Alpha-lactalbumin in human milk alters the proteolytic degradation of soluble CD14 by forming a complex.

Abstract:

:Mother's milk represents a foundational step in the proper development of newborn immunity. This is achieved, in part, through the action of numerous regulatory proteins such as soluble cluster of differentiation 14 (sCD14) found in significant quantities in human milk (~25-50 μg/mL). In adults, CD14 stimulates cytokine production in response to lipopolysaccharide (LPS), the major lipid component found in the outer membrane of Gram-negative bacteria. However, the fate and function of sCD14 in the neonatal gastrointestinal (GI) tract are unknown and may function differently from adults. Therefore, we administered human sCD14 to experimental animals and observed that it persisted in the upper GI tract after feeding. In our search for potential proteolytic protectants, immunoprecipitation of sCD14 from human milk revealed a 15-kD novel protein that copurified with sCD14. Mass spectrometry analysis of the protein identified alpha-lactalbumin. CD14 was also identified by immunoblot after immunoprecipitation of alpha-lactalbumin from milk. In vitro digestion assays revealed that purified alpha-lactalbumin decreases the proteolytic degradation of human milk derived sCD14 in vitro, suggesting a mechanism by which this key LPS receptor may remain functional in the neonate gut.

journal_name

Pediatr Res

journal_title

Pediatric research

authors

Spencer WJ,Binette A,Ward TL,Davis LD,Blais DR,Harrold J,Mack DR,Altosaar I

doi

10.1203/PDR.0b013e3181f70f21

subject

Has Abstract

pub_date

2010-12-01 00:00:00

pages

490-3

issue

6

eissn

0031-3998

issn

1530-0447

journal_volume

68

pub_type

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