Abstract
Background: The protease inhibitors α 1-antitrypsin and antichymotrypsin are present in human milk, but little is known about their roles in protein digestion during infancy. It has been hypothesized that α 1-antitrypsin and antichymotrypsin may modulate digestion in the infant gut. Objective: We determined whether the mammary gland expresses α 1-antitrypsin and antichymotrypsin, measured α 1-antitrypsin and antichymotrypsin throughout lactation, assessed the resistance of α 1-antitrypsin to proteolysis, and determined the potential of α 1-antitrypsin to affect the survival of other milk proteins. Design: A pool of complementary DNA from the human mammary gland was analyzed with polymerase chain reaction to detect genes for α 1-antitrypsin and antichymotrypsin. α 1-Antitrypsin and antichymotrypsin concentrations were measured in milk samples obtained longitudinally (days 4-47) from 8 women. An in vitro model of infant digestion was used to assess the digestive stability of α 1-antitrypsin against pepsin and pancreatin. Lactoferrin, with α 1-antitrypsin present, was digested by pancreatin, and the digested proteins were separated. Results: α 1-Antitrypsin and antichymotrypsin concentrations were high in early milk and decreased throughout lactation. Polymerase chain reaction products were detected for both genes. After in vitro digestion, much of the α 1-antitrypsin was still intact, whereas many other milk proteins were digested. Much of the lactoferrin was still intact after digestion, but only when α 1-antitrypsin was added. Conclusions: The results suggest that α 1-antitrypsin and antichymotrypsin are produced by the mammary gland and are present in milk in relatively high amounts in early lactation. α 1-Antitrypsin may survive digestion and may affect the survival of other proteins.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 828-833 |
| Number of pages | 6 |
| Journal | American Journal of Clinical Nutrition |
| Volume | 76 |
| Issue number | 4 |
| State | Published - Oct 2002 |
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Keywords
- α -Antitrypsin
- Antichymotrypsin
- Breast milk
- Breast-feeding
- Human milk
- Infant digestion
- Mammary gland
- Milk proteins
- Protease inhibitors
ASJC Scopus subject areas
- Medicine (miscellaneous)
- Food Science
Cite this
α 1-antitrypsin and antichymotrypsin in human milk : Origin, concentrations, and stability. / Chowanadisai, Winyoo; Lönnerdal, Bo.
In: American Journal of Clinical Nutrition, Vol. 76, No. 4, 10.2002, p. 828-833.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - α 1-antitrypsin and antichymotrypsin in human milk
T2 - Origin, concentrations, and stability
AU - Chowanadisai, Winyoo
AU - Lönnerdal, Bo
PY - 2002/10
Y1 - 2002/10
N2 - Background: The protease inhibitors α 1-antitrypsin and antichymotrypsin are present in human milk, but little is known about their roles in protein digestion during infancy. It has been hypothesized that α 1-antitrypsin and antichymotrypsin may modulate digestion in the infant gut. Objective: We determined whether the mammary gland expresses α 1-antitrypsin and antichymotrypsin, measured α 1-antitrypsin and antichymotrypsin throughout lactation, assessed the resistance of α 1-antitrypsin to proteolysis, and determined the potential of α 1-antitrypsin to affect the survival of other milk proteins. Design: A pool of complementary DNA from the human mammary gland was analyzed with polymerase chain reaction to detect genes for α 1-antitrypsin and antichymotrypsin. α 1-Antitrypsin and antichymotrypsin concentrations were measured in milk samples obtained longitudinally (days 4-47) from 8 women. An in vitro model of infant digestion was used to assess the digestive stability of α 1-antitrypsin against pepsin and pancreatin. Lactoferrin, with α 1-antitrypsin present, was digested by pancreatin, and the digested proteins were separated. Results: α 1-Antitrypsin and antichymotrypsin concentrations were high in early milk and decreased throughout lactation. Polymerase chain reaction products were detected for both genes. After in vitro digestion, much of the α 1-antitrypsin was still intact, whereas many other milk proteins were digested. Much of the lactoferrin was still intact after digestion, but only when α 1-antitrypsin was added. Conclusions: The results suggest that α 1-antitrypsin and antichymotrypsin are produced by the mammary gland and are present in milk in relatively high amounts in early lactation. α 1-Antitrypsin may survive digestion and may affect the survival of other proteins.
AB - Background: The protease inhibitors α 1-antitrypsin and antichymotrypsin are present in human milk, but little is known about their roles in protein digestion during infancy. It has been hypothesized that α 1-antitrypsin and antichymotrypsin may modulate digestion in the infant gut. Objective: We determined whether the mammary gland expresses α 1-antitrypsin and antichymotrypsin, measured α 1-antitrypsin and antichymotrypsin throughout lactation, assessed the resistance of α 1-antitrypsin to proteolysis, and determined the potential of α 1-antitrypsin to affect the survival of other milk proteins. Design: A pool of complementary DNA from the human mammary gland was analyzed with polymerase chain reaction to detect genes for α 1-antitrypsin and antichymotrypsin. α 1-Antitrypsin and antichymotrypsin concentrations were measured in milk samples obtained longitudinally (days 4-47) from 8 women. An in vitro model of infant digestion was used to assess the digestive stability of α 1-antitrypsin against pepsin and pancreatin. Lactoferrin, with α 1-antitrypsin present, was digested by pancreatin, and the digested proteins were separated. Results: α 1-Antitrypsin and antichymotrypsin concentrations were high in early milk and decreased throughout lactation. Polymerase chain reaction products were detected for both genes. After in vitro digestion, much of the α 1-antitrypsin was still intact, whereas many other milk proteins were digested. Much of the lactoferrin was still intact after digestion, but only when α 1-antitrypsin was added. Conclusions: The results suggest that α 1-antitrypsin and antichymotrypsin are produced by the mammary gland and are present in milk in relatively high amounts in early lactation. α 1-Antitrypsin may survive digestion and may affect the survival of other proteins.
KW - α -Antitrypsin
KW - Antichymotrypsin
KW - Breast milk
KW - Breast-feeding
KW - Human milk
KW - Infant digestion
KW - Mammary gland
KW - Milk proteins
KW - Protease inhibitors
UR - http://www.scopus.com/inward/record.url?scp=0036784342&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0036784342&partnerID=8YFLogxK
M3 - Article
C2 - 12324297
AN - SCOPUS:0036784342
VL - 76
SP - 828
EP - 833
JO - American Journal of Clinical Nutrition
JF - American Journal of Clinical Nutrition
SN - 0002-9165
IS - 4
ER -