Direct on-filter assay of subtilisin-type proteolytic enzymes for rapid analysis of analyte captured from the workplace atmosphere

2000 ◽  
Vol 2 (5) ◽  
pp. 451-454 ◽  
Author(s):  
Zhi-Feng Miao ◽  
Frederick J. Rowell ◽  
Roger N. Reeve ◽  
Robert H. Cumming
Keyword(s):  
Proteolytic Enzymes ◽  
Rapid Analysis ◽  
Filter Assay

The ubiquitin–proteasome system and skeletal muscle wasting

2005 ◽  
Vol 41 ◽  
pp. 173-186 ◽  
Author(s):  
Didier Attaix ◽  
Sophie Ventadour ◽  
Audrey Codran ◽  
Daniel Béchet ◽  
Daniel Taillandier ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Muscle Wasting ◽  
Proteolytic Enzymes ◽  
Cathepsin L ◽  
Ubiquitin Proteasome System ◽  
Complete Breakdown ◽  
Skeletal Muscle Proteins ◽  
Ubiquitin Proteasome ◽  
Tripeptidyl Peptidase Ii ◽  
F Box Protein

The ubiquitin–proteasome system (UPS) is believed to degrade the major contractile skeletal muscle proteins and plays a major role in muscle wasting. Different and multiple events in the ubiquitination, deubiquitination and proteolytic machineries are responsible for the activation of the system and subsequent muscle wasting. However, other proteolytic enzymes act upstream (possibly m-calpain, cathepsin L, and/or caspase 3) and downstream (tripeptidyl-peptidase II and aminopeptidases) of the UPS, for the complete breakdown of the myofibrillar proteins into free amino acids. Recent studies have identified a few critical proteins that seem necessary for muscle wasting {i.e. the MAFbx (muscle atrophy F-box protein, also called atrogin-1) and MuRF-1 [muscle-specific RING (really interesting new gene) finger 1] ubiquitin–protein ligases}. The characterization of their signalling pathways is leading to new pharmacological approaches that can be useful to block or partially prevent muscle wasting in human patients.

Rapid analysis of N-phenylpropenoyl-L-amino acids (NPA) from cocoa by UPLC and CE

Planta Medica ◽  
2010 ◽  
Vol 76 (12) ◽  
Author(s):  
M Lechtenberg ◽  
K Henschel ◽  
U Liefländer-Wulf ◽  
B Quandt ◽  
A Hensel
Keyword(s):  
Amino Acids ◽  
Rapid Analysis

Recent data on the causative agent of pale green dwarf (Acholeplasma laidlawii var. granulum incertae sedis) in Ukraine: pathogenicityand virulence factors and host reactions

2015 ◽  
Vol 2 (1) ◽  
pp. 30-34
Author(s):  
K. Korobkova ◽  
V. Patyka
Keyword(s):  
Phenylalanine Ammonia Lyase ◽  
Proteolytic Enzymes ◽  
Physiological State ◽  
Plant Cells ◽  
Temporary Increase ◽  
Adhesive Properties ◽  
The Impact ◽  
Signaling Interactions ◽  
Pale Green

Contemporary state of the distribution of mycoplasma diseases of cultivated crops in Ukraine was analyzed. The changes of the physiological state of plant cells under the impact of mollicutes were investigated. It was demonstrated that there is temporary increase in the activity of peroxidase, catalase, polyphenoloxidase, phenylalanine-ammonia-lyase at the early stages of interaction. The adhesive properties are changed in the mollicutes under the impact of plant lectin; there is synthesis of new polypeptides. It was determined that the phytopathogenic acholeplasma is capable of producing a complex of proteolytic enzymes into the culture me- dium. It was concluded that when plant cells are infected with acholeplasma, a number of signaling interactions and metabolic transformations condition the recognition of pathogenesis and ensure the aggregate response of a plant to stress in the form of defense reactions. It was assumed that some specifi cities of the biology of phy- topathogenic acholeplasma determine their avoiding the immune mechanisms of plants and promote long-term persistence of mollicutes.

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