Role of intracellular acid Ca2+stores in pathological pancreatic protease activation

2012 ◽  
Vol 6 (2) ◽  
pp. 129-131
Author(s):  
Oleg V Gerasimenko ◽  
Ole H Petersen ◽  
Julia V Gerasimenko
Keyword(s):  
Protease Activation ◽  
Pancreatic Protease ◽  
Intracellular Acid

scholarly journals VimA is part of the maturation pathway for the major gingipains of Porphyromonas gingivalis W83

Microbiology ◽  
2006 ◽  
Vol 152 (11) ◽  
pp. 3383-3389 ◽  
Author(s):  
E. Vanterpool ◽  
F. Roy ◽  
W. Zhan ◽  
S. M. Sheets ◽  
L. Sangberg ◽  
...  
Keyword(s):  
Gene Product ◽  
Porphyromonas Gingivalis ◽  
Protein Interaction ◽  
Protein Protein Interaction ◽  
Interaction Studies ◽  
Defective Mutant ◽  
Protease Activation ◽  
Porphyromonas Gingivalis W83

The authors have shown previously that the vimA gene, which is part of the bcp-recA-vimA operon, plays an important role in protease activation in Porphyromonas gingivalis. The gingipain RgpB proenzyme is secreted in the vimA-defective mutant P. gingivalis FLL92. An important question that is raised is whether the vimA gene product could directly interact with the proteases for their activation or regulate a pathway responsible for protease activation. To further study the mechanism(s) of VimA-dependent protease activation, the vimA gene product was further characterized. A 39 kDa protein consistent with the size of the predicted VimA protein was purified. In protein–protein interaction studies, the VimA protein was shown to interact with gingipains RgpA, RgpB and Kgp. Immune sera from mice immunized with P. gingivalis immunoreacted with the purified VimA protein. Taken together, these data suggest an interaction of VimA with the gingipains and further confirm the role of this protein in their regulation or maturation.

scholarly journals The role of proteases in excitation-contraction coupling failure in muscular dystrophy

2015 ◽  
Vol 308 (1) ◽  
pp. C33-C40 ◽  
Author(s):  
Davi A. G. Mázala ◽  
Robert W. Grange ◽  
Eva R. Chin
Keyword(s):  
Muscular Dystrophy ◽  
Protease Inhibition ◽  
Excitation Contraction Coupling ◽  
Contraction Coupling ◽  
Fura 2 ◽  
Flexor Digitorum Brevis ◽  
Protease Activation ◽  
Flexor Digitorum ◽  
Stimulation Of

Duchenne muscular dystrophy (DMD) is one of the most frequent types of muscular dystrophy. Alterations in intracellular calcium (Ca2+) handling are thought to contribute to the disease severity in DMD, possibly due to the activation of Ca2+-activated proteases. The purpose of this study was twofold: 1) to determine whether prolonged excitation-contraction (E-C) coupling disruption following repeated contractions is greater in animals lacking both dystrophin and utrophin ( mdx/Utr−/−) compared with mice lacking only dystrophin ( mdx); and 2) to assess whether protease inhibition can prevent E-C coupling failure following repeated tetani in these dystrophic mouse models. Excitation-contraction coupling was assessed using Fura-2 ratio, as an index of intracellular free Ca2+ concentration, in response to electrical stimulation of single muscle fibers from the flexor digitorum brevis muscle. Resting Fura-2 ratio was higher in dystrophic compared with control (Con) fibers, but peak Fura-2 ratios during stimulation were similar in dystrophic and Con fibers. One hour after a series of repeated tetani, peak Fura-2 ratios were reduced by 30 ± 5.6%, 23 ± 2%, and 36 ± 3.1% in mdx, mdx/Utr+/−, and mdx/Utr−/−, respectively, with the greatest reduction in mdx/Utr−/− fibers ( P < 0.05). Protease inhibition attenuated this decrease in peak Fura-2 ratio. These data indicate that E-C coupling impairment after repeated contractions is greatest in fibers lacking both dystrophin and utrophin and that prevention of protease activation can mitigate the prolonged E-C coupling impairment. These data further suggest that acute protease inhibition may be useful in reducing muscle weakness in DMD.

