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Membrane-Type 1 Matrix Metalloproteinase Cleaves Cd44 and Promotes Cell Migration
It is demonstrated that MT1-MMP acts as a processing enzyme for CD44H, releasing it into the medium as a soluble 70-kD fragment that stimulates cell motility and reveals a novel interaction of the two molecules that have each been implicated in tumor cell migration and invasion.
Membrane Type 4 Matrix Metalloproteinase (MT4-MMP, MMP-17) Is a Glycosylphosphatidylinositol-anchored Proteinase*
Results indicate that MT4-MMP is the first GPI-anchored proteinase in the MMP family, indicating a unique biological function and character for this proteinase.
Membrane-type 5 matrix metalloproteinase is expressed in differentiated neurons and regulates axonal growth.
Expression of membrane-type (MT) 5 matrix metalloproteinase (MMP) in the mouse brain was examined. MT5-MMP was expressed in the cerebrum in embryos, but it declined after birth. In contrast,
MT-MMP, the cell surface activator of proMMP-2 (pro-gelatinase A), is expressed with its substrate in mouse tissue during embryogenesis.
Results indicated that proMMP-2 activation through its activator, MT-MMP, is a physiological system used by organisms to initiate tissue remodeling on the cell surface.
Generation of a recombinant Sendai virus that is selectively activated and lyses human tumor cells expressing matrix metalloproteinases
These results demonstrate the selective targeting and killing of human tumor cells by recombinant SeV technology and greatly advance the reemerging concept of oncolytic virotherapy, which currently appears to rely largely upon a natural preference of certain viruses for cancer cells.
Expression of a putative precursor mRNA for sperm-activating peptide I in accessory cells of the ovary in the sea urchin Hemicentrotus pulcherrimus
An expression study of the SAM precursor gene, by in situ hybridization with a non-radioactive RNA probe synthesized using the 1.3 kb cDNA as template, demonstrated that abundant SAM precursor transcripts were expressed in the accessory cells, but not in the growing oocytes.
Purification and Characterization of the Egg Jelly Macromolecules, Sialoglycoprotein and Fucose Sulfate Glycoconjugate, of the Sea Urchin Hemicentrotus Pulcherrimus
Sialoglycoprotein and a fucose sulfate glycoconjugate were purified from egg jelly of the sea urchin Hemicentrotus pulcherrimus and carboxymethylted FSG was less potent than intact FSG in induction of the acrosome reaction.