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MUC1 mucin is a target protein for many monoclonal antibodies. Human MUC1 detected by a murine anti-KL-6 monoclonal antibody that recognizes a sialylated carbohydrate chain has been designated KL-6/MUC1. Given the heterogeneous antigenicity of KL-6/MUC1, we established a new murine monoclonal antibody, H9, that reacts with epitope DTRP (Asp-Thr-Arg-Pro) peptides within the immunodominant region of the tandem repeat of MUC1 mucin. The reactivity of the H9 antibody differs from that of other previously reported antibodies that recognize the tandem repeat region of MUC1. Immunohistochemical experiments indicate that the reactivity of the H9 antibody is similar to that of other antibodies directed against MUC1 core proteins. A new cancer-associated protein detected by a sandwich assay using the H9 antibody as a catcher and the KL-6 antibody as a tracer is designated HK9. Serum HK9 levels showed a high expression level in lung cancer: 51% (19/37 cases) for adenocarcinoma, 39% (11/28 cases) for squamous cell carcinoma, and 67% (10/15 cases) for small cell carcinoma. The HK9 expression in lung cancer increased with cancer progression. These findings suggest monoclonal antibody H9 to be a novel antibody that reacts with an epitope within the tandem repeat region of MUC1, and that the cancer-associated antigen HK9 may have useful tumor-associated properties.
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PMID:A novel monoclonal antibody, H9, directed against the core protein of MUC1 mucin. 1067 62

Mammalian proteases segregate into several distinct protein families that employ different functional domains to hydrolyze peptides bonds with different specificities and affinities. These enzymes play central roles in critical cellular and systemic processes, including regulation of cell growth, differentiation, homeostasis, and apoptosis; and cancer initiation, progression, and metastasis. Human proteases segregate into five distinct catalytic classes; the metalloprotease, serine protease, and cysteine protease families have the most members, while the aspartic and threonine peptidase families have relatively few examples. Section 1 discusses the five different types of human proteases and summarizes some of their known functions during tumorigenesis, migration, and metastasis. Section 2 focuses on how cancer degradomes, defined as all the proteases, protease inhibitors, and protease substrates regulated by a given cancer, affect cancer promotion and suppression, and current approaches for degradome profiling. Protein degradation products generated during cancer progression, invasion, and metastasis alter the tumor microenvironment to influence these processes. These cancer-associated protein degradation profiles (aka tumor peptidomes) represent a potentially rich pool of candidates for cancer biomarker discovery. Section 3 focuses on the benefits and challenges associated with peptidome studies, and methods employed to conduct them. Section 4 discusses recent studies that use circulating peptides as cancer biomarkers, and how the abundance of peptides reflects the activity of their source proteases during cancer progression. We hope this chapter will convey a good sense of current research on how cancer-associated proteases, degradomes, and their resulting peptidomes can improve our knowledge of cancer biology, improve diagnosis and evaluation, and inspire new ideas in this and related research areas.
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PMID:Circulating Peptidome and Tumor-Resident Proteolysis. 2905 66