Masters et al. (1985) purified and characterized the cerebral amyloid protein that forms the plaque core in Alzheimer
disease and in older persons with Down syndrome. The protein consists of multimeric aggregates of a
polypeptide of about 40 residues (4 kD). The amino acid composition, molecular mass, and NH2-terminal sequence of
this amyloid protein were found to be almost identical to those described for the amyloid deposited in the congophilic
angiopathy of Alzheimer disease and Down syndrome.
General function
Comment
Cellular localization
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Ovarian function
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Expression regulated by
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Ovarian localization
Granulosa, Follicular Fluid
Comment
[Kimura A, et al 2000 ] reported
amyloid precursor
protein (APP) expression using porcine ovary mRNA. The isolated cDNA clone and the clones
generated by 5'RACE spanned 3,051 bp containing the complete open reading
frame of APP which consisted of 770 amino acid residues. The expression of APP in
several porcine tissues was examined by Northern blot analysis. The ovaries
and adrenal glands showed a strong expression of the APP mRNA, as did the
granulosa cells from small and large follicles of the porcine ovary. RT-PCR
analyses using two primer sets revealed that the porcine ovary expressed at
least four types of APP mRNAs. Western blot analysis was conducted using the
extract of granulosa cells and the fluid of ovarian follicles, and the results
indicated that the follicular fluid contained soluble APP in relatively high
content. These results suggest that APP undergoes proteolytic processing
and/or degradation within the follicles during follicular development.