Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:Q9UIJ5 (Rec)
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Ultrastructural and cytochemical methods were utilized to study the human Fallopian tube fimbrial epithelium during the different stages of the menstrual cycle. Alkaline phosphatase reaction product was located along the apical and lateral plasma membranes of the secretory cells only, regardless of the stage of the cycle. The ciliated cells were almost devoid of any reaction product at all stages of the cycle. Acid phosphatase reaction product depicted the lysosomes. These appeared as electron-dense bodies, of almost equal numbers in the ciliated and the secretory cells at all stages of the cycle. Thus the number of lysosomes did not vary appreciable during the different stages of the menstrual cycle. Many lipid droplets were found in both cells; these were rimmed by acid phosphatase reaction product, and some were partially enveloped by electron-dense bodies containing acid phosphatase deposits. Acid phosphatase deposits were also found on the inner face of Golgi vesicles.
Anat Rec 1982 May
PMID:Ultrastructural localization of alkaline and acid phosphatases in the human fallopian tube epithelium during the menstrual cycle. 710 26

The three-dimensional architecture of the myosalpinx in the mare was investigated by means of scanning electron microscopy (SEM) after removal of interstitial connective tissue with NaOH digestion. In the extramural portion of the tubo-uterine junction (TUJ), isthmus, and ampulla, the myosalpinx architecture is represented by a unique muscular structure which runs from the mesosalpinx to the base of the inner mucous folds. This unique muscular structure consists mainly of bundles of muscular fibers independent of one another, which show a multiple spatial arrangement and form a complex network. Such a muscular architecture is likely more suitable for stirring rather than pushing the embryos and gametes through the Fallopian tube.
Anat Rec 2002 Jul 01
PMID:Three-dimensional architecture of the myosalpinx in the mare as revealed by scanning electron microscopy. 1211 74