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Morphological Studies on the Resistance of Cartilage to Invasion by Osteosarcoma Cells in Vitro and in Vivo¹

Departments of Biochemistry [K. E. K], Pathology [B. U. P], and Orthopedic Surgery [K. E. K., L. S.], Rush Medical College and Rush College of Health Sciences, Rush Presbyterian-St. Luke's Medical Center, Chicago, Illinois 60612

Cartilage-bone explants from human ribs and phalanges were simultaneously cultured on Millipore membranes with either human osteosarcoma cells (TE-85) or human primary foreskin fibroblasts. The explant-tumor cell interfaces were histologically compared with biopsies from an osteogenic sarcoma. In both specimens, bone spicules were embedded in tumor cell clusters. Irregularities and lacunae in the spicule surfaces with closely attached tumor cells were considered morphological evidence of direct bone erosion by osteosarcoma cells. In contrast to bone, articular and epiphyseal cartilage resisted tumor invasion. Osteosarcoma cells infiltrated the cartilage matrix only to areas that were occupied by vascularized mesenchyme, such as the capillary loops in the growth plate and the nutrient cartilage canals. Inhibition of tumor cell growth underneath the explant on the bottom of the Petri dish and the delayed outgrowth on Millipore membrane areas occupied previously by cartilage explants suggest the release of substances that inhibit growth and proliferation of tumor cells. No such effects have been observed in control cultures with fibroblasts.

These observations are similar to those obtained in previous studies on the resistance of cartilage to vascular invasion. Since collagenolytic activities have been demonstrated in both endothelial and osteosarcoma cells, it has been suggested that these cells share the mechanisms of invasion involving matrix destruction by collagen breakdown. Collagenolytic activity can be inhibited by a cartilage-derived collagenase inhibitor. The capacity of tumor cells to invade a tissue may therefore depend not only on their ability to elaborate collagenase but also on local regulation of such enzyme activity by inhibitory substances.

¹ This work was supported by NIH Grant CA-21566 and in part by Grant AM-09132.

² To whom requests for reprints should be addressed, at Department of Orthopedic Surgery, Rush Medical College, 600 South Paulina Street, Chicago, Ill. 60612.

Received 8/ 4/77. Accepted 11/ 7/77.

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