Children's Memorial Research Center, Cancer Biology and Epigenomics Program, Northwestern University Feinberg School of Medicine, Chicago, Illinois USA.
Cancer Biol Ther. 2010 Sep 1;10(5):457-66. doi: 10.4161/cbt.10.5.12534. Epub 2010 Oct 1.
Cathepsin D (CatD) is a lysosomal aspartyl endopeptidase originally considered a "house keeping enzyme" involved in the clearance of unwanted proteins. However, recent studies have revealed CatD's involvement in apoptosis and autophagy, thus signifying an important function in the proper development and maintenance of multi-cellular organs. In the mammary gland, matrix degradation and the remodeling process are orchestrated by proteolytic enzymes, but the role of CatD at distinct developmental stages has remained mostly unexplored. Based on our previous studies we sought to address the role of this endopeptidase in mammary gland development and remodeling. By employing a mouse model, we report a previously unidentified participation of CatD in different stages of mammary gland development. Our findings reveal that CatD undergoes distinct protein processing at different stages of mammary gland development, and this customized processing results in differential enzymatic activity (constitutive and low pH activatable) best fitting particular stage(s) of development. In addition, at the onset of involution the N-glycan structure of this endopeptidase switches from a mixed high mannose and hybrid structure to an almost exclusively high mannose type, but reverts back to the original N-glycan composition by day 4 of involution. Our findings illuminate (at least in part) the "raison d'être" for CatD's numerous and highly regulated proteolytic processing steps from the pro-form to the mature enzyme. In the mammary gland, specific cleavage product(s) perform specialized function(s) befitting each stage of remodeling. It is noteworthy that deregulated synthesis, secretion and glycosylation of CatD are hallmarks of cancer progression. Thus, identifying the role of CatD in a dynamic normal tissue undergoing highly regulated cycles of remodeling could provide valuable information illuminating the deregulation of CatD associated with cancer development and metastasis.
组织蛋白酶 D(CatD)是一种溶酶体天冬氨酸内肽酶,最初被认为是一种参与清除不需要的蛋白质的“管家酶”。然而,最近的研究揭示了 CatD 参与细胞凋亡和自噬,因此在多细胞器官的正常发育和维持中具有重要功能。在乳腺中,基质降解和重塑过程由蛋白水解酶协调,但 CatD 在不同发育阶段的作用在很大程度上仍未得到探索。基于我们之前的研究,我们试图研究这种内肽酶在乳腺发育和重塑中的作用。通过使用小鼠模型,我们报告了 CatD 以前未被识别的参与乳腺发育的不同阶段。我们的研究结果表明,CatD 在乳腺发育的不同阶段经历不同的蛋白加工,这种定制的加工导致不同的酶活性(组成型和低 pH 激活型),最适合特定的发育阶段。此外,在退化开始时,这种内肽酶的 N-聚糖结构从混合高甘露糖和杂合结构转变为几乎完全高甘露糖型,但在退化的第 4 天又恢复到原始的 N-聚糖组成。我们的研究结果至少部分阐明了 CatD 从前体到成熟酶的众多高度调控的蛋白水解加工步骤的“存在理由”。在乳腺中,特定的切割产物执行适合每个重塑阶段的特殊功能。值得注意的是,CatD 的合成、分泌和糖基化失调是癌症进展的标志。因此,确定 CatD 在一个动态的正常组织中经历高度调控的重塑循环中的作用,可以提供有价值的信息,阐明与癌症发展和转移相关的 CatD 失调。