Download Cell Surface Proteases by Stanley Zucker, Wen-Tien Chen PDF

By Stanley Zucker, Wen-Tien Chen

Cell floor Proteases presents a complete evaluation of those vital enzymes that catalyze the hydrolysis of a protein because it degrades to a less complicated substance. within the Nineties, an explosion of latest discoveries make clear the position of cellphone floor proteases and prolonged it past degradation of extracellular matrix parts to incorporate its impact on progress elements, mobile signaling, and different mobile occasions. This quantity unites the medical literature from throughout disciplines and teases out unified topics of interactions among telephone floor proteases and interconnecting cellphone surface-related platforms -- together with integrins and different adhesion molecules. Scientists and scholars excited by developmental biology, telephone biology and sickness methods will locate this an integral resource.

* presents an summary of the whole box of mobilephone floor proteases in one volume
* provides significant concerns and excellent discoveries on the leading edge of recent developmental biology and developmental medication
* A thematic quantity within the longest-running discussion board for modern matters in developmental biology with over 30 years of assurance

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Membrane Type-Matrix Metalloproteinases (MT-MMP) 11 comparisons among the six distinct MT-MMPs have revealed that they show a significant percentage of overall amino acid sequence identities (about 40–50%) and contain all protein domains characteristic of MMPs including signal peptide, propeptide, catalytic domain with the zinc-binding site, hinge region, and hemopexin domain (Fig. 1). However, MT-MMPs also contain unique structural features that confer on them specific properties. Thus, they differ from the remaining MMP family members by the presence of a C-terminal extension rich in hydrophobic residues and involved in the membrane attachment of these proteases.

MT4-MMP has the least degree of sequence identity to the other family members (Pei, 1999). Another distinction is that MT4-MMP is most potently inhibited by TIMP-1 rather than TIMP-2 or TIMP-3, like the proMMP-2 activating MT-MMPs. a. Propeptide Domain of MT-MMPs. The propeptide domain of MT-MMPs has some characteristic features when compared with the equivalent region of other MMPs. , 2000). , 2002). Furthermore, mutations in this conserved region have been shown to be detrimental for MT1-MMP function in terms of activation of proMMP-2, binding of TIMP-2 to the cell surface, cell migration, and substrate degradation.

2000) reported that a truncation of 10 amino acids, but not the 6 terminal amino acid residues in the MT1-MMP cytoplasmic tail, decreased the invasive activity of 1. Membrane Type-Matrix Metalloproteinases (MT-MMP) 15 human melanoma cells, supporting a role for this MT-MMP domain in cell invasion. Ure˜na et al. (1999) and Nakahara et al. (1998) reported that the cytoplasmic tail is critically involved in trafficking of MT1-MMP to discrete regions of the cell surface and in communicating with putative intracellular components.

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