Polyadenylated RNA of mouse ova and loss of maternal RNA in early development

Bachvarova, Rosemary F.; Leon, Victor De

doi:10.1016/0012-1606(80)90048-2

Cited by 199 publications

(93 citation statements)

References 18 publications

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“…Based on observations of other species this maternal RNA would constitute a store of developmental molecules for early embryo development. The progressive decline in RNA content between the 1, 2 and 4 cell embryo stages ( fig.1), is consistent with the view that stored RNAs are being utilized during the initial phase of early cleavage development (see also Bachvarova and De Leon 1980).…”

supporting

confidence: 87%

Relative changes in the RNA contents of oocytes and preimplantation embryos of the mouse

Moore¹,

Lintern‐Moore²,

Scott-Murphy³

1981

Reprod. Nutr. Dévelop.

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supporting

confidence: 87%

Relative changes in the RNA contents of oocytes and preimplantation embryos of the mouse

Moore¹,

Lintern‐Moore²,

Scott-Murphy³

1981

Reprod. Nutr. Dévelop.

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“…We have detected all three splicing forms of APP at every developmental stage examined, including both the ovulated oocyte and late two-cell embryo. While the mouse oocyte carries a large store of maternal mRNAs, these in general are degraded by the first cleavage division, and transcription from the embryonic genome is activated in the late two-cell embryo (37,40). Detection of APP at both stages implies either that the maternal APP mRNA is not totally degraded by the late two-cell stage or that the gene encoding APP is one of the earlier genes transcribed from the embryonic genome.…”

Section: Discussionmentioning

confidence: 99%

Expression of the amyloid precursor protein gene in mouse oocytes and embryos.

Fisher

Gearhart

Oster-Granite

1991

Proc. Natl. Acad. Sci. U.S.A.

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The amyloid precursor protein (APP) is thought to be processed aberrantly to yield the major constituent of the amyloid plaques observed in the brains of patients with Alzheimer disease and Down syndrome. However, the gene encoding APP is expressed widely in normal human tissues and in adult and fetal mouse tissues and is alternately spliced in a tissue-specific pattern in the adult. There is evidence that APP may function as a growth factor and as a mediator of cell adhesion and in these roles could be important in morphogenesis. As a step toward determining the role of APP in development and in determining how the adult pattern of tissuespecific splicing is established, we have used reverse transcription and the polymerase chain reaction to demonstrate APP expression in mouse oocytes, preimplantation embryos, and postimplantation embryonic stages to the late embryonic period. All three splicing forms described in mouse were present at each stage, although there were changes in the ratios of the splicing forms at different stages. Screens for APP clones in embryonic cDNA libraries from the egg cylinder stage and the early somite stage were used to confirm the results of the polymerase chain reaction, and APP clone abundance was found to increase 10-fold between these two stages./3-Amyloid peptide is the main component of the neuritic and cerebrovascular amyloid plaques of patients with Alzheimer disease (AD) (1) and aging individuals with Down syndrome (DS) (2). Its 42-amino acid sequence is found as part of a 695-amino acid protein, the amyloid precursor protein (APP695) (3-6). APP is encoded by a gene mapped on human chromosome 21 and in the syntenic region of mouse chromosome 16 (7, 8). The /3-amyloid peptide includes portions of both the extracellular domain and the single membranespanning domain of APP, but it is not known how the full-length protein is processed to yield the short peptide. However, it must involve a change in the normal processing of the protein, since the full-length precursor is cleaved constitutively at a site within the /3-amyloid sequence (9). Two other forms of APP have been described, APP751 and APP770, which are identical to APP695 except for the inclusion of either one or two additional exons, respectively, in the mRNA (10)(11)(12). Inclusion of only the second of these exons results in another form, APP714, detected in several human tissues but at much lower levels than the first three forms (13). A fifth form, APP563, has been cloned from a human brain cDNA library; its deduced sequence is identical to APP751 for the first 543 amino acids and then diverges for the remaining 20 amino acids (14). APP563, a minor component of the total APP message in brain, lacks the membrane-spanning domain and presumably encodes a secreted protein. Total APP expression is highest in the brain (6); APP695 is expressed predominantly in neurons (15), whereas APP751 and APP770 have been detected in every adult tissue examined (6). In the mouse, only splicing forms corresponding to APP695, AP...

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“…About half of the transcripts found in two-cell embryos were not detected in oocytes and appear to represent a set of embryo-specific genes that are transcriptionally activated at the two-cell stage (Taylor and Piko, 1987). Between the eight-cell and blastocyst stages, maternal mRNA continues to decrease, and this is accompanied by an increased synthesis of embryonic mRNA (Bachvarova and DeLeon, 1980). Between the morula and blastocyst stages, recently synthesized embryonic mRNAs become more stable (Kidder and Pedersen, 1982), and protein synthesis begins to increase (Brinster et al, 1976).…”

Section: Mousementioning

confidence: 99%