Depletion of high-affinity corticosteroid-binding globulin corresponds to illness severity in sepsis and septic shock; clinical implications.

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Abstract

Corticosteroid-binding globulin (CBG) is cleaved by neutrophil elastase converting the high-affinity (haCBG) conformation of CBG to a low-affinity (laCBG) conformation with a ninefold reduced cortisol-binding affinity. These in vitro data suggest that cortisol release by CBG cleavage results in the targeted delivery of cortisol to areas of inflammation. Our objective was to determine whether CBG cleavage alters circulating levels of haCBG and laCBG in vivo in proportion to sepsis severity.

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Journal

Journal ID (iso-abbrev): Clin. Endocrinol. (Oxf)

Title: Clinical endocrinology

ISSN (Electronic): 1365-2265

ISSN (Print): 0300-0664

Publication date (Electronic): Jun 2015

Volume: 82

Issue: 6

Affiliations

[1 ] Endocrine and Metabolic Unit, Royal Adelaide Hospital, Adelaide, SA, Australia.

[2 ] School of Medicine, University of Adelaide, Adelaide, SA, Australia.

[3 ] Chemical Pathology Directorate, SA Pathology, Adelaide, SA, Australia.

[4 ] Intensive Care Unit, Royal Adelaide Hospital, Adelaide, SA, Australia.

[5 ] Experimental Therapeutics Laboratory, Hanson Institute and Sansom Institute, University of South Australia, Adelaide, SA, Australia.

[6 ] Robinson Research Institute and School of Paediatrics and Reproductive Health, University of Adelaide, Adelaide, SA, Australia.

[7 ] Steroid and Immunobiochemistry Laboratory, Canterbury Health Laboratories, Christchurch, New Zealand.

Article

DOI: 10.1111/cen.12680

PubMed ID: 25409953

SO-VID: 3ef3b6a3-a895-4689-adf6-cc7f8db1543b

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