The serum proteins in health and disease

Ogryzlo, M. A.; Maclachlan, Margaret J.; Dauphinee, Julie; Fletcher, A. A.

doi:10.1016/0002-9343(59)90045-2

Cited by 60 publications

(9 citation statements)

References 42 publications

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“…The frequently observed fall in albumin concentration accompanying elevations in globulin concentration is in agreement with this concept (27). In the present studies, the decrease in plasma oncotic pressure resulting from the decrease in albumin concentration was not compensated for by the increase in oncotic pressure calculated from the measured concentration of circulating dextran.…”

Section: Discussionsupporting

confidence: 92%

Studies on Albumin Synthesis: The Effects of Dextran and Cortisone on Albumin Metabolism in Rabbits Studied With Albumin-I131*

Rothschild¹,

Oratz²,

Wimer³

et al. 1961

J. Clin. Invest.

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Following plasmapheresis, the depressed serum albumin concentration rapidly returns to normal (1) indicating alterations in albumin synthesis or degradation. Both dextran administration (2-6) and elevation of serum globulin levels produced by means of hyperimmunization (7,8) are associated with hypoalbuminemia; a colloid osmotic regulatory mechanism has been suggested as responsible for the reciprocal changes in serum proteins observed after hyperimmunization (7, 9). If such a mechanism does exert control over the concentration of serum albumin, alterations of albumin metabolism either in the rate of synthesis or in the rate of degradation might be expected when osmotically active molecules other than albumin are added to the circulation. The present study represents an attempt to define, more specifically than heretofore reported, the changes in albumin metabolism resulting from such a procedure. Dextran was administered to rabbits to depress albumin concentration. After the development of hypoalbuminemia, the rates of albumin synthesis and degradation were studied and compared with control values. Cortisone acetate was then given to increase the rate of albumin degradation (10), and the rates of albumin synthesis were remeasured. METHODSFemale rabbits were used in all studies. Animals were kept in metabolism cages and fed a standard rabbit diet.

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Section: Discussionsupporting

confidence: 92%

Studies on Albumin Synthesis: The Effects of Dextran and Cortisone on Albumin Metabolism in Rabbits Studied With Albumin-I131*

Rothschild¹,

Oratz²,

Wimer³

et al. 1961

J. Clin. Invest.

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“…The first 10 proteins as indicated by PC2 are detailed in Supplementary Table 2; these proteins are found in similar amounts when BrCr Pt serum was analyzed twice and were not found in sera from HVs. This comes in line with previous reports indicating the difference in serum protein make-up in diseases 15,16,70 including breast cancer. 71 Supplementary Table 3 shows the 10 variable importance projections according to the first principal component; these proteins are found in the sera, but not in the NP coronas and contribute to the major difference observed between the sera and the coronas.…”

Section: ■ Results and Discussionsupporting

confidence: 93%

“…In most of the in vitro setups, NPs are incubated with cells usually in cell culture media either in the complete absence of serum , or in the presence of fetal bovine serum (FBS). − In both cases, these experiments are somewhat misleading because the former completely neglects the role of the protein corona in NP–cell interactions and the latter takes into account the effects of a protein corona that does not really represent the one forming in humans nor in the respective disease state. The latter becomes even more important because the serum proteomic profile changes with disease , including cancer − and that even the slightest variations in the protein source composition (e.g., plasma and serum from the same source) can alter the composition of the corona formed. , To that end, in vitro experiments evaluating active targeted NPs should be conducted in human sera of the respective diseases.…”

Section: Introductionmentioning

confidence: 99%

Different Serum, Different Protein Corona! The Impact of the Serum Source on Cellular Targeting of Folic Acid-Modified Chitosan-Based Nanoparticles

et al. 2022

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The nanoparticle (NP) protein corona represents an interface between biological components and NPs, dictating their cellular interaction and biological fate. To assess the success of cellular targeting, NPs modified with targeting ligands are incubated with target cells in serum-free culture medium or in the presence of fetal bovine serum (FBS). In the former, the role of the corona is overlooked, and in the latter, the effects of a corona that does not represent the one forming in humans nor the respective disease state are considered. Via proteomic analysis, we demonstrate how the difference in the composition of FBS, sera from healthy human volunteers, and breast cancer patients (BrCr Pt) results in the formation of completely different protein coronas around the same NP. Successful in vitro targeting of breast cancer cells was only observed when NPs were incubated with target cells in the presence of BrCr Pt sera only. In such cases, the success of targeting was not attributed to the targeting ligand itself, but to the adsorption of specific serum proteins that facilitate NP uptake by cancer cells in the presence of BrCr Pt sera. This work therefore demonstrates how the serum source affects the reliability of in vitro experiments assessing NP−cell interactions and the consequent success or failure of active targeting and may in fact indicate an additional reason for the limited clinical success of drug targeting by NPs in cancer.

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“…In this case there was hypogamma-globulin and cells resembling plasma-cells in the bone marrow. I n their series Ogryzlo et al (1959) found no indication of abnormal protein constituents of the type described by Arends et al (1954) and Azar et al (1957).…”

Section: Discussionmentioning

confidence: 71%

“…Studies of the serum proteins in our group of patients revealed low levels of gamma globulin in six out of ten cases with chronic lymphocytic leukemia. Ogryzlo et al (1959) found low gammaglobulin in six out of twelve cases with chronic lymphocytic leukemia. In four of our cases there was a history of zoster infection.…”

Section: Discussionmentioning

confidence: 85%