Adrenomedullin and its binding protein attenuate the proinflammatory response after hemorrhage

Cui, Xiaoxuan; Wu, Rongqian; Zhou, Mian; Dong, Weifeng; Ulloa, Luis; Yang, Fei; Wang, Haichao; Tracey, Kevin J.; Simms, Henry S.; Wang, Ping

doi:10.1097/01.ccm.0000153416.41398.a9

Cited by 34 publications

(38 citation statements)

References 52 publications

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“…An increasing number of agents (ethyl pyruvate, stearoyl lysophosphatidylcholine, nicotine) dose-dependently inhibits HMGB1 release, and confers significant protection against lethal sepsis [2,8,[35][36][37][38]. Neutralizing antibodies against IFN-γ, a cytokine capable of stimulating HMGB1 release [10], significantly reduced circulating HMGB1 levels in septic rats, and consequently rescued rats from lethal sepsis [39].…”

Section: Suppression Of Hmgb1 Release -The Caging Of the Beastmentioning

confidence: 99%

Role of HMGB1 in cardiovascular diseases

Sama

Wang

2006

Current Opinion in Pharmacology

109

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A nuclear protein, high mobility group box 1 (HMGB1), is released passively by necrotic cells, and actively by macrophages/monocytes in response to exogenous and endogenous inflammatory stimuli. After binding to the receptor for advanced glycation end products (RAGE) or toll-like receptor 4 (TLR4), HMGB1 activates vascular endothelial cells and macrophages/monocytes to express proinflammatory cytokines, chemokines and adhesion molecules. Pharmacological suppression of its activities or release is protective against lethal endotoxemia and sepsis, establishing HMGB1 as a critical mediator of lethal systemic inflammation. In light of the pathogenic role of inflammation in cardiovascular diseases, we propose that HMGB1, a proinflammatory cytokine derived from both injured endothelium and activated macrophages/monocytes, could contribute to the progression of atherosclerosis and other cardiovascular diseases.

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Section: Suppression Of Hmgb1 Release -The Caging Of the Beastmentioning

confidence: 99%

Role of HMGB1 in cardiovascular diseases

Sama

Wang

2006

Current Opinion in Pharmacology

109

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“…The band densities were determined using a BioRad image system. Our previous study indicates that the anti-human AMBP-1 antibodies recognize rat AMBP-1 (27). The band densities were determined with the use of a Bio-Rad image system.…”

Section: Western Blot Analysis Of Ambp-1mentioning

confidence: 99%

Peripheral Administration of Human Adrenomedullin and Its Binding Protein Attenuates Stroke-Induced Apoptosis and Brain Injury in Rats

Chaung

et al. 2011

Mol Med

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Stroke is a leading cause of death and the primary medical cause of acquired adult disability worldwide. The progressive brain injury after acute stroke is partly mediated by ischemia-elicited inflammatory responses. The vasoactive hormone adrenomedullin (AM), upregulated under various inflammatory conditions, counterbalances inflammatory responses. However, regulation of AM activity in ischemic stroke remains largely unknown. Recent studies have demonstrated the presence of a specific AM binding protein (that is, AMBP-1) in mammalian blood. AMBP-1 potentiates AM biological activities. Using a rat model of focal cerebral ischemia induced by permanent middle cerebral artery occlusion (MCAO), we found that plasma levels of AM increased significantly, whereas plasma levels of AMBP-1 decreased significantly after stroke. When given peripherally early after MCAO, exogenous human AM in combination with human AMBP-1 reduced brain infarct volume 24 and 72 h after MCAO, an effect not observed after the treatment by human AM or human AMBP-1 alone. Furthermore, treatment of human AM/AMBP-1 reduced neuron apoptosis and morphological damage, inhibited neutrophil infiltration in the brain and decreased serum levels of S100B and lactate. Thus, human AM/AMBP-1 has the ability to reduce stroke-induced brain injury in rats. AM/AMBP-1 can be developed as a novel therapeutic agent for patients with ischemic stroke.

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“…Interestingly, the activity of AM-BP as complement factor-H (responsible cofactor for the factor I-dependant cleaving of complement C3B) is increased when AM is bound [17] suggesting that aspects of the innate complement cascade within the mammary gland [49] are also modulated by AM. Furthermore, increased beneficial clinical outcome (decreased morbidity and mortality) recently has been attributed to the use of an AM/AM-BP complex as an intervention strategy to limit the complicating effects of sepsis and hypovolumic shock on progression into multiple organ failure [19,[42][43][44].…”

Section: Discussionmentioning

confidence: 99%

“…Further research into this binding protein revealed it to be a member of the complement cascade, namely, complement factor-H (C-F H , [17]). The interaction of AM with AM-BP/C-F H results in the modulation of the bioactivity of each component of the complex [17][18][19].…”

Section: Introductionmentioning

confidence: 99%

Adrenomedullin (AM) and adrenomedullin binding protein (AM-BP) in the bovine mammary gland and milk: Effects of stage of lactation and experimental intramammary E. coli infection

Elsasser

Capuco

Caperna

et al. 2007

Domestic Animal Endocrinology

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(AM) and adrenomedullin binding protein (AM-BP) in the bovine mammary gland and milk: Effects of stage of lactation and experimental intramammary E. coli infection" (2007 AbstractAdrenomedullin (AM) has been characterized as an endogenous tissue survival factor and modulator of many inflammatory processes. Because of the increased susceptibility of the mammary gland to infection during the time surrounding parturition in the cow, we investigated how milk and tissue content of AM and its binding protein (AM-BP) might be affected by the stage of lactation and the udder health status. Milk and mammary biopsy samples were obtained from Holstein cows 21 days prior to and at various times after calving to represent the dry period and early and midstages of lactation. Additional cows received an intramammary challenge with Escherichia coli for immunohistochemical characterization of AM and AM-BP. Milk AM concentrations were relatively constant across the stages of lactation while AM-BP increased two-fold (P < 0.04) between early and ଝ This article is a U.S. Government work and, as such, is in the public domain in the U.S.A. Mention of a brand name or product does not constitute an endorsement of that product by the U.S. Government where other suitably related products are adequately functional in a similar application. This article is a U.S. government work, and is not subject to copyright in the United States. T.H. Elsasser et al. / Domestic Animal Endocrinology 32 (2007) 138-154139 mid-lactation. Milk AM (P < 0.04) and AM-BP (P < 0.03) increased as somatic cell counts (SCCs) increased within a given stage of lactation. Tissue content of both (AM and AM-BP) were significantly affected by stage of lactation, lowest in the dry period and progressively increasing to peak at mid-lactation as well as increasing in association with higher levels of SCCs. Following E. coli challenge, AM increased in epithelial cells surrounding mammary alveoli presenting high levels of SCCs. The data suggest that AM and AM-BP are cooperatively regulated in the mammary gland during lactation; changes in localized tissue AM and AM-BP content reflect a dynamic regulation of these tissue factors in the bovine mammary gland consistent with their protective effects within inflamed tissue. Published by Elsevier Inc.

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Adrenomedullin and its binding protein attenuate the proinflammatory response after hemorrhage

Cited by 34 publications

References 52 publications

Role of HMGB1 in cardiovascular diseases

Role of HMGB1 in cardiovascular diseases

Peripheral Administration of Human Adrenomedullin and Its Binding Protein Attenuates Stroke-Induced Apoptosis and Brain Injury in Rats

Adrenomedullin (AM) and adrenomedullin binding protein (AM-BP) in the bovine mammary gland and milk: Effects of stage of lactation and experimental intramammary E. coli infection

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