Somatolactogenic hormones and interferon-gamma as regulators of neutrophil activation
Fu, Yung-Kang
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Permalink
https://hdl.handle.net/2142/22681
Description
Title
Somatolactogenic hormones and interferon-gamma as regulators of neutrophil activation
Author(s)
Fu, Yung-Kang
Issue Date
1991
Doctoral Committee Chair(s)
Kelley, Keith W.
Department of Study
Animal Sciences
Discipline
Animal Sciences
Degree Granting Institution
University of Illinois at Urbana-Champaign
Degree Name
Ph.D.
Degree Level
Dissertation
Keyword(s)
Health Sciences, Immunology
Language
eng
Abstract
Experiments described in this thesis investigated the role of two somatolactogenic hormones, growth hormone (GH) and prolactin (PRL), as well as the classic phagocyte activator, interferon-gamma (IFN-$\gamma$), in activating polymorphonulear neutrophils (PMN) from pigs, cows, rats and humans to kill Escherichia coli and secrete superoxide anion (O$\sb2\sp-$) after stimulation with phorbol myristate acetate (PMA). GH, as well as its growth promoting peptide, insulin-like growth factor-I (IGF-I), were both comparable to IFN-$\gamma$ in augmenting the secretion of O$\sb2\sp-$ by PMN. These results indicated that the IGF-I receptor was not essential for GH-mediated priming. However, PRL was able to prime human PMN as well as human GH, so the hypothesis was explored that GH primes human PMN by binding to PRL receptors. All of these data suggested that the PRL receptor rather than the GH receptor was responsible for the GH-mediated priming of human PMN for an enhanced respiratory burst. Since GH secretion declines with advancing age, the effector activity of PMN from young and aged rats in response to both GH and IFN-$\gamma$ was compared. PMN from young rats demonstrated a higher capacity for oxygen-dependent killing of E. coli than those from the aged rats. These results defined an intrinsic defect in PMN from aged rats by showing that their PMN were less sensitive to phagocyte activators and that IFN-$\gamma$ and GH synergized to restore this defective response of PMN and potentiated bactericidal activity.
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