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J. Biol. Chem., Vol. 265, Issue 23, 13650-13654, 08, 1990

Differences in targeting and secretion of cathepsins B and L by BALB/3T3 fibroblasts and Moloney murine sarcoma virus-transformed BALB/3T3 fibroblasts

C Achkar, QM Gong, A Frankfater and AS Bajkowski
Department of Biochemistry, Loyola University of Chicago, Stritch School of Medicine, Maywood, Illinois 60153.

BALB/3T3 fibroblasts (3T3) were observed to secrete latent, pepsin- activatable forms of cathepsin B and cathepsin L as well as an active form of beta-glucuronidase when cultured in the absence of serum. The secretion of these proteins was stimulated by the cation ionophore monensin: cathepsin B, 4.3-fold; cathepsin L, 7.2-fold; and beta- glucuronidase, 3.1-fold. These increases were accompanied by a 50% decline in cellular levels of the active forms of these enzymes and by the cellular accumulation of latent forms of cathepsin B and cathepsin L. Latent forms of beta-glucuronidase were not detected. In contrast, Moloney murine sarcoma virus-transformed BALB/3T3 fibroblasts (MMSV) secreted greatly increased amounts of latent cathepsin B (17-fold) and latent cathepsin L (27-fold), and moderately increased amounts of active beta-glucuronidase (2-fold) in a manner which was not further increased by monensin. The increased monensin-insensitive secretion of these lysosomal enzymes by MMSV cells may be due to a transformation- induced decrease in mannose 6-phosphate receptors. Thus, 3T3 cells bound the neoglycoconjugate pentamannosyl 6-phosphate-bovine serum albumin at 4 degrees C in a pentamannosyl 6 phosphate and mannose 6- phosphate-inhibitable manner, whereas MMSV cells showed no measurable cell surface mannose 6-phosphate receptor binding activity.
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