Chemokines and Cancer (Contemporary Cancer Research) by Barrett Rollins

By Barrett Rollins

Chemokines and melanoma synthesizes a state of the art knowing of the function that chemokines and their receptors play within the pathophysiology of malignancy. It examines the effect of chemokines on a huge array of malignant cells, together with their results on such intrinsic houses as development and move, in addition to exploring their impact at the host's reaction to a transforming into tumor. The authors additionally reveal the physiological effects of chemokine expression and recommend how chemokines can be utilized to manage tumor development in vivo, together with their direct results on tumor development, on tumor destruction by way of host inflammatory cells, and on tumor angiogenesis. the single e-book to be had that relates chemokines to melanoma, Chemokines and melanoma holds out the promise of novel healing methods to malignancy throughout the manipulation of chemokines and/or their receptors.

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MONOCYTE FUNCTIONS OTHER THAN CHEMOTAXIS C-C chemokines, MCP-1 in particular, affect several functions of mononuclear phagocytes related to recruitment or to effector activity. Interaction with, and localized digestion of, extracellular matrix components is essential for phagocyte extravasation and migration in tissues. MCP-1 induces production of gelatinase and of urokinase- 40 Mantovani et al. type plasminogen activator (uPA) (47,60). Concomitantly, MCP-1 augments expression of the cell surface receptor for uPA.

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Ahuja S. , Lee J. , and Murphy P. M. 1996. CXC chemokines bind to unique sets of selectivity determinants that can function independently and are broadly distributed on multiple domains of human interleukin-8 receptor B. Determinants of high affinity binding and receptor activation are distinct. J. Biol. Chem. 271: 225–232. 19. Ahuja S. , and Murphy P. M. 1996. The CXC chemokines growth-regulated oncogene (GRO) alpha, GRObeta, GROgamma, neurophil-activating peptide-2, and epithelial cellderived neutrophil-activating peptide-78 are potent agonists of the type B, but not the type A, human interleukin-8 receptor.

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