertilization and disappears before neurulation, maternal CK-IV/IV isozyme is active far beyond the onset of zygotic expression and is still detectable when tadpoles start feeding. Zygotic expression of CK-IV begins after neurulation, at stage 22/24, and seems to start simultaneously with that of another gene, CK-III. Modulation in the expression of these two genes and the appearance of two other isoforms, the CK-I and CK-II/III isozymes, take place during development in a tissue-specific manner. During metamorphosis, the CK phenotypes of eyes and skeletal musculature undergo additional changes. The final adult pattern only appears several weeks after metamorphosis. The presumed orthologous CK isozymes of X. borealis show a developmental profile similar to that of X. laevis, except that CK-II/II is equally present in oocytes and during early development, in addition to CK-IV/IV isozyme. These results show that the expression of each of the four CK genes of Xenopus is under differential developmental control.

scholarly journals Maternal mRNA and early development in Fucus serratus

1992 ◽  
Vol 2 (4) ◽  
pp. 619-622 ◽  
Author(s):  
A. K. Masters ◽  
A. D. Shirras ◽  
A. M. Hetherington
Keyword(s):  
Early Development ◽  
Maternal Mrna ◽  
Fucus Serratus

Expression of early development-related genes in bovine nuclear transferred and fertilized embryos

Zygote ◽  
2003 ◽  
Vol 11 (4) ◽  
pp. 355-360 ◽  
Author(s):  
Sang Hyun Park ◽  
Soo-Bong Park ◽  
Nam-Hyung Kim
Keyword(s):  
Mrna Expression ◽  
Early Development ◽  
Interleukin 6 ◽  
Nuclear Transfer ◽  
Glucose Transporter ◽  
Expression Patterns ◽  
Glucose Transporter 1 ◽  
E Cadherin

Cloning efficiency following somatic cell nuclear transfer is very low. In order to obtain insights into this problem, mRNA expression patterns of early development-related genes in nuclear transferred embryos were compared with those obtained from in vivo and in vitro fertilization. Semiquantitative reverse-transcription polymerase chain reaction assay was used to compare the gene expression of, the cell adhesion protein E-cadherin, interleukin -6, heat-shock protein 70.1 and bos taurus apoptosis regulator box-a (Bax). The relative abundances of glucose transporter-1, E-cadherin and interleukin-6 were significantly (P<0.05) higher in in vitro fertilized morulae than in vivo derived morulae. Transcription of the gene encoding octamer-binding transcription factor 4 was higher in blastocysts obtained from in vivo fertilization than in those from in vivo blastocysts. The transcript for Bax was markedly upregulated in blastocysts derived from in vitro production and nuclear transfer procedures compared with in vivo fertilization. These results suggest that alterations in mRNA expression of early development genes are more associated with in vitro culture condition than the nuclear transfer procedure itself.

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