Chondroclasts and osteoclasts in bones of young rats: comparison of ultrastructural and functional features.
The aim of the present study was to characterize cells involved in resorption during endochondral bone formation. We investigated whether the cells involved in cartilage breakdown at the epiphyseal/metaphyseal border, i.e., chondroclasts, share the characteristics of bone/cartilage-resorbing osteoclasts at the metaphyseal/diaphyseal border regarding ultrastructural features and functional activity. Morphometric evaluation showed that chondroclasts do not form ruffled borders and clear zones, i.e., well-known resorption characteristics, to the same extent as osteoclasts, present at the lower metaphysis. Instead, chondroclasts tend to express an undifferentiated surface adjacent to the matrix, not structurally different from the basolateral plasma membrane. Tartrate-resistant acid phosphatase (TRAP) was used as a marker for functional activity. Immunohistochemical staining by light microscopy was strong in both chondroclasts and in osteoclasts. Furthermore, in situ hybridization revealed large amounts of TRAP mRNA in chondroclasts as well as in osteoclasts. Ultrastructural immunohistochemistry suggests extensive secretion of the TRAP enzyme in the ruffled border area of both chondroclasts and osteoclasts. Intracellular accumulation was seen particularly in chondroclasts, possibly as a consequence of a relative disinclination to develop a ruffled border. Thus, semiquantitative estimation of TRAP distribution showed an inverse relationship between extracellular and intracellular TRAP in chondroclasts and osteoclasts. These results indicate that chondroclasts and osteoclasts differ, not only with respect to location but possibly also by mode of action. The observed differences may reflect the maturation sequence of these multinucleated cells when associated with different metaphyseal trabecular surfaces.
Nordahl
J
J
Department of Immunology, Microbiology, Pathology and Infectious Diseases, Division of Pathology, Karolinska Institutet, Huddinge Hospital, S-141 86 Huddinge, Sweden.
Andersson
G
G
Reinholt
F P
FP
D000135:Acid Phosphatase / Q000032:analysis / Q000235:genetics*; D000818:Animals; D001846:Bone Development; D002356:Cartilage / Q000166:cytology* / Q000502:physiology / Q000648:ultrastructure; D002462:Cell Membrane / Q000648:ultrastructure; D002467:Cell Nucleus / Q000648:ultrastructure; D015726:Giant Cells / Q000166:cytology* / Q000502:physiology / Q000648:ultrastructure; D007150:Immunohistochemistry; D017403:In Situ Hybridization; D007527:Isoenzymes / Q000032:analysis / Q000235:genetics*; D008854:Microscopy, Electron; D010010:Osteoclasts / Q000166:cytology* / Q000502:physiology / Q000648:ultrastructure; D012333:RNA, Messenger / Q000032:analysis; D051381:Rats; D017207:Rats, Sprague-Dawley; D000071681:Tartrate-Resistant Acid Phosphatase; D014158:Transcription, Genetic
D007527:Isoenzymes; D012333:RNA, Messenger; D000135:Acid Phosphatase; D000071681:Tartrate-Resistant Acid Phosphatase