PMID: 9531972Apr 9, 1998Paper

The acute-phase protein alpha 1-antitrypsin inhibits transferrin-receptor binding and proliferation of human skin fibroblasts

Biochimica Et Biophysica Acta
I GraziadeiW Vogel

Abstract

Transferrin (Tf) is required for proliferation of most cells, because cellular iron uptake is mainly mediated by binding of Tf to its specific cell surface receptors (TfR). The acute-phase protein alpha 1-antitrypsin (alpha 1-AT) completely inhibits binding of diferric Tf to TfRs on human skin fibroblasts in a dose-dependent fashion. The inhibition is competitive as proved in equilibrium saturation binding and kinetic studies. In saturation binding experiments alpha 1-AT apparently increased the dissociation constant (KD), but did not change the maximal density of binding sites (Bmax). As shown in kinetic studies, this reduction of the affinity of Tf to its receptor caused by alpha 1-AT was due to a decrease of the association rate constant (k + 1), whereas the dissociation rate constant (k - 1) remained unchanged. Furthermore, alpha 1-AT almost completely prevented internalization of the Tf-TfR complex. These interactions demonstrated biological implication, as alpha 1-AT reduced the proliferation of human fibroblasts up to maximal 30% of control. The inhibitory potency of alpha 1-AT was already seen in physiologic concentrations; the maximal effect, however, was achieved at concentrations above the normal range, which are att...Continue Reading

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Citations

Jun 16, 2009·American Journal of Physiology. Lung Cellular and Molecular Physiology·Zhenjun LiRavi Mahadeva
Feb 5, 2013·International Journal of Chronic Obstructive Pulmonary Disease·Andrew J GhioDonald E Schmechel
Sep 29, 2006·Hepatology : Official Journal of the American Association for the Study of Liver Diseases·Luca ValentiSilvia Fargion
Feb 24, 2001·The American Journal of the Medical Sciences·B R Gochuico
Nov 10, 2006·Journal of Animal Science·M HamelinE Laville
Apr 23, 2003·The American Journal of Pathology·Kim R BridleGrant A Ramm

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