alpha-chymotrypsin and Joint-Diseases

Light chain Inc, obtained from a patient with amyloid arthropathy, has an Mr of 23,550 and consists of 219 amino acid residues. The complete primary structure of its variable domain has been determined by sequence analysis of the corresponding tryptic peptides, aligned by fragments derived from cyanogen bromide digestion, and by partially sequencing the intact protein. Although closely related to protein of the V kappa II subgroup, light chain Inc differs from its counterpart by the replacement of some invariant residues in its variable domain. By comparing its sequence with that of the nonamyloid kappa II Nim, a different distribution of some polar and apolar amino acid residues through the molecule is evidenced. A computer graphic analysis shows that some of the replaced amino acid residues cannot be readily accommodated in the known three-dimensional structure of the immunoglobulin light chains.

Topics: Amino Acid Sequence; Amino Acids; Amyloid; Chromatography, Gel; Chromatography, High Pressure Liquid; Chymotrypsin; Cyanogen Bromide; Female; Humans; Immunoglobulin kappa-Chains; Joint Diseases; Macromolecular Substances; Middle Aged; Molecular Sequence Data; Molecular Weight; Peptide Fragments; Trypsin

Thirteen post-partum patients with symphysiolysis were treated by intra-symphysial injection of a combination of hydrocortisone, chymotrypsin and lidocain. The injection was given once a day and the full treatment consisted of between three to seven injections according to the severity of the symptoms. No other medication was given. Immediate relief was obtained in all cases after the first injection and all symptoms disappeared after the completion of treatment. The average time of hospitalization was 9.8 days. No complications were seen as a result of the treatment and the patients resumed their normal activities after being discharged from hospital. In comparison with other modes of treatment, the intra-symphysial injection of the above drug combination shortened the time of morbidity and effected complete recovery.

Topics: Adult; Chymotrypsin; Drug Therapy, Combination; Female; Humans; Hydrocortisone; Joint Diseases; Lidocaine; Ligaments; Pregnancy; Pubic Symphysis; Puerperal Disorders; Rupture, Spontaneous

The present work was undertaken to explore the effect of two purified neutral proteases derived from human peripheral blood polymorphonuclear leukocytes (PMN) on articular cartilage as a model of joint injury. Human leukocyte elastase and chymotrypsin-like enzyme, purified by affinity chromatography, released 32SO4 from labeled rabbit articular cartilage slices in vitro. Release of isotope was initially delayed, suggesting that either a lag in enzyme penetration occurs or that size of degradation fragments is a limiting factor in diffusion of label out of the tissue. The release of 35SO4 was inhibited by preincubation of elastase and chymotrypsin-like enzyme with human alpha 1-anti-trypsin, or with their specific chloromethyl ketone inactivators, and the action of elastase was also inhibited by a monospecific antiserum to PMN elastase, freed of major serum proteinase inhibitors. Immunohistochemical staining procedures revealed the presence of PMN elastase inside the matrix of cartilage slices after a 20-min exposure of tissue to either the pure enzyme or crude PMN granule extract. Serum alpha 1-antitrypsin failed to penetrate into the cartilage slices under identical in vitro conditions. In association with the results reported in the accompanying paper, these findings suggest a model of cartilage matrix degradation by PMN neutral proteases in which local protease-antiprotease imbalance, coupled with different rates of penetration of protease and antiprotease into target tissue, plays a key role in accounting for matrix damage.

Topics: alpha 1-Antitrypsin; Animals; Cartilage, Articular; Chymotrypsin; Cytoplasmic Granules; Disease Models, Animal; Enzyme Inhibitors; Glycosaminoglycans; Humans; Immune Sera; Joint Diseases; Kinetics; Leukocytes; Oligopeptides; Pancreatic Elastase; Peptide Hydrolases; Phenylalanine; Proteoglycans; Rabbits; Sulfur Radioisotopes

Extracts of human peripheral blood polymorphonuclear leukocyte granules, and two purified proteases derived from such extracts, an elastase and a chymotrypsin-like enzyme, degrade isolated bovine nasal cartilage proteoglycan at neutral pH. Viscosity studies indicate that the leukocyte granule extracts lack hyaluronidase activity and that their degradative effect on proteoglycan at physiological pH is due entirely to proteolytic action. Sepharose 4B gel chromatography and SDS-polyacrylamide gel electrophoresis of proteoglycan fractions treated with leukocyte granule enzymes at pH 7.0 indicate that they degrade one of the proteoglycan link proteins, release a fragment from the hyaluronic acid-binding portion of the proteoglycan subunit core protein, and break down the remainder of the proteoglycan subunit molecule into peptide fragments with varying numbers of chondroitin sulfate chains. Immunodiffusion studies indicate that the antigenic determinants of the proteoglycan subunit core protein and the link proteins survive treatment with granule proteases. Similar degradation of human articular cartilage proteoglycan by granule neutral proteases can be presumed to occur, in view of the similarity of structure of human articular and bovine nasal cartilage proteoglycans. The release of granule enzymes in the course of neutrophil-mediated inflammation can thus result in the degradation of cartilage matrix proteoglycan, leading to cartilage destruction and joint injury.

Topics: Animals; Arthritis; Cartilage, Articular; Cattle; Chemical Phenomena; Chemistry; Chondroitin Sulfates; Chromatography, Gel; Chymotrypsin; Cytoplasmic Granules; Disease Models, Animal; Electrophoresis, Polyacrylamide Gel; Glycosaminoglycans; Humans; Immunodiffusion; Joint Diseases; Leukocytes; Nasal Septum; Pancreatic Elastase; Proteoglycans; Sodium Dodecyl Sulfate; Viscosity

Topics: Anti-Inflammatory Agents; Chymotrypsin; Fibrinolysin; Humans; Infusions, Parenteral; Injections, Intra-Articular; Joint Diseases; Peptides; Protease Inhibitors; Rheumatic Diseases; Sciatica; Trypsin

Topics: Adolescent; Adult; Brain Concussion; Brain Edema; Chymotrypsin; Female; Fracture Fixation; Hemarthrosis; Hematoma; Humans; Joint Diseases; Male; Middle Aged; Wounds and Injuries

Topics: Administration, Sublingual; Chymotrypsin; Fractures, Bone; Humans; Joint Diseases; Tablets

Topics: Analgesics; Analgesics, Non-Narcotic; Antipyretics; Chymotrypsin; Humans; Joint Diseases; Musculoskeletal System; Oxyphenbutazone; Traumatology; Trypsin