Subject(s)
Cyclosporins/administration & dosage , Graft Survival/drug effects , Immunosuppression Therapy , Skin Transplantation , Animals , Antibodies, Bacterial/biosynthesis , Antibody Formation/drug effects , Cyclosporins/pharmacology , Rabbits , Streptococcus pneumoniae/immunology , Transplantation, HomologousSubject(s)
Autoantibodies/analysis , Anti-Glomerular Basement Membrane Disease/immunology , Antibodies, Antinuclear/analysis , Arthritis, Rheumatoid/immunology , Erythrocytes/immunology , Graves Disease/immunology , Humans , Lupus Erythematosus, Systemic/immunology , Mixed Connective Tissue Disease/immunology , Myasthenia Gravis/immunology , Rheumatoid Factor/analysis , Sjogren's Syndrome/immunology , Thyroiditis, Autoimmune/immunologyABSTRACT
Acute cartilage degradation was produced in rabbits by the intravenous injection of crude papain. This resulted in a significant rise in serum lysozyme in 97% of the animals, as well as a fall in the residual lysozyme content of auricular and costal cartilage. The rise in serum lysozyme paralleled the rise in serum chondroitin sulfate. The source of the rise in lysozyme appeared to be the release of extracellular, nonlysosomal lysozyme from the cartilage matrix. Serum lysozyme elevation in arthritic disorders may reflect cartilage degradation.
Subject(s)
Cartilage Diseases/enzymology , Disease Models, Animal , Muramidase/metabolism , Acute Disease , Animals , Arthritis/enzymology , Cartilage Diseases/chemically induced , Cartilage Diseases/metabolism , Cartilage, Articular/analysis , Cartilage, Articular/enzymology , Chondroitin/blood , Female , Male , Methods , Muramidase/blood , Muramidase/isolation & purification , Ovalbumin , Papain , RabbitsSubject(s)
Brain Neoplasms/diagnosis , Histiocytosis, Langerhans-Cell/diagnosis , Muramidase/cerebrospinal fluid , Brain Neoplasms/cerebrospinal fluid , Cerebrospinal Fluid/enzymology , Female , Glioma/cerebrospinal fluid , Glioma/diagnosis , Histiocytosis, Langerhans-Cell/cerebrospinal fluid , Humans , Lymphoma, Large B-Cell, Diffuse/cerebrospinal fluid , Lymphoma, Large B-Cell, Diffuse/diagnosis , Lymphoma, Non-Hodgkin/cerebrospinal fluid , Lymphoma, Non-Hodgkin/diagnosis , Male , Meningitis/cerebrospinal fluid , Neoplasm MetastasisSubject(s)
Intestinal Mucosa/metabolism , Kidney Failure, Chronic/metabolism , Nitrogen/metabolism , Potassium/metabolism , Starch/metabolism , Adolescent , Adult , Amino Acids/blood , Blood Urea Nitrogen , Clinical Trials as Topic , Creatinine/blood , Dietary Proteins/administration & dosage , Feces , Female , Humans , Intestinal Absorption , Male , Middle Aged , Nitrogen/blood , Nitrogen/urine , Potassium/blood , Potassium/urine , Sodium Chloride/administration & dosageSubject(s)
Immune System Diseases/blood , Immunoglobulin A/isolation & purification , Immunoglobulin Fragments/isolation & purification , Aged , Animals , Antibody Specificity , Antigen-Antibody Reactions , Chromatography, Gel , Ear Diseases/immunology , Electrophoresis, Starch Gel , Humans , Immune Sera , Immune System Diseases/immunology , Immunodiffusion , Immunoelectrophoresis , Immunoglobulin A/biosynthesis , Immunoglobulin M , Immunologic Techniques , Male , Molecular Weight , Rabbits/immunology , Skin Manifestations , SplenomegalyABSTRACT
The lysozyme content of human cartilage was measured by incubation of lyophilized, powdered cartilage in a variety of buffers and salt solutions, and the factors controlling the binding of lysozyme within cartilage were studied. Lysozyme was extracted from hyaline cartilage by buffers of pH greater than 9.0 by solutions 1 M in monovalent cations, and by solutions 0.12-0.40 M in divalent cations. The ability of cations to extract lysozyme from cartilage agreed with their known affinities for binding to chondroitin sulfate. The total extractable lysozyme content of five samples of human costal cartilage ranged from 1.45 to 3.36 mug lysozyme per mg of cartilage; for five samples of hyaline cartilage from peripheral joints the range was 0.80-3.03 mug lysozyme per mg of cartilage. Cartilage incubated in excess exogenous lysozyme could bind 0.053 equivalents of lysozyme per equivalent of chondroitin sulfate. Fibrocartilage and synovium from knee joints yielded no detectable lysozyme, despite the fact that synovium, a tissue rich in lysosomes, contained measurable quantities of beta-glucuronidase. Lysozyme extraction from cartilage was not augmented by incubation with streptolysin S. When incubation was carried out with mild extraction techniques, lysozyme extraction from cartilage tended to parallel uronic acid release, both as a function of time and from one specimen to another. The active material as lysozyme. Lysozyme occurs in human hyaline cartilage as a counterion to polyanionic glycosaminoglycans. Carextracted from cartilage met five criteria for identification tilage lysozyme appears to be extracellular and nonlysosomal. Degradation of cartilage may contribute to the increased serum and synovial fluid lysozyme levels often present in patients with rheumatoid arthritis.
