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Biomedical subjects

B Kotzur

Publications and source records attributed to B Kotzur.

2 recordsLinked to original sources

Round-headed human spermatozoa.

Ultrastructural investigation of two cases of round-headed spermatozoa from human ejaculates revealed the existence of two different pathomorphogenetic types. Case 1 represented round-headed spermatozoa of the Schirren and Holstein type caused by loss of the abnormally formed acrosome during spermiogenesis and the missing nuclear transformation. In case 2 a primary maturing inhibition was responsible for the round-headed feature of the spermatozoa; the normally flattened, conical nucleus and acrosomal cap were surrounded by huge droplets of ample cytoplasm. Secondary degenerative changes contributed to the decreased motility of these round-headed spermatozoa. Therapeutic trials for this oligospermic patient showed that an increase in cell count to values in the low-normal range and a drastic reduction in the percentage of round-headed cells (from 80% to 47%) could be achieved. The Schirren and Holstein type, however, must be regarded as absolutely infertile due to the absence of an acrosome and its intrinsic enzymes.

Acrosome↗

[Nodular cutaneous amyloidosis. Clinical, histopathological and ultrastructural findings].

A case of nodular amyloidosis cutis of the face with minimal deposits of amyloid in the rectum is reported with respect to clinical, histopathological, and ultrastructural findings. A discussion of the problem of systematization in nodular amyloidoses is included. By electron microscopy, the principal similarity of the ultrastructure of amyloid is stressed again. Amyloid in this case of nodular amyloidosis cutis is thought to be synthesized by plasma cells which are found especially in the growing peripheral parts of the tumors. Fibroblasts with extremely dilated endoplasmic reticulum are almost totally surrounded by the fibrillar masses of amyloid within the tumor. Unusual spindle-formed cisternae of Golgi bodies containing oriented coarse fibrils are found in the fibroblasts. They are thought to represent a disturbance of the secretion of tropocollagen to the interstitium due to the surrounding amyloid masses.

Amyloid↗