Demonstration of protein-losing gastroenteropathy the disappearance rate of 51Cr from plasma and the binding of 51Cr to different serum proteins

Tongeren, J. H. M. Van; Majoor, C.L.H.

doi:10.1016/0009-8981(66)90061-1

Cited by 59 publications

(14 citation statements)

References 11 publications

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“…Studies of thoracic fluid proteins of a patient with a rapidly accumulating chylous thoracic effusion and of the urine protein in a nephrotic patient confirmed this hypothe- 4 It was recently reported that 10 days after the intravenous administration of Cls51Cr the majority of radioactivity was in the globulin fraction and could be precipitated by antitransferrin (51). A shift of 5'Cr from albumin to transferrin did not take place when incubated with serum saturated with iron (52). In our studies no experiments with antitransferrin were made, and no information about transferrin binding was obtained.…”

Section: Discussioncontrasting

confidence: 53%

Use of 125I- and 51Cr-Labeled Albumin for the Measurement of Gastrointestinal and Total Albumin Catabolism*

Kerr¹,

Bois²,

Holt³

1967

J. Clin. Invest.

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Abstract. A method for the simultaneous measurement of gastrointestinal protein loss and total albumin turnover entailing the use of a combination of 125iodine-and 51chromium-labeled albumin is described. Albumin turnover was calculated by the measurement of albumin-125I plasma decay and cumulative urinary excretion, and the results obtained agreed closely with previous studies utilizing albumin-'31I. Gastrointestinal catabolism was calculated from the rate of fecal excretion of 51Cr and the specific activity of plasma albumin-51Cr, and these data were related to the calculated albumin turnover results. During the period of 6-14 days after administration, the ratio of specific activties of albumin-125I and -51Cr in plasma and in extravascular spaces or gastric and biliary secretions remained almost identical. Fecal excretion of 51Cr was also quite stable at this time. In six normal subjects gastrointestinal catabolism accounted for less than 10% of total albumin catabolism. Excessive gastrointestinal protein losses did not contribute to the low serum albumin in three patients with cirrhosis or in two adults with the nephrotic syndrome. Multiple mechanisms leading to hypoalbuminemia were demonstrated in other subjects with a variety of gastrointestinal disorders.

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Section: Discussioncontrasting

confidence: 53%

Use of 125I- and 51Cr-Labeled Albumin for the Measurement of Gastrointestinal and Total Albumin Catabolism*

Kerr¹,

Bois²,

Holt³

1967

J. Clin. Invest.

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“…Moreover, it is well known that Cr ions bind to serum proteins, such as albumin and transferrin, known to play scavenger role by binding and transporting these ions. [39][40][41] However, the effect of serum protein on the potency of Cr ions in inducing the nitration of proteins is not known.…”

Section: +mentioning

confidence: 98%

Cobalt and chromium ions induce nitration of proteins in human U937 macrophages in vitro

Petit

Mwale

Tkaczyk

et al. 2006

J Biomedical Materials Res

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The in situ localization of nitrotyrosine, a product of the nitration of tyrosine residues by peroxynitrite, in the interface membranes from Co--Cr--Mo and Ti--Al--V prostheses provided evidence of nitric oxide-induced oxidative damage in the periprosthetic environment. In the present study, we compared the effects of different wear products from hip prostheses on the nitration of proteins in macrophages in vitro. Nitration of proteins was measured by Western blot using a polyclonal antibody directed against nitrotyrosines. Results showed that Co(2+) and Cr(3+) ions induced the nitration of a 79 +/- 4 kDa protein in a time- and dose-dependent manner. Indeed, the stimulation was significant (p < 0.05) after 24 h with 10 ppm Co(2+) and reached a plateau level between 48 and 72 h. With Cr(3+), the stimulation was significant (p < 0.05) only after 48 and 72 h. The effect of both Co(2+) and Cr(3+) ions was inhibited by glutathione monoethyl-ester that provides protection against oxidative stress. However, ultrahigh-molecular-weight-polyethylene and alumina ceramic particles had no significant effect on the nitration of proteins. Finally, the results showed that nitrated proteins are mainly found in the cytoplasmic fraction of cells and are absent from the nucleus. In conclusion, our results show that Co(2+) and Cr(3+) ions induce the nitration of cytoplasmic proteins in human U937 macrophages, suggesting that metal ions from MM prostheses have the potential to modify protein function in the periprosthetic environment and in circulating cells.

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“…The am ount of this *1 parallels the protein loss. It can be estim ated by means of 51CrCl3 (or 51Cr-albumin) [12] and 59Fe-labelled iron dextran [5]. However, it is the reabsorption of this *1 th at determines the fraction ultim ately excreted in the stools.…”

Section: Repeated Studies Following Remissionmentioning

confidence: 99%

Topographic Diagnosis of Gastrointestinal Protein Loss

Westergaard¹,

Jarnum²,

Jensen³

et al. 1968

Digestion

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Demonstration of protein-losing gastroenteropathy the disappearance rate of 51Cr from plasma and the binding of 51Cr to different serum proteins

Cited by 59 publications

References 11 publications

Use of 125I- and 51Cr-Labeled Albumin for the Measurement of Gastrointestinal and Total Albumin Catabolism*

Use of 125I- and 51Cr-Labeled Albumin for the Measurement of Gastrointestinal and Total Albumin Catabolism*

Cobalt and chromium ions induce nitration of proteins in human U937 macrophages in vitro

Topographic Diagnosis of Gastrointestinal Protein Loss

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