Role of Protease Activation in Subcellular Remodeling and Heart Failure

2013 ◽  
pp. 365-381
Author(s):  
Naranjan S. Dhalla ◽  
Vijayan Elimban ◽  
Davinder S. Jassal
Keyword(s):  
Heart Failure ◽  
Protease Activation

scholarly journals Mutagenesis of the West Nile virus NS2B cofactor domain reveals two regions essential for protease activity

2008 ◽  
Vol 89 (4) ◽  
pp. 1010-1014 ◽  
Author(s):  
Keith J. Chappell ◽  
Martin J. Stoermer ◽  
David P. Fairlie ◽  
Paul R. Young
Keyword(s):  
West Nile Virus ◽  
Proteolytic Activity ◽  
The West ◽  
West Nile ◽  
Mutagenesis Screen ◽  
Antiviral Compounds ◽  
Protease Activation ◽  
Primary Focus ◽  
Ns3 Protease

The flavivirus NS2B/NS3 protease has received considerable attention as a target for the development of antiviral compounds. While substrate based inhibitors have been the primary focus to date, an approach focussing on NS2B cofactor displacement could prove to be an effective alternative. To understand better the role of the NS2B cofactor in protease activation, we conducted an alanine mutagenesis screen throughout the 42-residue central cofactor domain (NS2B51–92) of West Nile virus (WNV). Two sites critical for proteolytic activity were identified (NS2B59–62 and NS2B75–87), where the majority of substitutions were found to significantly decrease proteolytic activity of a recombinant WNV NS2B/NS3 protease. These findings provide mechanistic insights into the structural and functional role that the cofactor may play in the substrate-bound and free protease complexes as well as providing novel sites for targeting new antiviral inhibitors.

scholarly journals Cell surface protease activation during RAS transformation: Critical role of the plasminogen receptor, S100A10

Oncotarget ◽  
2016 ◽  
Vol 7 (30) ◽  
pp. 47720-47737 ◽  
Author(s):  
Patricia A. Madureira ◽  
Alamelu G. Bharadwaj ◽  
Moamen Bydoun ◽  
Katy Garant ◽  
Paul O'Connell ◽  
...  
Keyword(s):  
Cell Surface ◽  
Critical Role ◽  
Protease Activation ◽  
Cell Surface Protease

ROLE OF OXYGEN-DERIVED FREE RADICALS IN PROTEASE ACTIVATION AFTER PANCREAS TRANSPLANTATION IN THE PIG1

1998 ◽  
Vol 65 (3) ◽  
pp. 421-426 ◽  
Author(s):  
Ulf Petersson ◽  
Ragnar K??ll??n ◽  
Agneta Montgomery ◽  
Anders Borgstr??m
Keyword(s):  
Free Radicals ◽  
Pancreas Transplantation ◽  
Oxygen Derived Free Radicals ◽  
Protease Activation

scholarly journals The Role of Apoptotic Signaling in Axon Guidance

2018 ◽  
Vol 6 (4) ◽  
pp. 24 ◽  
Author(s):  
Riley Kellermeyer ◽  
Leah Heydman ◽  
Grant Mastick ◽  
Thomas Kidd
Keyword(s):  
Axon Guidance ◽  
Neurotrophic Factors ◽  
Tumor Suppressors ◽  
Growth Cones ◽  
Cytoskeletal Proteins ◽  
Guidance Cues ◽  
Cytoskeletal Dynamics ◽  
Protease Activation ◽  
Entire Trajectory

Navigating growth cones are exposed to multiple signals simultaneously and have to integrate competing cues into a coherent navigational response. Integration of guidance cues is traditionally thought to occur at the level of cytoskeletal dynamics. Drosophila studies indicate that cells exhibit a low level of continuous caspase protease activation, and that axon guidance cues can activate or suppress caspase activity. We base a model for axon guidance on these observations. By analogy with other systems in which caspase signaling has non-apoptotic functions, we propose that caspase signaling can either reinforce repulsion or negate attraction in response to external guidance cues by cleaving cytoskeletal proteins. Over the course of an entire trajectory, incorrectly navigating axons may pass the threshold for apoptosis and be eliminated, whereas axons making correct decisions will survive. These observations would also explain why neurotrophic factors can act as axon guidance cues and why axon guidance systems such as Slit/Robo signaling may act as tumor suppressors in cancer.

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