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Relationship between insulin secretion, insulin content and dry weight of single rat pancreatic islets.

Single islets were incubated at glucose 5 mM for 60 min and subsequently at glucose 15 nM for 30 min. The insulin content of the incubated islets was proportional to the dry weight of the islets. The insulin secretion (Y) demonstrated a curvilinear relationship with the dry weight (X) of the islets, which could be described by the function Y = aX2/3 (a being a constant). On basis of this function it can be calculated that the insulin secretion of a particular islet is proportional to its outer surface. The consequence of this is that small sized islets secrete relatively much more insulin than large islets. Islets isolated with either purified or crude collagenase gave the same results except that a higher basal insulin secretion was observed with crude collagenase.

Animals↗

[Inhibition of PZ-peptidases by serum (author's transl)].

The inhibition of two PZ-peptidases by several sera was studied with the aid of methods based on the PZ-peptidase assay of Wünsch and Heidrich Clostridiopeptidase A is inhibited by all sera, whilst the PZ-peptidase from the rabbit serum is inhibited only by heterologous sera. The inhibition is weak and cannot be compared with the strong serum inhibition shown by collagenases.

Animals↗

Osteoblast collagenase: collagenase synthesis by clonally derived mouse osteogenic (MC3T3-E1) cells.

Latent collagenase was isolated by heparin-Sepharose affinity chromatography from the culture medium of clonally derived mouse osteogenic (MC3T3-E1) cells. Collagenase synthesis by MC3T3-E1 cells was significantly stimulated by the addition of parathyroid hormone to the serum-containing culture medium. The cellular origin of the isolated collagenase was confirmed by demonstrating the characteristic 3/4 and 1/4 fragments of collagen alpha-chain, as well as inhibition of the enzyme by anti-mouse bone collagenase antibody.

Animals↗

Collagenase in synovial fluid.

Free collagenase activity was demonstrated in all 13 normal, 5 osteoarthrotic and 54 rheumatoid synovial fluids studied. Osteoarthrotic, normal, and rheumatoid fluids showed a free collagenase content increasing in that order. However, the total activities after trypsin activation did not differ significantly. The concentrations of alpha1-at and alpha2-M in synovial fluids reflected those in sera. The complex interactions between serum inhibitors, and free or latent collagenase released from both synovial cells and leukocytes are discussed.

Arthritis, Rheumatoid↗