Attenuation of Lysophosphatidylcholine-Induced Suppression of ANP Release From Hypertrophied Atria

Han, Jeong Hee; Cao, Chunhua; Kim, Soo Mi; Piao, Feng Lian; Kim, Suhn Hee

doi:10.1161/01.hyp.0000107779.92645.89

Cited by 8 publications

(4 citation statements)

References 41 publications

(38 reference statements)

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“…Although animal studies suggest that increasing plasma LPC with exogenous administration is protective in sepsis, this would need to be carefully examined further in animal models to determine critical levels that are therapeutically advantageous. Alternately, pathways downstream of LPC could be identified to replicate the potentially beneficial role of LPC in sepsis, as LPC also has many deleterious consequences, including proinflammatory, atherogenic, and arrhythmogenic effects (55)(56)(57).…”

Section: J O U R N a L P R E -P R O O Fmentioning

confidence: 99%

The lipid biology of sepsis

Amunugama

Pike

Ford

2021

Journal of Lipid Research

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Section: J O U R N a L P R E -P R O O Fmentioning

confidence: 99%

The lipid biology of sepsis

Amunugama

Pike

Ford

2021

Journal of Lipid Research

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“…However, the suppression of ANP release by lysophosphatidyl choline was attenuated in hypertrophied atria. 42 Conditions associated with increased circulating BNP and NT-proBNP are listed in Table 3.…”

Section: Synthesis and Release Of B-type Natriuretic Peptidementioning

confidence: 99%

Natriuretic Peptides: Physiologic and Analytic Considerations

Omland

Hagve

2009

Heart Failure Clinics

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“…18 This endogenous phospholipid is released from cell membranes during ischemia. In isolated perfused atria LPC attenuated release of ANP in response to atrial stretch.…”

Section: Secretory Stimuli For Natriuretic Peptidesmentioning

confidence: 99%

Natriuretic Peptides

Richards

2007

Hypertension

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In the 25 years since de Bold et al demonstrated the existence of an atrial natriuretic factor, investigation of the cardiac natriuretic peptides has produced a maturing knowledge base 1,2 identifying the cardiac peptides and addressing stimuli for secretion of atrial (ANP) and B-type (BNP) natriuretic peptides, the processing and release of the mature bioactive carboxy terminal peptides, together with their propeptides and amino terminal fragments, the nature of natriuretic peptide receptors, and the bioactivities of natriuretic peptides (including natriuresis, vasodilatation, suppression of renin-angiotensin-aldosterone and sympathetic nervous activity, and trophic effects inhibiting vascular and cardiac hypertrophy and fibrosis). Less is known of the more recently discovered C-type natriuretic peptide (CNP and its cosecreted amino-terminal peptide, NTproCNP). 3,4 Increasingly, measurements of the B-type peptides have found diagnostic and prognostic application in cardiovascular disease. [5][6][7] The genes for ANP and BNP are in tandem on human chromosome 1. 8 Upstream regulatory regions identified for the BNP gene include an AP1 binding site, serum response elements, M-CAT and GATA sites. 9,10 Translation results in pre-pro BNP from which a 26 amino acid signal peptide is cleaved to produce the 108 amino acid precursor proBNP. This in turn is processed between amino acid residues 76 and 77 resulting in a 32 amino acid biologically active peptide (BNP) from its carboxy terminal plus the remaining amino terminal peptide sequence (NTproBNP 1 to 76). ANP is synthesized as a 126 amino acid precursor and is stored in granules within atrial tissue. 11 During or shortly after secretion, the precursor is processed to an active 28 amino acid carboxy terminal peptide (ANP) and amino terminal ANP (proANP 1 to 98). The amino terminal propeptides NTproANP, NTproBNP, and NTproCNP have no known biological actions. The mature bioactive human forms of ANP, BNP, and CNP all contain a 17 member amino acid ring bound by cysteine-to-cysteine disulphide bonds with 11 of the 16 residues being conserved across ANP, BNP, and CNP. The 3 peptides have varying length amino terminal and carboxy terminal amino acid residue "tails" with CNP essentially lacking any carboxy terminal extension beyond the ring structure. The actions of ANP and BNP are mediated predominantly via the GC-A receptor and those of CNP via the GC-B receptor. All 3 peptides are subject to varying degrees of degradation by neutral endopeptidase (EC 3.4.24.11) and via uptake by the C ("clearance") receptor.ANP and BNP and their receptors are widely distributed in brain, spinal cord, pituitary, kidney, adrenal gland, and vasculature in addition to the heart. Concentrations of immunoreactive ANP and BNP within the heart are up to 3 orders of magnitude higher than elsewhere, and within cardiac atria the concentrations of both peptides are 1 to 2 orders of magnitude higher than in ventricle. 12 CNP is also widely distributed mainly in the vasculature with far lower cardiac ...

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Attenuation of Lysophosphatidylcholine-Induced Suppression of ANP Release From Hypertrophied Atria

Cited by 8 publications

References 41 publications

The lipid biology of sepsis

The lipid biology of sepsis

Natriuretic Peptides: Physiologic and Analytic Considerations

Natriuretic Peptides

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