February 15, 2002Biochemical JournalOpen Access

Allotopic antagonism of the non-peptide atrial natriuretic peptide (ANP) antagonist HS-142-1 on natriuretic peptide receptor NPR-A

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Population

Wild-type natriuretic peptide receptor NPR-A, a disulphide-bridged constitutively active mutant, and…

Design

Preclinical

Authors

HPHugo PoirierAegera Therapeutics (Canada)JLJean LabrecqueMedical Council of Canada JDJulie DESCHEÊNES

Discussion

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Implication

Allosteric NPR-A inhibition is mechanistically feasible in models; leaves open therapeutic translation to cardiovascular disease.

Structured PICO

Population

Wild-type natriuretic peptide receptor NPR-A (WT), a disulphide-bridged constitutively active mutant (C423S), and truncated mutants lacking either their cytoplasmic domain (DeltaKC) or both the cytoplasmic and the transmembrane domains (ECD)

Intervention

HS-142-1 (microbial polysaccharide)

Outcome

Inhibition of atrial natriuretic peptide (ANP) binding and dissociation of NPR-A-bound (125)I-ANPsurrogate

HS-142-1 acts as an allosteric antagonist of the natriuretic peptide receptor NPR-A, requiring the transmembrane domain for its inhibitory effect on ANP binding.

Cite This Study

Poirier et al. (2002) studied this question.

synapsesocial.com/papers/6a894296abe412682d92d41d https://doi.org/10.1042/0264-6021:3620231

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Allotopic antagonism of the non-peptide atrial natriuretic peptide (ANP) antagonist HS-142-1 on natriuretic peptide receptor NPR-A

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Allotopic antagonism of the non-peptide atrial natriuretic peptide (ANP) antagonist HS-142-1 on natriuretic peptide receptor NPR-A

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Also Consider

Also Consider