Inhibition of Membrance-Type 1 Matrix Metalloproteinase at Cell-Matrix Adhensions

Division of Molecular Viology and Oncolog

Activation of Matrix Metalloproteinase (MMP)-2 By Membrane-type 1-MMP Through An Artificial Receptor For ProMMP-2 Generates Active MMP-2

Division of Molecular Viology and Oncolog

Substrate choice of membrane-type 1 matrix metalloproteinase is dictated by tissue inhibitor of metalloproteinase-2 levels

Division of Molecular Viology and Oncolog

Figuring and smoothing capabilities of elastic emission machining for low-thermal-expansion glass optics

The use of elastic emission machining (EEM) for fabricating optics from low-thermal-expansion glass for extreme ultraviolet (EUV) lithography is examined. EUV optics require figure accuracy and surface roughness of 0.1 nm root mean square (rms) or better. EEM using a rotating-sphere head is demonstrated to achieve this level of surface smoothness after a certain depth of removal dependent on the material being processed. In tests of continuous machining for 12 h, no increase in surface roughness is observed, demonstrating the high temporal stability of this noncontact processing method. EEM using a rotating-sphere head is thus confirmed to have sufficient figuring and smoothing capability for the fabrication of EUV optics. © 2007 American Vacuum Society.M. Kanaoka et al. "Figuring and smoothing capabilities of elastic emission machining for low-thermal-expansion glass optics", Journal of Vacuum Science & Technology B: Microelectronics and Nanometer Structures Processing, Measurement, and Phenomena 25, 2110-2113 (2007) https://doi.org/10.1116/1.2789440

Cleavage of growth differentiation factor 15 (GDF15) by membrane type 1-matrix metalloproteinase abrogates GDF15-mediated suppression of tumor cell growth

Division of Molecular Viology and Oncolog

Cleavage of Amyloid-β Precursor Protein (APP) by Membrane-Type Matrix Metalloproteinases

Division of Molecular Viology and Oncolog

Membrane-type 1 matrix metalloproteinase modulates focal adhension stability and cell migration

Division of Molecular Viology and Oncolog

Cleavage of growth differentiation factor 15 (GDF15) by membrane type 1-matrix metalloproteinase abrogates GDF15-mediated suppression of tumor cell growth

金沢大学がん研究所がん病態制御Growth differentiation factor 15 (GDF15), a transforming growth factor (TGF)-β superfamily member, has been cloned from a placenta cDNA library as a gene product that has promoted activation of pro-matrix metalloproteinase (MMP)2 mediated by membrane type (MT)1-MMP. Expression of MT1-MMP in HEK293T cells caused cleavage of the GDF15 mature form at N252 -M253 to produce a 6-kDa C -terminal fragment. Treatment of MCF7 cells with GDF15 induced activation of p53 and enhanced expression of p21, which was abrogated by MT1-MMP expression. GDF15 mRNA synthesis was also shown to be induced by treatment of cells with GDF15. Treatment of MCF7 cells with GDF15 caused suppression of cell proliferation. However, proliferation of MCF7 cells transfected with the MT1-MMP gene was not affected by GDF15 treatment, but was suppressed in the presence of the MMP inhibitor BB94. HT1080 cells transfected with the GDF15 gene, which endogenously express MT1-MMP, synthesize a high-level GDF15 precursor form and a low-level mature form, and treatment of cells with BB94 enhanced production of the GDF15 mature form. Consistent with GDF15 production, HT1080 cells transfected with the GDF15 gene proliferated almost equally with control cells, and addition of BB94 effectively suppressed growth of HT1080 cells transfected with the GDF15 gene concomitant with the accumulation of the GDF15 mature form, but not control cells. These results suggest that MT1-MMP contributes to tumor cell proliferation through the cleavage of GDF15, which down-regulates cell proliferation by inducing activation of p53 and p21 synthesis. © 2007 Japanese Cancer Association

The scaffold protein c-Jun NH2-terminal kinase-associated leucine zipper protein regulates cell migration through interaction wity the G protein Gα13

Division of Molecular Cell Signalin