The Journal of Bone and Joint Surgery, Vol 68, Issue 4 521-526, Copyright © 1986 by Journal of Bone and Joint Surgery, Inc
S-100 protein in human cartilage lesions
AP Weiss and HD Dorfman
S-100 protein is an acidic calcium-binding protein that was originally
isolated from the mammalian central nervous system in 1965. Initially,
S-100 protein was thought to be specific to neuroectodermal tissues, but
its presence in chondrocytes was recently reported. This study is an
analysis of the distribution of S-100 protein in lesions of human cartilage
and its possible significance. Several cartilaginous tumors, both benign
and malignant, as well as normal epiphyseal growth plates, were examined
for S-100 protein by the immunoperoxidase technique. Each cartilaginous
lesion that was examined showed immunoreactivity for S-100 protein. The
staining product was noted only intracellularly. The highest intensity of
staining was seen in the hypertrophic chondrocytes of the zone of
provisional calcification in the growth plate and in the large chondrocytes
located adjacent to areas of matrix mineralization in cartilaginous tumors.
In normal epiphyseal growth plates, the intensity of staining increased in
chondrocyte cytoplasm as one moved from the proliferating columnar
chondrocytes through the zone of hypertrophic chondrocytes to the
hypertrophic, degenerating chondrocytes in the zone of provisional
calcification. In cartilaginous tumors, the cells of enchondroma and of the
cartilaginous cap of osteochondroma were more immunoreactive than those of
chondromyxoid fibroma. In benign chondroblastoma, the chondroblasts were
less reactive than the chondrocytes in areas of chondroid matrix
production. The latter areas of chondroblastomas showed stronger
immunoreactivity in the matrix-enclosed cells adjacent to areas of mineral
deposition. Among conventional chondrosarcomas, grade-I tumors showed
greater immunoreactivity of the chondrocyte cytoplasm than did those of a
higher grade, in which chondroid matrix production was less
abundant.(ABSTRACT TRUNCATED AT 250 WORDS)