Abstract
At the transition between growth plate cartilage and the endochondral bone region, transverse septa are being eroded to allow the advance of invasive capillaries. To find out whether resorption is due to proteinase activity, tissue sections prepared from the growth plate/metaphyseal interface of young rats were immunostained with antibodies to the cysteine proteinase cathepsin B. Intense staining was found in a cell that is associated with the growing portion of the invasive capillaries and extends between them and the transverse septum. This cell has a single nucleus, actively synthesizes protein, and shows two other characteristic features: the cytoplasm is packed with multivesicular and dense bodies rich in cathepsin B, and the cell apex ends in a ruffled border extending into the transverse septum and signs of dissociated extracellular matrix. Even though the ruffled border resembles that of the osteoclast, the cell was not immunostained by a monoclonal antibody that recognizes a 97 KD protein known as ED1 which characterizes rat osteoclasts, monocytes, and macrophages. Therefore, this distinctive cell produces the proteinase cathepsin B and appears to be involved in the resorption of the transverse septum. The cell has been named the "septoclast."