The transport and metabolism of bovine IgM

V. L. Frenyo, J. E. Butler, R. A. Wilson, J. Kavanagh

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5 Citations (Scopus)

Abstract

IgM is present in cows milk, is able to bind secretory component (SC), has a purported role as a secretory immunoglobulin in other species and has been identified with various antibody functions in cows milk. To determine the origin of cows milk IgM, we administered extrinsic 131I-IgM to lactating cows with cannulated bile and parotid ducts and studied the kinetics of its disappearance from serum and its appearance in milk, bile and parotid saliva for 60 hr post-injection. Pentameric IgM appeared to require a long equilibration time and disappeared from serum with a T 1 2 of 40 hr. The transport of IgM into bile also appeared biphasic. Results showed that no 131I-IgM was transported intact into parotid saliva and that most radioactivity in milk and bile after 6 hr was in the form of low mol. wt, TCA-precipitable fragments rather than of the size of a pentamer. During the first 24 hr only 0.83% of the administered dose reached the milk in pentameric form, nevertheless, isotope dilution calculations indicated that nearly all milk IgM was derived from serum. During a 12hr collection period, corresponding to one milking, > 200 mg of serum IgM is secreted in milk. During the first 24 hr, only 0.70% of the administered IgM reached the bile as a pentamer. It was calculated that 50% of the pentameric IgM in bile, 3 hr after administration, was serum-derived. Twenty-five per cent of the IgM appearing in bile and ca 10% of the IgM appearing in milk, becomes associated with secretory component. A hypothesis to explain the degradation associated with this inefficient transport mechanism is presented.

Original languageEnglish
Pages (from-to)207-219
Number of pages13
JournalMolecular Immunology
Volume24
Issue number3
DOIs
Publication statusPublished - Mar 1987

ASJC Scopus subject areas

  • Immunology
  • Molecular Biology

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