title: Anti-complement activities of human breast-milk.
abstract: OBJECTIVE
  It has long been observed that the human milk possesses significant anti-inflammatory properties, while simultaneously protecting the infant against many intestinal and respiratory pathogens. There is, however, a paucity of information on the degree and extent of this anti-inflammatory activity. In the present study, the inhibitory effects of different fractions of human milk on serum complement activity were analysed.
  
  
  METHODS
  Colostrum and milk samples from healthy voluntary lactating donors at different postpartum ages were obtained and pooled normal human serum was used as source of complement in a modified CH50 assay. Inherent complement activity in human milk was also investigated by measuring the deposition of an activated C3 fragment on a serum-sensitive bacteria, and by haemolytic assays.
  
  
  RESULTS
  Most whole- and defatted-milk samples consistently showed a dose-dependent inhibition of the serum complement activity. This inhibition was greater in mature milk compared to transitional milk samples. It was enhanced by inactivation of milk complement, and diminished by centrifugation of milk samples, which partly removed fat and larger protein components including casein micelles. Inherent complement activity in human milk was also demonstrated by haemolysis of sensitised sheep erythrocytes and deposition of C3 fragments on solid-phase bacteria. These activities were highest in the colostrum and gradually decreased as lactation proceeded.
  
  
  CONCLUSIONS
  Several natural components abundant in the fluid phase of the human breast-milk have been shown to be inhibitors of complement activation in vitro. Their physiological significance probably reside in their ability to prevent inflammatory-induced tissue damage of the delicate immature gastrointestinal tract of the new-born as well as the mammary gland itself, which may arise from ongoing complement activation.
authors.affiliation: Department of Immunology, Georg-August University, Göttingen, Germany. mogundel@yahoo.com
authors.forename: M O
authors.initials: MO
authors.lastname: Ogundele
mesh_terms: D000328:Adult; D000818:Animals; D002021:Buffers; D002498:Centrifugation; D003167:Complement Activation / Q000502:physiology; D003176:Complement C3 / Q000378:metabolism; D003169:Complement Inactivator Proteins / Q000494:pharmacology / Q000502:physiology*; D004797:Enzyme-Linked Immunosorbent Assay; D004926:Escherichia coli / Q000276:immunology; D005260:Female; D006461:Hemolysis; D006358:Hot Temperature; D006801:Humans; D066298:In Vitro Techniques; D007774:Lactation / Q000502:physiology; D008894:Milk Proteins / Q000737:chemistry / Q000494:pharmacology; D008895:Milk, Human / Q000737:chemistry / Q000276:immunology / Q000502:physiology*; D009895:Opsonin Proteins / Q000276:immunology; D012756:Sheep
chemical_list: D002021:Buffers; D003176:Complement C3; D003169:Complement Inactivator Proteins; D008894:Milk Proteins; D009895:Opsonin Proteins