The sites of catabolism of murine monomeric IgA

Academic Article

Abstract

  • The tissue sites of monomeric IgA (mIgA) catabolism were determined in a BALB/c mouse model. Mouse mIgA myeloma proteins were labeled either by direct iodination or by coupling the residualizing label, dilactitol I-tyramine ( I-DLT) to the proteins; catabolites from protein labeled with I-DLT accumulate at the site of protein degradation, allowing identification of the tissue and cellular sites involved in catabolism of the protein. The circulating half-lives of I- and I-DLT-mIgA were the same. The distribution of radioactivity in tissues was measured at 1, 3, 24, and 96 h after iv. injection of I-DLT-labeled mIgA, dimeric IgA (dIgA), IgG, or mouse serum albumin. The greatest uptake of I-DLT-mIgA was attributable to the liver. This organ accounted for more internal catabolism of mIgA than all other tissues combined. In contrast, I-DLT-IgG was catabolized equally in skin, muscle, and liver. These data indicate that, in mice, the liver is the major site of mIgA catabolism. To determine the cell types involved, collagenase digestion was used to isolate parenchymal and non-parenchymal cells from perfused liver of animals injected with -DLT-mIgA. Most of the radioactivity was associated with the hepatocytes fraction, even though both cell types showed uptake of I-DLT-mIgA. Inhibition studies, with asialofetuin and mouse IgA demonstrated that the uptake of mIgA by liver cells was mediated primarily by the asialoglycoprotein receptor. -125 125 125 125 125 125 125 125 125 125
  • Published In

    Author List

  • Moldoveanu Z; Epps JM; Thorpe SR; Mestecky J
  • Start Page

  • 208
  • End Page

  • 213
  • Volume

  • 141
  • Issue

  • 1