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Clinical Chemistry 51: 1750-1751, 2005; 10.1373/clinchem.2005.053819
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(Clinical Chemistry. 2005;51:1750-1751.)
© 2005 American Association for Clinical Chemistry, Inc.

Letters to the Editor

High {gamma}-Glutamyltransferase (GGT) Activity in Human Breast Milk Confounds Interpretation of High Serum GGT Activity in a Nursing Infant with Liver Disease

Dorothy B. Colagiovanni1,a, Dennis J. Meyer1, Julie M. Wolf1, Karen Hart1, Elizabeth Abbott1 and Corrie Santos2

1 OSI Pharmaceuticals, Inc., Boulder, CO
2 University of Colorado at Denver, Health Sciences Center, Department of Geography, and Environmental Sciences Denver, CO

aAddress correspondence to this author at: OSI Pharmaceuticals, Inc., 2860 Wilderness Place, Boulder, CO 80301. Fax 303-665-3455; e-mail dotc{at}replidyne.com.

To the Editor:

We are writing to reiterate to the medical community that {gamma}-glutamyltransferase (GGT) activity is high in human breast milk for at least 4 weeks postpartum (1)(2) and to suggest that GGT from milk may increase circulating GGT activity in breastfed newborns. An infant was diagnosed with biliary atresia and was surgically managed by a Roux-en-Y hepatoportojejunostomy. The subsequent persistence of high serum GGT activity in the circulation, despite a gradual decrease in the serum bilirubin concentration, prompted concern of an incomplete response to treatment. Because the infant was being breast fed, an alternative explanation for the persistence of the high circulating GGT activity was proposed.

To affirm that breast milk is high in GGT activity and to determine the duration of the increased activity, we evaluated 17 women (16 Caucasian and 1 Hispanic; age range, 25–38 years) during their lactation periods (from 1 day to 17 months postpartum). Procedures were approved by the Institutional Review Board, and informed consent was given by all patients. Breast milk was collected by artificial pump and stored frozen (approximately –20 °C) before analysis. GGT was measured on the VitrosTM 250 Chemistry System (Ortho-Clinical Diagnostics) by a modification of the method of Szasz (3). GGT was detectable in all milk samples. The GGT activity in breast milk was high during the first 4 weeks postpartum with values ranging from 1231 to 16 060 U/L with a decreasing trend at week 4 (Table 1 ). The GGT activity of the breast milk of the patient’s mother was 1138 U/L at 3 months, the first obtained measurement. The GGT activity in breast milk continued to decrease in all milk samples with an ~10-fold decrease in activity from 1 week postpartum to 6 months postpartum (Table 1 ). The mean values for 2 samples collected 1 and 3 days after delivery in this study was 12 613 U/L, between the mean (SD) value of 22 990 (7263) U/L for colostrum and 4090 (2069) U/L for early breast milk collected on postpartum day 4 in a previous study (2).


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  		Table 1. Median breast milk GGT activity over 6 months.

High GGT activity in breast milk is not unique to humans. In animals, the circulating GGT concentration is increased in canine pups after the ingestion of colostrum, and the concentration correlates with the passive transfer of immunoglobulin into the circulation of newborn lambs (4)(5). The high GGT activity in human breast milk may reflect activity in the terminal and lactiferous ducts of the breast, which may facilitate the transport of essential proteins into milk (6)(7). Whether GGT facilitates protein absorption by the developing mucosa of the small intestine is not known.

In conclusion, we suggest that the persistence of a high GGT activity in the circulation of an infant with surgically treated biliary atresia may reflect, at least in part, ingestion and absorption of GGT from breast milk.


References

  1. Landon M. {gamma}-Glutamyltransferase in breast milk. Ann Clin Biochem 1975;12:48-50.[Medline] [Order article via Infotrieve]
  2. Patel KP, Rangnekar NR. {gamma}-Glutamyltransferase activity in human milk. Clin Chem 1982;28:1724-1725.[Free Full Text]
  3. Szasz G. A kinetic photometric method for serum {gamma}-glutamyl transpeptidase. Clin Chem 1969;15:124-136.[Abstract]
  4. Britti D, Massimini G, Peli A, Luciani A, Boari A. Evaluation of serum enzyme activities as predictors of passive transfer status in lambs. J Am Vet Med Assoc 2005;226:951-955.[CrossRef][ISI][Medline] [Order article via Infotrieve]
  5. Center SA, Randolph JF, ManWarren T, Slater M. Effect of colostrum ingestion on gamma-glutamyltransferase and alkaline phosphatase activities in neonatal pups. Am J Vet Res 1991;52:499-504.[ISI][Medline] [Order article via Infotrieve]
  6. Binkley F, Wiesemann ML, Groth DP. {gamma}-Glutamyl transferase: a secretory enzyme. FEBS Lett 1975;51:168-170.[CrossRef][ISI][Medline] [Order article via Infotrieve]
  7. Dupont C. Protein requirements during the first year of life. Am J Clin Nutr 2003;77(Suppl):1544S-1549S.[Abstract/Free Full Text]



The following articles in journals at HighWire Press have cited this article:


Home page
 Clin. Chem.Home page
R. Iorio, A. Giannattasio, E. Lamberti, C. Della Corte, E. Nicastro, and M. I. Spagnuolo
Hyper-{gamma}-Glutamyltransferase Is Commonly Present in Non-Breast-Fed Infants with Biliary Atresia Successfully Treated with Portoenterostomy.
Clin. Chem., July 1, 2006; 52(7): 1430 - 1430.
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