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Maspin and Cathepsin D Partnership in Regulating Mammary Gland Development and Breast Cancer, pp. 161-176 $100.00
Authors:  Zhila Khalkhali-Ellis, Ming Zhang, Mary J.C. Hendrix, Robert H. Lurie Comprehensive Cancer Center, Northwestern University Feinberg School of Medicine, Chicago, Illinois and others
Maspin (mammary serine protease inhibitor) was identified in 1994
by subtractive hybridization analysis of normal mammary tissue and
breast cancer cell lines. Although Maspin exhibited sequence homology
with members of the serine protease inhibitor superfamily, based on its
structure and in the absence of an identified protease ligand, Maspin was
considered a non-inhibitory serpin. Maspin is expressed in myoepithelial,
epithelial and adipocyte components of mammary tissue, and plays a
critical role in mammary gland development. After a decade of intensive
research, Maspin is now recognized as a multifaceted protein, interacting
with a diverse group of intra- and extra-cellular proteins, regulating a
multitude of cellular functions.
Our laboratory has identified the aspartyl lysosomal proteinase
cathepsin D (CatD) as a putative Maspin binding partner. Apart from its
well studied function in intercellular clearance of proteins, CatD is
critically involved in apoptotic cell death. In addition, excessive
production and aberrant secretion of CatD are believed to contribute to
breast cancer progression and metastasis. To date, our studies have
illuminated novel aspects of the CatD and Maspin partnership in
regulating key stages of normal mammary gland differentiation and
remodeling. In this short communication we will examine this complex
interaction, and speculate on how alteration in pathways operative in
mammary gland remodeling could promote malignant growth. 

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Maspin and Cathepsin D Partnership in Regulating Mammary Gland Development and Breast Cancer, pp. 161-176