Monitoring matrix metalloproteases based on the selective interaction between an Ir(iii) solvent complex and a histidine-rich polypeptide

2019 ◽  
Vol 55 (49) ◽  
pp. 7085-7088 ◽  
Author(s):  
Huijuan Su ◽  
Menghan Zang ◽  
Lihua Lu ◽  
Feng Li
Keyword(s):  
Matrix Metalloproteases ◽  
Selective Interaction ◽  
Solvent Complex

A luminescent biosensor was developed for MMP-9 assays based on the selective interaction between an Ir(iii) solvent complex and a histidine-rich peptide.

scholarly journals Conformation-Specific Inhibitory Anti-MMP-7 Monoclonal Antibody Sensitizes Pancreatic Ductal Adenocarcinoma Cells to Chemotherapeutic Cell Kill

Cancers ◽  
2021 ◽  
Vol 13 (7) ◽  
pp. 1679
Author(s):  
Vishnu Mohan ◽  
Jean P. Gaffney ◽  
Inna Solomonov ◽  
Maxim Levin ◽  
Mordehay Klepfish ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Active Site ◽  
Drug Targets ◽  
Fas Ligand ◽  
Specific Activity ◽  
Matrix Metalloproteases ◽  
Ductal Adenocarcinoma ◽  
Enzyme Active Site ◽  
Induced Apoptosis

Matrix metalloproteases (MMPs) undergo post-translational modifications including pro-domain shedding. The activated forms of these enzymes are effective drug targets, but generating potent biological inhibitors against them remains challenging. We report the generation of anti-MMP-7 inhibitory monoclonal antibody (GSM-192), using an alternating immunization strategy with an active site mimicry antigen and the activated enzyme. Our protocol yielded highly selective anti-MMP-7 monoclonal antibody, which specifically inhibits MMP-7′s enzyme activity with high affinity (IC50 = 132 ± 10 nM). The atomic model of the MMP-7-GSM-192 Fab complex exhibited antibody binding to unique epitopes at the rim of the enzyme active site, sterically preventing entry of substrates into the catalytic cleft. In human PDAC biopsies, tissue staining with GSM-192 showed characteristic spatial distribution of activated MMP-7. Treatment with GSM-192 in vitro induced apoptosis via stabilization of cell surface Fas ligand and retarded cell migration. Co-treatment with GSM-192 and chemotherapeutics, gemcitabine and oxaliplatin elicited a synergistic effect. Our data illustrate the advantage of precisely targeting catalytic MMP-7 mediated disease specific activity.

Identification of domains that control the heteromeric assembly of Kir5.1/Kir4.0 potassium channels

2003 ◽  
Vol 284 (4) ◽  
pp. C910-C917 ◽  
Author(s):  
Angelos-Aristeidis Konstas ◽  
Christoph Korbmacher ◽  
Stephen J. Tucker
Keyword(s):  
Potassium Channels ◽  
Potassium Channel ◽  
Functional Diversity ◽  
Kir Channels ◽  
Selective Interaction ◽  
Inwardly Rectifying ◽  
In Cells ◽  
Heteromeric Channels

Heteromultimerization between different inwardly rectifying (Kir) potassium channel subunits is an important mechanism for the generation of functional diversity. However, little is known about the mechanisms that control this process and that prevent promiscuous interactions in cells that express many different Kir subunits. In this study, we have examined the heteromeric assembly of Kir5.1 with other Kir subunits and have shown that this subunit exhibits a highly selective interaction with members of the Kir4.0 subfamily and does not physically associate with other Kir subunits such as Kir1.1, Kir2.1, and Kir6.2. Furthermore, we have identified regions within the Kir4.1 subunit that appear to govern the specificity of this interaction. These results help us to understand the mechanisms that control Kir subunit recognition and assembly and how cells can express many different Kir channels while maintaining distinct subpopulations of homo- and heteromeric channels within the cell.

scholarly journals Glycosylation of matrix metalloproteases and tissue inhibitors: present state, challenges and opportunities

2016 ◽  
Vol 473 (11) ◽  
pp. 1471-1482 ◽  
Author(s):  
Lise Boon ◽  
Estefania Ugarte-Berzal ◽  
Jennifer Vandooren ◽  
Ghislain Opdenakker
Keyword(s):  
Matrix Metalloproteinases ◽  
Present State ◽  
Cellular Localization ◽  
Current Knowledge ◽  
Matrix Metalloproteases ◽  
Inhibitor Binding ◽  
Attachment Sites ◽  
Functional Aspects ◽  
Functional Implications ◽  
Challenges And Opportunities

Current knowledge about the glycosylation of matrix metalloproteinases (MMPs) and the inhibitors of metalloproteinases (TIMPs) is reviewed. Whereas structural and functional aspects of the glycobiology of many MMPs is unknown, research on MMP-9 and MMP-14 glycosylation reveals important functional implications, such as altered inhibitor binding and cellular localization. This, together with the fact that MMPs contain conserved and many potential attachment sites for N-linked and O-linked oligosaccharides, proves the need for further studies on MMP glycobiology.

Evaluation of Selective Interaction of Ga3+withN-Octadecanoyl-N-phenylhydroxylamine by L–B Technique

1996 ◽  
Vol 183 (2) ◽  
pp. 315-319
Author(s):  
Hiroshi Okushita ◽  
Takeo Shimidzu
Keyword(s):  
Selective Interaction

A Selective Interaction between Cation and Separator Membrane in Lithium Secondary Batteries

2017 ◽  
Vol 121 (43) ◽  
pp. 23926-23930 ◽  
Author(s):  
Yuria Saito ◽  
Sahori Takeda ◽  
Wataru Morimura ◽  
Rika Kuratani ◽  
Satoshi Nishikawa
Keyword(s):  
Lithium Secondary Batteries ◽  
Selective Interaction

Human ubiquitin-protein ligase Nedd4: expression, subcellular localization and selective interaction with ubiquitin-conjugating enzymes

1998 ◽  
Vol 3 (11) ◽  
pp. 751-763 ◽  
Author(s):  
Tadashi Anan ◽  
Yoichi Nagata ◽  
Hisashi Koga ◽  
Yoshiomi Honda ◽  
Nami Yabuki ◽  
...  
Keyword(s):  
Subcellular Localization ◽  
Ubiquitin Protein Ligase ◽  
Human Ubiquitin ◽  
Selective Interaction ◽  
Conjugating Enzymes ◽  
Ubiquitin Conjugating Enzymes

Inhibition of stromal matrix metalloproteases: Effects on breast-tumor promotion by fibroblasts

1998 ◽  
Vol 76 (2) ◽  
pp. 267-273 ◽  
Author(s):  
Agnès Noël ◽  
Amin Hajitou ◽  
Cécile L'Hoir ◽  
Erik Maquoi ◽  
Eugénia Baramova ◽  
...  
Keyword(s):  
Breast Tumor ◽  
Tumor Promotion ◽  
Matrix Metalloproteases ◽  
Stromal Matrix

scholarly journals 359 ASSOCIATION OF REGULATORY POLYMORPHISMS IN MATRIX METALLOPROTEASES WITH OSTEOARTHRITIS RISK

2008 ◽  
Vol 16 ◽  
pp. S156
Author(s):  
A. Gonzalez ◽  
C. Rodriguez-Fontenla ◽  
J. Rodriguez-Lopez ◽  
J. Loughlin ◽  
A. Tsezou ◽  
...  
Keyword(s):  
Matrix Metalloproteases
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