Monbiots first book was Poisoned Arrows (1989), a work of investigative travel journalism exposing what he calls the "devastating effects" of the partially World Bank-funded transmigration program on the peoples and tribes of Papua and West Papua in Indonesia. It was followed by Amazon Watershed (1991) which documented expulsions of Brazilian peasant farmers from their land and followed them thousands of miles across the forest to the territory of the Yanomami Indians, and showed how timber sold in Britain was being stolen from indigenous and biological reserves in Brazil. His third book, No Mans Land: An Investigative Journey Through Kenya and Tanzania (1994), documented the seizure of land and cattle from nomadic people in Kenya and the Tanzania, by - among other forces - game parks and safari tourism.. In 2000, he published Captive State: The Corporate Takeover of Britain. The book examines the role of corporate power within the United Kingdom, on both a local and national level, and argues ...
Matrix metalloproteinases (MMPs) are a group of structurally related proteolytic enzymes containing a zinc ion in the active site. They are secreted from cells or bound to the plasma membrane and hydrolyze extracellular matrix (ECM) and cell surface-bound molecules. They therefore play key roles in morphogenesis, wound healing, tissue repair and remodeling in diseases such as cancer and arthritis. Although the cell anchored membrane-type MMPs (MT-MMPs) function pericellularly, the secreted MMPs have been considered to act within the ECM, away from the cells from which they are synthesized. However, recent studies have shown that secreted MMPs bind to specific cell surface receptors, membrane-anchored proteins or cell-associated ECM molecules and function pericellularly at focussed locations. This minireview describes examples of cell surface and pericellular partners of MMPs, as well as how they alter enzyme function and cellular behaviour.
The Indonesian Republic declared its independence on 17 August 1945. Indonesia became a member of United Nations Food and Agriculture Organization (FAO) in 1948. The partnership was strengthened with the opening of a FAO country office in 1978.[35] The agriculture sector of the republic has been supervised and regulated by the Indonesian Ministry of Agriculture.[3] The Indonesian Republic also nationalized many of its colonial economic infrastructures, institutions and businesses and inherited the agricultural system of its predecessor, the Dutch East Indies. In the 1960s until the 1980s, the republic made every effort to develop a post-war agricultural sector and led to the sectors significant expansion. During the Suharto era, the government launched the transmigration program that relocated landless farmers from the overpopulated Java to the less populated Sumatra, Kalimantan, Sulawesi and Papua, thus expanded agricultural farms in the outer islands of the territory.[36] The most ...
The membrane-type matrix metalloproteinases (MT-MMPs) are a subclass of the matrix metalloproteinase (MMP) family which uniquely possess a C-terminal transmembrane domain and are initiators of an activation cascade for progelatinase A (MMP-2). Recent studies have shown that they can also efficiently directly degrade a number of matrix macromolecules. We now show that cells expressing MT1-MMP on their cell surfaces cause subjacent proteolysis of a gelatin film and that this proteolysis is inhibited by TIMP-2 but not by TIMP-1. These data indicate that expression of MT1-MMP on the cell surface may lead to both progelatinase A activation and extracellular matrix degradation.
Proteolysis is essential during branching morphogenesis but the functions of MT-MMPs and their proteolytic products are not clearly understood. into how MT2-MMP-dependent release of bioactive NC1 domains from collagen IV P505-15 is critical for integrating collagen IV synthesis and proteolysis with epithelial proliferation during branching morphogenesis. 8 and 2-fold whereas and did not change (Physique […]. ...
Prions are the cause of neurodegenerative disease in humans and other mammals. The structural conversion of the prion protein (PrP) from a normal cellular protein (PrPC) to a protease-resistant isoform (PrPSc) is thought to relate to Cu2+ binding to histidine residues. In this study, we focused on the membrane-type matrix metalloproteinases (MT-MMPs) such as MT1-MMP and MT3-MMP, which are expressed in the brain as PrPC-degrading proteases. We synthesized 21 prion fragment peptides. Each purified peptide was individually incubated with recombinant MT1-MMP or MT3-MMP in the presence or absence of Cu2+ and the cleavage sites determined by LC-ESI-MS analysis. Recombinant MMP-7 and human serum (HS) were also tested as control. hPrP61-90, from the octapeptide-repeat region, was cleaved by HS but not by the MMPs tested here. On the other hand, hPrP92-168 from the central region was cleaved by MT1-MMP and MT3-MMP at various sites. These cleavages were inhibited by treatment with Cu2+. The C-terminal peptides
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Principal Investigator:ITOH Yoshifumi, Project Period (FY):1998 - 1999, Research Category:Grant-in-Aid for Scientific Research (C), Section:一般, Research Field:Functional biochemistry
Anyone else experiencing anything similar? I have been running low doses of mt2 on and off over the last 7 years. Within the last 5 months I have expe
Among the five membrane-type matrix metalloproteinases (MT-MMPs), MT1-, MT2-, MT3-, and MT5-MMPs have about a 20-amino acid cytoplasmic tail following the transmembrane domain. In contrast, a putative transmembrane domain of MT4-MMP locates at the very C-terminal end, and the expected cytoplasmic tail is very short or nonexistent. Such sequences often act as a glycosylphosphatidylinositol (GPI) anchoring signal rather than as a transmembrane domain. We thus examined the possibility that MT4-MMP is a GPI-anchored proteinase. Our results showed that [(3)H]ethanolamine, which can be incorporated into the GPI unit, specifically labeled the MT4-MMP C-terminal end in a sequence-dependent manner. In addition, phosphatidylinositol-specific phospholipase C treatment released the MT4-MMP from the surface of transfected cells. These results indicate that MT4-MMP is the first GPI-anchored proteinase in the MMP family. During cultivation of the transfected cells, MT4-MMP appeared to be shed from the cell surface by
MMP9小鼠单克隆抗体[56-2A4](ab58803)可与大鼠, 兔, 豚鼠, 人样本反应并经WB, IHC, ICC/IF实验严格验证,被14篇文献引用并得到5个独立的用户反馈。