Where to Get Cathepsin L

Cathepsin L has been identified independently as a 39 kDa glycoprotein with acid-proteinase activity, termed MEP major excreted protein], which is secreted by malignantly transformed mouse fibroblasts. Chromatin undergoes developmentally-regulated structural and chemical changes as cells differentiate, which subsequently lead to differences in cellular function by altering patterns of gene expression.
Cathepsin L has been identified independently also as IL8 converting enzyme and as CP-2 [cycling protein-2]. Here we show that histone H3 is proteolytically cleaved at its N-terminus during ESC differentiation. Mason et al have shown that MEP is a catalytically active precursor of cathepsin L. To gain insight into chromatin alterations that occur during mammalian differentiation, we turned to a mouse embryonic stem cell (ESC) model.
Boujrad et al have identified a 70 kDa protein complex secreted from rat Sertoli cells that stimulates steroidogenesis by Leydig cells and ovarian granulosa cells. The cathepsin L gene is activated by a variety of growth factors (PDGF and EGF), tumor promoters (including v-ras, v-src and v-mos), and second messengers (cAMP).4,9-12 Expression of cathepsins is regulated by natural inhibitors of cathepsins including the pro-peptides of papain-like cysteine proteases,13 Cystatins, 14,15 and Stefin B.16,17 Squamous cell carcinoma antigen (SSCA)18 and human c-Haras p21 (related to Cystatin b) have been shown to specifically inhibit cathepsin L.19
Cathepsin L, a lysosomal endopeptidase expressed in most eukaryotic cells, is a member of the papain-like family of cysteine proteinases. This complex is a potent activator of steroidogenesis and may regulate steroid concentrations and, thus, germ cell development in both males and females. Cathepsin L plays a major role in antigen processing, tumor invasion and metastasis, bone resorption, and turnover of intracellular and secreted proteins involved in growth regulation. This comples has been shown to consist of TIMP-1 and the proenzyme form of cathepsin L..
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