PMID: 9169617May 1, 1997Paper

Isolated rat hepatocytes differentially bind and internalize bovine lactoferrin N- and C-lobes

The Biochemical Journal
M P Sitaram, D D McAbee

Abstract

Isolated rat hepatocytes bind and internalize bovine lactoferrin (Lf) and its bound iron in a Ca2+-dependent manner. In this study, we determined if one or both halves of Lf (N- and C-lobes) were responsible for the interaction of Lf with hepatocytes. We isolated three tryptic fragments of bovine Lf. Cleavage at Arg284-Ser285 generated two fragments: N-terminal pp36 that contained 80% of Lf N-lobe and C-terminal pp51. A second cleavage at Arg338-Ala339 generated a smaller fragment (pp44) that contained all of the C-lobe with no N-lobe elements. Hepatocytes bound Lf and pp51 in a Ca2+-dependent manner with the same affinity (Kd approx. 75 nM) and to nearly identical extents (approx. 10(6) sites per cell). Lf and pp51 competed with each other for binding to cells over a similar titration range. Hepatocytes internalized Lf at a faster rate than pp51 (kin=0.28 and 0.19 min-1 respectively), but cells degraded pp51 at approx. twice the rate of native Lf. pp44 competed with 125I-labelled Lf for binding to Ca2+-dependent binding sites on hepatocytes as well as native Lf or pp51. In contrast, hepatocytes bound pp36 (Kd=90 nM, <=5x10(6) sites per cell) but did not internalize or degrade it appreciably. Moreover, pp36 binding to cells was...Continue Reading

Citations

Dec 10, 2002·Biochemical and Biophysical Research Communications·Yoshiharu TakayamaToshiaki Takezawa
Jul 6, 2014·BMC Complementary and Alternative Medicine·Elrashdy M RedwanMustafa H Linjawi
Nov 9, 2006·Bioscience, Biotechnology, and Biochemistry·Woan-Sub KimTomohiro Tamura
Feb 12, 2009·Biotechnology Letters·Morshedur RahmanKei-ichi Shimazaki

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