title: Studies on the human oocyte and its follicle. I. Ultrastructural and histochemical observations on the primordial follicle stage.
abstract: Oocytes in primordial ("resting") follicles in adult human ovaries contain a complex paranuclear structure identified by light microscopists as Balbiani's vitelline body. By electron microscopy this structure is composed of a mass of mitochondria with associated endoplasmic reticulum, multiple compound aggregates which form a ring around the cytocentrum, and a single stack or coil of annulate lamellae either attached to the nuclear membrane or free in the cytoplasm. The compound aggregates contain vacuoles and finely divided electron-opaque material. Evidence is presented for the probable transport of this material between the oocyte and its environment. The cytocentrum contains a central aggregate of amorphous electron-opaque deposits which appear to become periodically aligned on fine fibrils to form the long coarse fibers at the periphery of the cytocentrum. The apparent prevalence of annulate lamellae attached or adjacent to the nuclear membrane of oocytes in ovaries removed during the mid-follicular (estrogenic) phase of the cycle indicates the need for further study of a possible hormonal influence on the resting oocyte. By light microscopy phosphatases were not found within the oocyte, but adenosine-monophosphatase activity is present in the cortical cells surrounding primordial follicles, and also at the periphery of each primitive follicle cell, most prominently at the oocyte side. Glucose-6-phosphate dehydrogenase activity is present within the oocyte cytoplasm.
mesh_terms: D000227:Adenine Nucleotides / Q000378:metabolism; D000328:Adult; D003593:Cytoplasm; D004721:Endoplasmic Reticulum; D005260:Female; D005954:Glucosephosphate Dehydrogenase / Q000378:metabolism; D006056:Golgi Apparatus; D006651:Histocytochemistry; D006801:Humans; D008854:Microscopy, Electron; D008928:Mitochondria; D006080:Ovarian Follicle / Q000166:cytology*; D010063:Ovum / Q000166:cytology* / Q000201:enzymology; D010744:Phosphoric Monoester Hydrolases / Q000378:metabolism
chemical_list: D000227:Adenine Nucleotides; D005954:Glucosephosphate Dehydrogenase; D010744:Phosphoric Monoester Hydrolases