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Hexosaminidase as a new potential marker for larynx cancer

Authors:	Ewa Olszewska Malgorzata Borzym-Kluczyk Ireneusz Rzewnicki Justyna Rutkowska Malgorzata Knas Marek Rogowski Edyta Waniewska Romuald Wielgosz

Affiliation:	1. Department of Otolaryngology, Medical University of Bialystok, ul. Sklodowskiej 24 A, 15-274 Bialystok, Poland;2. Department of Pharmaceutical Biochemistry, Medical University of Bialystok, Poland;3. Department of Otolaryngology, Krupp Hospital, Essen, Germany;1. Department of Histology and Embryology, Jessenius Faculty of Medicine, Comenius University, Malá Hora 4, 03601 Martin, Slovakia;2. Department of Pathology, Faculty of Medicine, University of Ostrava, Syllabova 19, 70300 Ostrava, Czech Republic;3. Department of Medical Biochemistry, Jessenius Faculty of Medicine, Comenius University, Malá Hora 4, 03601 Martin, Slovakia;4. Department of Histology and Embryology, Faculty of Medicine, University of Ostrava, Syllabova 19, 70300 Ostrava, Czech Republic;1. Material and Chemical Engineering College, Sichuan University of Science and Engineering, Zigong 643000, PR China;2. Key Laboratory of Chemistry of Northwestern Plant Resources and Key Laboratory for Natural Medicine of Gansu Province, Lanzhou Institute of Chemical Physics, Chinese Academy of Sciences, Lanzhou 730000, PR China;1. Thomas Jefferson University Kimmel Cancer Center Philadelphia, PA;2. University of Manchester Manchester Breast Centre & Breakthrough Breast Cancer Research Unit Manchester, UK;1. Department of Electrical and Computer Engineering, University of Connecticut, 371 Fairfield Way, Storrs, CT 06269, USA;2. Department of Chemistry, University of Connecticut, 55 N. Eagleville Road, Storrs, CT 06269-3060, USA;1. Laboratory of Biotransformation, Institute of Microbiology, Czech Academy of Sciences, Vídeňská 1083, CZ 14220 Praha 4, Czech Republic;2. Department of Biochemistry and Microbiology, University of Chemistry and Technology Prague, Technická 5, CZ 16628 Praha 6, Czech Republic;3. Department of Structure and Function of Proteins, Institute of Microbiology, Czech Academy of Sciences, Zámek 136, CZ 37333 Nové Hrady, Czech Republic;1. Department of Biochemistry, Faculty of Science, Charles University, Hlavova 2030, Prague 2 128 40, Czech Republic;2. Department of Analytical Chemistry, Faculty of Science, Charles University, Hlavova 2030, Prague 2 128 40, Czech Republic

Abstract:	ObjectivesLarynx squamous cell carcinoma is one of the most common forms of cancer in the area of the neck. The aim of our study was to investigate the activities of N-acetyl-β-d-hexosaminidase (HEX) in larynx cancer compared with the specimens from the healthy space of the tumor that served as controls.Design and methodsLarynx cancer (n = 15) and normal healthy tissue around the tumor (n = 15) were collected from the patients during total laryngectomy. Specimens were immediately frozen in ? 80 °C. To assess hexosaminidase activity, release of p-nitrophenol from p-nitrophenol derivatives was used.ResultsWe observed a significantly higher activity of the investigated enzyme in all laryngeal cancer specimens compared with that in healthy tissue homogenates. The differences were statistically significant.ConclusionsIt could be assumed that HEX may release particular sugars from the ends of oligosaccharide chains of glycocalyx proteins, changing adhesive forces binding together cells, and the communication between cells and elements of extracellular matrix.

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