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The Role of Cathepsins in Osteoimmunology
Critical Reviews in Eukaryotic Gene Expression, 2013Cathepsins are proteases comprising two small groups of serine and aspartic cathepsins and a large group of lysosomal cysteine cathepsins. Most of them are ubiquitously expressed throughout human tissues but some of them display a more restricted expression pattern and are involved in explicit tasks such as collagen degradation in the process of bone ...
Ursula Föger-Samwald +3 more
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Current Medicinal Chemistry, 2006
Cathepsin B is an abundant and ubiquitously expressed cysteine peptidase of the papain family. It is involved in many physiological processes, such as remodeling of the extracellular matrix (wound healing), apoptosis, and activation of thyroxine and renin.
Stanislav Gobec, Rok Frlan
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Cathepsin B is an abundant and ubiquitously expressed cysteine peptidase of the papain family. It is involved in many physiological processes, such as remodeling of the extracellular matrix (wound healing), apoptosis, and activation of thyroxine and renin.
Stanislav Gobec, Rok Frlan
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The action of cathepsin B and collagenolytic cathepsin in the degradation of collagen
1977Cathepsin B and collagenolytic cathepsin were obtained from bovine spleen and human placenta and identified as thiol proteinases. Both enzymes degraded insoluble fibrous collagen maximally at pH 3.5 and soluble monomeric collagen near pH 4.5. The response to activators and inhibitors was similar for both enzymes.
D J, Etherington, P J, Evans
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Intracellular distribution of cathepsin B and cathepsin C in rat liver
Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation, 1966Summary 1. The intracellular distribution of cathepsin B and cathepsin C (EC 3,4,4.9) in rat liver has been investigated by means of differential and density-equilibrium centrifugation, activation and solubilization experiments. 2. The enzymes appear to be localized in the lysosomes.
Max Gruber, J.M.W. Bouma
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Purification and properties of rabbit liver cathepsin M and cathepsin B
Archives of Biochemistry and Biophysics, 1985Cathepsins M and B from rabbit liver lysosomes were separated by chromatography on Ultrogel AcA34 at low ionic strength and purified to homogeneity, and their catalytic and molecular properties were compared. Cathepsin M was relatively inactive with synthetic peptide substrates.
Erickson Viitanen S +5 more
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1977
Cathepsin D was purified from human liver by a procedure involving autolysis, acetone fractionation, and chromatography on ion-exchange media and organomercurial-sepharose. Multiple forms of the enzyme were then separated by preparative isoelectric focusing. The molecular weight of the protein was found to be 43,000.
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Cathepsin D was purified from human liver by a procedure involving autolysis, acetone fractionation, and chromatography on ion-exchange media and organomercurial-sepharose. Multiple forms of the enzyme were then separated by preparative isoelectric focusing. The molecular weight of the protein was found to be 43,000.
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Cathepsin S inhibitors: WO2010070615
Expert Opinion on Therapeutic Patents, 2011This article evaluates a patent application of the company Medivir (SE/UK) describing the synthesis of dipeptide-derived α-ketoamides containing a propylene glycine moiety in P1 as selective inhibitors of cathepsin S for the potential treatment of various systemic human diseases such as several autoimmune diseases, MS, rheumatoid arthritis ...
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Purification of Bovine Spleen Collagenolytic Cathepsin (Cathepsin N)
Biochemical Society Transactions, 1978Andre Ducastaing, David J. Etherington
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