scholarly journals The role of monocytes in serum sickness nephritis.

1979 ◽  
Vol 150 (3) ◽  
pp. 413-425 ◽  
Author(s):  
L G Hunsicker ◽  
T P Shearer ◽  
S B Plattner ◽  
D Weisenburger

We have investigated the pathogenesis of glomerular hypercellularity seen in acute serum sickness nephritis induced in rabbits with bovine serum albumin (BSA). The increase in cellularity began with the first stages of immune clearance of BSA, with a peak cellularity occuring at the time of onset of proteinuria. Although there was a significant increase in the fraction of glomerular cells incorporating [3H]thymidine, first seen at the onset of proteinuria, this increase occurred too late and was too small to explain the observed rate of increase in glomerular cellularity. On the other hand, a striking monocytic infiltration of the glomeruli was documented by electron microscopy and by staining for nonspecific esterase. This monocytic infiltration paralleled the observed course of glomerular hypercellularity and was quantitatively sufficient to explain the total increase seen. It appears, therefore, that glomerular hypercellularity seen in this model is principally a result of monocyte infiltration.

Author(s):  
L. J. Brenner ◽  
D. G. Osborne ◽  
B. L. Schumaker

Exposure of the ciliate, Tetrahymena pyriformis, strain WH6, to normal human or rabbit sera or mouse ascites fluids induces the formation of large cytoplasmic bodies. By electron microscopy these (LB) are observed to be membrane-bounded structures, generally spherical and varying in size (Fig. 1), which do not resemble the food vacuoles of cells grown in proteinaceous broth. The possibility exists that the large bodies represent endocytic vacuoles containing material concentrated from the highly nutritive proteins and lipoproteins of the sera or ascites fluids. Tetrahymena mixed with bovine serum albumin or ovalbumin solutions having about the same protein concentration (7g/100 ml) as serum form endocytic vacuoles which bear little resemblance to the serum-induced LB. The albumin-induced structures (Fig. 2) are irregular in shape, rarely spherical, and have contents which vary in density and consistency. In this paper an attempt is made to formulate the sequence of events which might occur in the formation of the albumin-induced vacuoles.


1998 ◽  
Vol 88 (3) ◽  
pp. 260-264 ◽  
Author(s):  
María L. Boyd ◽  
Lori M. Carris

The effect of activated charcoal as an amendment to water agar medium on teliospore germination was analyzed for two species of wheat-infecting bunts, Tilletia controversa and T. tritici, and two related wild-grass infecting species, T. bromi and T. fusca. Final percentages of teliospore germination, area under the germination progress curves (AUGPC), and a standardized AUGPC (SAUGPC) on carbon agar and water agar were compared among strains. Carbon agar (CA) significantly increased the final germination percentage of teliospores, AUGPC, and SAUGPC when compared with water agar (WA) for all taxa under study. Additionally, CA reduced significantly the incubation (i.e., lag) period when compared with WA for teliospores of T. bromi, T. controversa, and T. fusca. Bovine serum albumin and polyvinyl pyrrolidone were used as alternative chemical adsorbent amendments to WA to establish the role of activated charcoal in the medium. Only media amended with bovine serum albumin and activated charcoal improved the final germination percentage of all taxa. Polyvinyl pyrrolidone was not significantly better than water agar.


1963 ◽  
Vol 41 (4) ◽  
pp. 931-939 ◽  
Author(s):  
J. H. Linford

Two proteins, haemoglobin and bovine serum albumin, have been studied with respect to their rates of alkylation by chlorambucil in vitro at 37 °C and pH 8.4. The proteins are of nearly the same molecular weight and free carboxylic acid content, but the alkylation reaction is 30 times faster with haemoglobin. On the other hand, the adsorption of chlorambucil by albumin is 20 times greater than that exhibited by haemoglobin. This inverse relationship between extent of adsorption and reaction rate suggests that adsorption protects the chlorambucil from activation in the solvent.


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