Έκφραση των ADAMTS στον καρκίνο του λάρυγγα

Laryngeal cancer is one of the less frequent human cancers. However, and since symptoms have not been always perceived by the patient quickly, the visit to the laryngologist is when cancer has reached an advanced state. Thus, the investigation of therapeutic targets for best treatment and increase in life expectancy is something of concern to the scientific community worldwide. Degrading enzymes might be considered as therapeutic targets in cancer, and much attention has been recently given to the ADAMTS family. ADAMTS proteins are members of the secreted, extracellular metalloprotease family possessing disintegrin structure and thrombospondin motif(s). ADAMTS enzymes possess proteolytic activities to different substrates; ADAMTS-1, -4, -5, -8, 9, -15 and -18 are proteoglycanases, ADAMTS-2, -3 and -14 are N-propeptide procollagenases, ADAMTS-7 and -12 can degrade COMP and ADAMTS-13 can degrade vWF. Through their proteolytic activity, together with the activity deriving of the presence of thrombospondin motif(s), the members have the ability to regulate cell proliferation, cell motility and angiogenesis. Since previous observations suggested increased expression of ADAMTS enzymes belonging to the proteoglycanase subfamily in laryngeal cancer, the present work is designed to study the expression of ADAMTS-2, -3, -7, -12, -13 and -14 in this type of cancer for understanding their biological role. The expression of ADAMTS was examined at transcriptional level by RT-PCR. The results have shown increased expression of ADAMTS-2, -3, -14 in cancerous tissue samples compared with the respective macroscopically normal. On the other hand, ADAMTS-7, -12 and -13 were not expressed in all samples and their expression differed with staging and anatomical position of cancer.