The Effect of Hypergammaglobulinemia on Albumin Metabolism in Hyperimmunized Rabbits Studied With Albumin-I131*

Rothschild, Marcus A.; Oratz, Murray; Franklin, Edward C.; Schreiber, Sidney S.

doi:10.1172/jci104613

Cited by 51 publications

(24 citation statements)

References 18 publications

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“…These results agree with what has been noted at low albumin levels, namely, that albumin synthesis does not respond to changes in albumin concentrations per se (12,18,19). It had been proposed that albumin syn-thesis may be controlled by a regulatory system responding to changes in colloid osmotic pressure; however, the infusions were isosmotic with the plasma, and a change in colloid osmotic pressure probably did not occur (12,19). Apparently, therefore, when albumin concentrations or pool size are increased, as in the present study, or diminished as in proteinuria (18), changes in albumin degradation are predominant.…”

Section: Discussionsupporting

confidence: 92%

“…Apparently, therefore, when albumin concentrations or pool size are increased, as in the present study, or diminished as in proteinuria (18), changes in albumin degradation are predominant. In contrast, the administration of dextran or the production of persistently elevated gamma globulin levels results in a reduction in the rate of albumin synthesis rather than a change in the rate of degradation (12,19). In the presence of an exogenous source of serum protein, albumin levels are maintained primarily by an increase in albumin degradation, indicating that albumin degradation and synthesis change independently of each other.…”

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Alterations in Albumin Metabolism after Serum and Albumin Infusions*

Rothschild¹,

Oratz²,

Evans³

et al. 1964

J. Clin. Invest.

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The intravenous administration of whole serum or of serum albumin results in a temporary increase in the concentration of circulating protein; the rate of return toward preinfusion levels depends upon the state of protein depletion or pool size and upon the rates of synthesis and degradation of albumin (1-6). Much of the infused protein can be accounted for by increased nitrogen excretion in the urine (2-4); the remainder has been assumed to be stored in intravascular or extravascular areas (1-6). The rate of disappearance of tracer-labeled homologous and heterologous albumin from plasma has been observed to increase during the infusion of whole serum or of serum albumin (6-7). Thus, although there is an increase in protein degradation associated with at least a temporary storage of protein, observations on the changes in endogenous protein synthesis and degradation that might follow such infusions are not available. The effects of prolonged infusions of pooled homologous serum or salt-poor human serum albumin on albumin metabolism in rabbits tolerant to human albumin are reported in the present study. MethodsFemale rabbits were used in all studies and were fed a standard Rockland rabbit ration. The rabbits were kept in metabolism cages, and complete urine and stool collections were made daily. Endogenous albumin metabolism was measured with rabbit albumin labeled with I' in all studies. Lugol's solution (2 to 3 drops) was added to the animals' drinking water daily to inhibit the thyroidal uptake of I' released from degraded protein.* Submitted for publication April 22, 1964; accepted June 11, 1964. A preliminary report of this work appeared in Clin. Res. 1964, 12, 279. This investigation was supported in part by grant no. A-2489 from the U. S. Public Health Service.The procedures for separating rabbit albumin from pooled rabbit serum and labeling with I' have been described previously (8-9). Two groups of rabbits were studied. The first group of 12 rabbits received whole rabbit serum.1 After the intravenous injection of 30 to 300 uc of rabbit albumin 131 (RSA-I"'), 0.6 to 0.8 ml of heparinized blood was obtained from the ear opposite to the side of injection 6 and 10 minutes later and daily thereafter for a control period of 10 to 12 days. Daily infusions of 20 to 30 ml of pooled serums containing 530 to 935 mg of albumin (equivalent to 105 to 207 mg of albumin per kg body weight) were then started and continued for 18 to 24 days while observations on plasma, urine, and stool radioactivity were continued. At this time, and while the infusions were continued, a second injection of albumin I131 was made to remeasure albumin distribution and pool size. Plasma samples were obtained just before the serum infusion for that day.A second group of 6 rabbits, tolerant to human serum albumin, was also studied. Seventy-five to 100 ,uc of rabbit albumin I' was injected intravenously, and control values were obtained for 7 to 10 days as described above. The rabbits then received between 125 and 150 mg of human albumin per...

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Section: Discussionsupporting

confidence: 92%

Section: Discussionmentioning

confidence: 99%

Alterations in Albumin Metabolism after Serum and Albumin Infusions*

Rothschild¹,

Oratz²,

Evans³

et al. 1964

J. Clin. Invest.

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“…This result is similar to the observations in human myeloma and in hyperimmunized animals where in the presence of hypergammaglobulinemia the gamma globulin half-life is usually shortened (18,19). The lack of effect of AD on albumin half-life is also in accord with studies on hypergammaglobulinemic rabbits (20), and is probably related to different degradatory mechanisms for these two serum proteins.…”

Section: Serum Proteinsupporting

confidence: 89%

Metabolism and Function of Gamma Globulin in Aleutian Disease of Mink

Porter

Dixon

Larsen

1965

The Journal of Experimental Medicine

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Aleutian disease-affected mink, which are markedly hypergammaglobulinemic, show a decreased half-life of the serum gamma globulin indicating that the hyperglobulinemia is due to increased production. No evidence that the gamma globulin was antibody to the infectious agent, to autologous or isologous tissues, or to antigens the animal was responding to prior to development of the disease was obtained. The increased gamma globulin was found to be of the 6.4S variety, and gamma globulin containing protein-protein complexes of 9S to 17S and 22S to 25S classes were observed in serums of affected mink. The findings are most consistent with the Aleutian disease virus acting as a direct and somewhat selective stimulus to plasma cell proliferation. There is no evidence that the arterial and glomerular lesions of Aleutian disease have an immunologic pathogenesis. It seems possible that these vascular changes may be directly caused by the viral agent, or may be the result of the increased gamma globulin levels.

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“…In a series of papers based on experimental reduction and expansion of the albumin pool size Rothschild and his colleagues (36)(37)(38)(39) concluded that the quantity of albumin degraded was related to albumin concentration or pool size. It would be of interest to know whether a fall in albumin catabolic rate is brought about by reduction of the serum albumin concentration or by contraction of either the intra-or extravascular pool.…”

Section: 26) Cohen and Hansenmentioning

confidence: 99%

“…These findings may correspond to our plasmapheresis experiments with ad libitum feeding and suggest that albumin synthesis will increase when protein is lost from the body, provided dietary nitrogen is adequate. In their series of experiments Rothschild and his colleagues (36)(37)(38)(39) concluded that synthesis of albumin was regulated by the colloidal osmotic pressure of plasma, not by the albumin concentration. This problem may not finally be answered until a direct method of measuring albumin synthesis is applied.…”

Section: 26) Cohen and Hansenmentioning

confidence: 99%