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Biomedical subjects

C A Krakower

Publications and source records attributed to C A Krakower.

14 recordsLinked to original sources
PubMed1983

The susceptibility of the mesangial matrix of isolated cell-free glomeruli to limited proteolysis.

Selective lysis of mesangial matrix can be achieved by limited proteolysis of isolated cell-free glomeruli. Such treated glomeruli present unfolded and confluent capillary loops forming irregularly shaped, saccular lobular structures, comparable to those described for chemical mesangiolysis. It was observed that the parietal capsules of the glomeruli were also susceptible to limited proteolysis by comparison with the resistance of the basement membranes of the peripheral capillary loops.

Animals↗
PubMed1980

Mesangiolysis of isolated renal glomeruli with the formation of lobular sacs or cysts.

60% trichloracetic acid (TCA) will dissolve the cells and mesangial matrix of isolated renal glomeruli before it dissolves the basement membranes (BM). With the removal of the mesangial cells and matrix, the paramesangial BM stands out in sharp relief. It is thicker than that of the capillary loops and is provided with prominent ridges and spurs. These thick collars of BM now border the narrow channels left after the removal of the mesangium. The channels communicate with the capillary lumens. They widen asynchronously with the continued action of the TCA leading at first to more axial cavitation of the lobules of the glomerulus and finally to the conversion of these lobules into sacs or cysts. This is brought about by the unfolding of the capillaries within the investing sheath of BM which is common to the capillary loops and the widened stalks and intercapillary axial portions of the mesangium.

Animals↗
PubMed1975

Biochemical, morphological and hybrid studies in hyperprolinemic mice.

Hyperprolinemia, hyperprolinuria and hydroxyprolinuria were observed in PRO/Re mice. Hepatic proline oxidase activity in PRO/Re mice was markedly deficient. It was demonstrated that the deficiency of proline oxidase activity was not due to the presence of an inhibitor. The mutant enzyme in PRO/Re showed no difference in heat stability but had a poor affinity for the substrate, L-proline as compared to normal enzymes. There was no significant proteinuria or hematuria in PRO/Re mice. Their serum protein and blood urea nitrogen were normal. Morphologic studies by light and electron microscopy demonstrated no abnormality in the renal tissues of PRO/Re up to 6 months of age, suggesting that hyperprolinemia did not cause renal damage. Pedigree studies showed that F1 generation (PRO/Re x CD 1) had approximately 50 percent of normal proline oxidase activity and significantly higher plasma proline. The distribution of hepatic proline oxidase activity in F2 GENERATION (F1 x F1) was characteristic of an autosomal recessive trait.

Amino Acid Metabolism, Inborn Errors↗
PubMed1973

The importance of the included serum proteins in the immune response in rabbits to a rat skin xenograft.

Various substances were isolated from rat skin including, protein-dermatan sulfate, certain other species of heavy and light protein-mucopolysaccharides, five electrophoretically separable nonstructural glycoproteins and a crude and two "purified" variants of structural glycoproteins. When the serum proteins contaminating these substances were removed as completely as possible, none of these produced an accelerated immune response to a rat skin graft in appropriately preimmunized rabbits, and none of those that were tested had a blocking effect on the immune response. On the other hand, the contaminated products and undenatured and denatured rat serum produced accelerated immune responses to a rat skin graft in appropriately preimmunized rabbits. These observations, together with those on skin reactions to the isolated products and to rat serum in rabbits sensitized by rat skin grafts, emphasize the importance of the included serum proteins in the immune response to this type of xenograft.

Adsorption↗