Kallikrein-Related Peptidases, Volume 2: Novel by Viktor Magdolen, Christian P. Sommerhoff, Hans Fritz,

By Viktor Magdolen, Christian P. Sommerhoff, Hans Fritz, Manfred Schmitt

Quite a few KLK proteins and their encoding genes have attracted elevated consciousness between scientists and clinicians world wide when you consider that they characterize very attention-grabbing and functionally detailed biomarkers, relatively, in melanoma. This ebook reports the position of kallikrein-related peptidases (KLKs) in quite a lot of cancers, together with lung, prostate, breast and ovarian melanoma. It presents clinicians, healthcare professional scientists and researchers with a complete assessment at the medical relevance of KLK expression in a variety of malignancies.

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2008). Human tissue kallikreins as promiscuous modulators of homeostatic skin barrier functions. Biol. Chem. 389, 669–680. P. (2011). Kallikrein-related peptidase-8 (KLK8) is an active serine protease in human epidermis and sweat and is involved in a skin barrier proteolytic cascade. J. Biol. Chem. 286, 687–706. P. (2007). New insights into the functional mechanisms and clinical applications of the kallikrein-related peptidase family. Mol. Oncol. 1, 269–287. P. (2008). Human kallikrein-related peptidase 14 (KLK14) is a new activator component of the KLK proteolytic cascade.

J. (2004). Mucins in cancer: protection and control of the cell surface. Nat. Rev. Cancer 4, 45–60. , and Sasano, H. (2005). Progesterone receptor in non-small cell lung cancer--a potent prognostic factor and possible target for endocrine therapy. Cancer Res. 65, 6450–6458. I. F. (2011). Taking aim at the extracellular matrix: CCN proteins as emerging therapeutic targets. Nat. Rev. Drug Discov. 10, 945–963. Y. (2011a). Antiangiogenic antitumor activities of IGFBP-3 are mediated by IGF-independent suppression of Erk1/2 activation and Egr-1-mediated transcriptional events.

Fragmentation of CCN1 by KLK12 triggered the release of BMP-2, VEGF, and TGF-β from the growth factor-CCN complexes. 0 mass (m/z) 3 (b) 1 1: K88-R89 2: K208 -K209 3: R218 -I219 (main cleavage site) 4: K291-K292 5: K345-N346 IGFBP 4 2 VWC TSR 5 C-terminal KLK12 cleavage sites in CCN1 (c) relative binding to control + + + 100 50 0 BMP BMP + KLK12 VEGF VEGF + KLK12 FGF2 FGF2 + KLK12 TGFb TGFb + KLK12 18 Nathalie Heuzé-Vourc’h, and Yves Courty of several important growth factors and related pathways, such as the IGFs, VEGF, TGF-β, BMPs (bone morphogenetic proteins), FGFs (fibroblast growth factors), and Wnt signalling.

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