Variation with Ageing and Degeneration of the Serine and Cysteine Proteinase Inhibitors of Human Articular Cartilage

1986 ◽  
pp. 69-81
Author(s):  
P. Ghosh ◽  
J. L. Andrews ◽  
R. A. Osborne ◽  
M. S. Lesjak
Keyword(s):  
Articular Cartilage ◽  
Proteinase Inhibitors ◽  
Cysteine Proteinase ◽  
Human Articular Cartilage ◽  
Cysteine Proteinase Inhibitors

scholarly journals Cysteine Proteinase Inhibitors Decrease Articular Cartilage and Bone Destruction in Chronic Inflammatory Arthritis

1994 ◽  
Vol 37 (2) ◽  
pp. 236-247 ◽  
Author(s):  
Ronald E. Esser ◽  
Richard A. Angelo ◽  
Mark D. Murphey ◽  
Lynnetta M. Watts ◽  
Larry P. Thornburg ◽  
...  
Keyword(s):  
Articular Cartilage ◽  
Inflammatory Arthritis ◽  
Proteinase Inhibitors ◽  
Cysteine Proteinase ◽  
Bone Destruction ◽  
Chronic Inflammatory Arthritis ◽  
Cysteine Proteinase Inhibitors

Molecular Characterization and Mapping of Murine Genes Encoding Three Members of the Stefin Family of Cysteine Proteinase Inhibitors

Genomics ◽  
1993 ◽  
Vol 15 (3) ◽  
pp. 507-514 ◽  
Author(s):  
Florence W.L. Tsui ◽  
Hing-Wo Tsui ◽  
Samuel Mok ◽  
Irena Mlinaric ◽  
Neal G. Copeland ◽  
...  
Keyword(s):  
Molecular Characterization ◽  
Proteinase Inhibitors ◽  
Cysteine Proteinase ◽  
Cysteine Proteinase Inhibitors ◽  
Genes Encoding

scholarly journals The properties of proteoglycan prepared from human articular cartilage by using associative caesium chloride gradients of high and low starting densities

1985 ◽  
Vol 232 (1) ◽  
pp. 111-117 ◽  
Author(s):  
M T Bayliss ◽  
P J Roughley
Keyword(s):  
Hyaluronic Acid ◽  
Articular Cartilage ◽  
Proteinase Inhibitors ◽  
Density Gradient Centrifugation ◽  
Gradient Centrifugation ◽  
Human Articular Cartilage ◽  
Adult Human ◽  
Cscl Density Gradient ◽  
Proteoglycan Aggregates ◽  
Hyaluronic Acid Binding

Proteoglycan was extracted from adult human articular cartilage from both the knee and the hip, and A1 preparations were prepared by CsCl-density-gradient centrifugation at starting densities of 1.69 and 1.5 g/ml. Irrespective of whether the cartilage was diced to 1 mm cubes or sectioned to 20 micron slices there was always a lower proportion of both protein and proteoglycan aggregate in the A1 preparation prepared at 1.69 g/ml. Furthermore, the addition of exogenous hyaluronic acid to the extracts before centrifugation did not improve the yield of aggregate at 1.69 g/ml. These results were not affected by the presence of proteinase inhibitors in the extraction medium. It appears that adult human articular cartilage contains a high proportion of low-density proteoglycan subunits and hyaluronic acid-binding proteins that make most of the re-formed proteoglycan aggregates of a lower density than is usually encountered with younger human and mammalian hyaline cartilages.

scholarly journals Cystatins — Inhibitors of Cysteine Proteinases

1992 ◽  
Vol 3 (4) ◽  
pp. 307-332 ◽  
Author(s):  
Libuse A. Bobek ◽  
Michael J. Levine
Keyword(s):  
Common Ancestor ◽  
Molecular Level ◽  
Proteinase Inhibitors ◽  
Cysteine Proteinase ◽  
Diverse Group ◽  
Cysteine Proteinases ◽  
Future Directions ◽  
Cysteine Proteinase Inhibitors ◽  
Physicochemical And Functional Properties

The cystatin superfamily of proteins, derived from a common ancestor, is comprised of a diverse group of potent cysteine proteinase inhibitors and antibacterial/viral agents grouped into several families. This review concentrates on family 2 cystatins, namely, the human salivary cystatins and cystatin C. Emphasis is given to their physicochemical and functional properties at both the protein and the molecular level. The role of cystatins in disease processes, including those in the oral cavity, is also discussed. Finally, future directions for cystatin research in oral biology are presented.

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