Superficial zone chondrocytes in normal and osteoarthritic human articular cartilages synthesize novel truncated forms of inter-alpha-trypsin inhibitor heavy chains which are attached to a chondroitin sulfate proteoglycan other than bikunin

Author:

Yoshihara Y.,Plaas A.,Osborn B.,Margulis A.,Nelson F.,Stewart M.,Rugg M.S.,Milner C.M.,Day A.J.,Nemoto K.,Sandy J.D.

Publisher

Elsevier BV

Subject

Orthopedics and Sports Medicine,Biomedical Engineering,Rheumatology

Reference34 articles.

1. Human inter-alpha-trypsin inhibitor. Isolation and characterization of heavy (H) chain cDNA clones coding for a 383 amino-acid sequence of the H chain;Salier;Biol Chem Hoppe Seyler,1988

2. Organization of the inter-alpha-inhibitor heavy chains on the chondroitin sulfate originating from Ser(10) of bikunin: posttranslational modification of inter-alpha-inhibitor-derived bikunin;Enghild;Biochemistry,1999

3. Mechanism of action of inter-alpha-trypsin inhibitor;Pratt;Biochemistry,1987

4. Inter-alpha-trypsin inhibitor-related immunoreactivity in human tissues and body fluids;Businaro;Cell Mol Biol,1992

5. Immunohistochemical investigation of inter-alpha-trypsin inhibitor in the urinary tract;Odum;APMIS,1989

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