BNP-induced activation of cGMP in human cardiac fibroblasts: interactions with fibronectin and natriuretic peptide receptors.

BNP-induced activation of cGMP in human cardiac fibroblasts: interactions with fibronectin and natriuretic peptide receptors. Research Abstract Details 

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BNP-induced activation of cGMP in human cardiac fibroblasts: interactions with fibronectin and natriuretic peptide receptors. Abstract Text:

Brenda K Huntley,Sharon M Sandberg,Josh A Noser,Alessandro Cataliotti,Margaret M Redfield,Yuzuru Matsuda,John C Burnett,

Cardiac remodeling involves the accumulation of extracellular matrix (ECM) proteins including fibronectin (FN). FN contains RGD motifs that bind integrins at DDX sequences allowing signaling from the ECM to the nucleus. We noted that the natriuretic peptide receptor A (NPR-A) sequence contains both RGD and DDX sequences. The goal of the current investigation was to determine potential interactions between FN and NPR-A on BNP induction of cGMP in cultured human cardiac fibroblasts (CFs). Further, we sought to determine whether a Mayo designed NPR-A specific RGD peptide could modify this interaction. Here we reconfirm the presence of all three natriuretic peptide receptors (NPR) in CFs. CFs plated on FN demonstrated a pronounced increase in cGMP production to BNP compared to non-coated plates. This production was also enhanced by the NPR-A specific RGD peptide, which further augmented FN associated cGMP production. Addition of HS-142-1, a NPR-A/B antagonist, abrogated the responses of BNP to both FN and the NPR-A specific RGD peptide. Finally, we defined a possible role for the NPR-C through non-cGMP mechanisms in mediating the anti-proliferative actions of BNP in CFs where the NPR-C antagonist cANF 4-28 but not HS-142-1 blocked BNP-mediated inhibition of proliferation of CFs. We conclude that NPR-A interacts with components of the ECM such as FN to enhance BNP activation of cGMP and that a small NPR-A specific RGD peptide augments this action of BNP with possible therapeutic implications. Lastly, the NPR-C may also have a role in mediating anti-proliferative actions of BNP in CFs.

BNP-induced activation of cGMP in human cardiac fibroblasts: interactions with fibronectin and natriuretic peptide receptors. Publishing Authors By Initials

BK Huntley,SM Sandberg,JA Noser,A Cataliotti,MM Redfield,Y Matsuda,JC Burnett,

For similar enzymes and coenzymes: enzymes: lyases: phosphorus-oxygen lyases: guanylate cyclase: receptors, guanylate cyclase-coupled: receptors, atrial natriuretic factor research abstracts see: enzymes and coenzymes: enzymes: lyases: phosphorus-oxygen lyases: guanylate cyclase: receptors, guanylate cyclase-coupled: receptors, atrial natriuretic factor research

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BNP-induced activation of cGMP in human cardiac fibroblasts: interactions with fibronectin and natriuretic peptide receptors. Journal Published:

PUBLICATION TYPE: Research Support, N.I.H., Extr

Journal: Journal of cellular physiology

VOLUME: 209

Page Numbers: 943-9

Journal Abbreviation: J. Cell. Physiol.

ISSN: 0021-9541

DAY: 3

MONTH: Dec

YEAR: 2006

BNP-induced activation of cGMP in human cardiac fibroblasts: interactions with fibronectin and natriuretic peptide receptors. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 50222

BNP-induced activation of cGMP in human cardiac fibroblasts: interactions with fibronectin and natriuretic peptide receptors. Keywords Mesh Terms:

KEYWORDS: Receptors, Atrial Natriuretic Factor

MESH TERMS: metabolism

Chemical & Substance for Abstract: BNP-induced activation of cGMP in human cardiac fibroblasts: interactions with fibronectin and natriuretic peptide receptors. Information

Substance Name: atrial natriuretic factor receptor C

Registry Number: EC 4.6.1.2

Grant and Affiliation Information for BNP-induced activation of cGMP in human cardiac fibroblasts: interactions with fibronectin and natriuretic peptide receptors.

AFFILIATION: Cardiorenal Research Laboratory, Division of Cardiovascular Diseases, Mayo Clinic and Foundation, Rochester, MN 55904, USA. huntley.brenda@mayo.edu

Country: United States

AGENCY: United States NHLBI

GRANT: HL 76611

ACRONYM: HL

MEDLINETA: J Cell Physiol

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