alpha 2-Macroglobulin in joint disease.
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Arthritis, Rheumatoid↗
Biomedical subjects
W Borth
Publications and source records attributed to W Borth.
Rheumatoid-like synovitis in rabbits by intra-articular administration of alpha 2-macroglobulin . trypsin complexes and alkylamine-treated alpha 2-macroglobulin.
The present animal experiments revealed that repeated intra-articular administration of alpha 2-macroglobulin . trypsin complexes caused a rheumatoid-like synovitis in not preimmunized rabbits. In early stages of synovitis, acute to subacute pathomorphological alterations were observed. In later stages, the chronic infiltration was accomplished by early onset of fibroplasia in some experimental joints. Similar lesions were caused by administration of methylamine-treated alpha 2-macroglobulin, an inactive alpha 2-macroglobulin (alpha 2-M), very like that produced in the trapping of a proteinase. In contrast, administration of native plasma alpha 2-M was ineffective, whereas active trypsin produced moderate inflammation. It is felt that the present experimental model resembles immunopathological processes in human arthritides, where the occurrence of alpha 2-M . proteinase complexes was verified.
Animals↗
Human serum inhibitors of collagenase as revealed by preparative isoelectric focusing.
Single step separation of pooled normal human serum by means of preparative isoelectric focusing in the range from pH 3.5--9.8 revealed more heterogeneous inhibition of collagenolytic activity than previously reported. Essentially three inhibition zones were resolved. According to their electrophoretic behaviour the respective serum fractions displaying inhibitory activity were designated alpha-, beta- and gamma-collagenase inhibitors. The main component responsible for collagenase inhibition in the alpha-zone was found to be alpha 2-macroglobulin. In the beta-zone inhibitory activity focused around pH 6.3. In the gamma-range a non-dialysable cationic component focusing at pH 9.2 was also able to decrease collagenolytic activity derived from rheumatoid arthritis synovial culture supernatant. These findings were supported by single step separation of serum on DEAE-anion exchange chromatography.
Acetic Anhydrides↗