About: Cell Surface Protein Disulfide Isomerase Regulates Natriuretic Peptide Generation of Cyclic Guanosine Monophosphate

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About: Cell Surface Protein Disulfide Isomerase Regulates Natriuretic Peptide Generation of Cyclic Guanosine Monophosphate Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : wasabi.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Cell Surface Protein Disulfide Isomerase Regulates Natriuretic Peptide Generation of Cyclic Guanosine Monophosphate
Creator	Correia, Cristina Dai, Haiming Pan, Shuchong Burnett, John Chen, Horng Kleppe, Laurel Simari, Robert Witt, Tyra
Source	PMC
abstract	RATIONALE: The family of natriuretic peptides (NPs), including atrial natriuretic peptide (ANP), B-type natriuretic peptide (BNP), and C-type natriuretic peptide (CNP), exert important and diverse actions for cardiovascular and renal homeostasis. The autocrine and paracrine functions of the NPs are primarily mediated through the cellular membrane bound guanylyl cyclase-linked receptors GC-A (NPR-A) and GC-B (NPR-B). As the ligands and receptors each contain disulfide bonds, a regulatory role for the cell surface protein disulfide isomerase (PDI) was investigated. OBJECTIVE: We utilized complementary in vitro and in vivo models to determine the potential role of PDI in regulating the ability of the NPs to generate its second messenger, cyclic guanosine monophosphate. METHODS AND RESULTS: Inhibition of PDI attenuated the ability of ANP, BNP and CNP to generate cGMP in human mesangial cells (HMCs), human umbilical vein endothelial cells (HUVECs), and human aortic smooth muscle cells (HASMCs), each of which were shown to express PDI. In LLC-PK1 cells, where PDI expression was undetectable by immunoblotting, PDI inhibition had a minimal effect on cGMP generation. Addition of PDI to cultured LLC-PK1 cells increased intracellular cGMP generation mediated by ANP. Inhibition of PDI in vivo attenuated NP-mediated generation of cGMP by ANP. Surface Plasmon Resonance demonstrated modest and differential binding of the natriuretic peptides with immobilized PDI in a cell free system. However, PDI was shown to co-localize on the surface of cells with GC-A and GC-B by co-immunoprecpitation and immunohistochemistry. CONCLUSION: These data demonstrate for the first time that cell surface PDI expression and function regulate the capacity of natriuretic peptides to generate cGMP through interaction with their receptors.
has issue date	2014-11-24(xsd:dateTime)
bibo:doi	10.1371/journal.pone.0112986
bibo:pmid	25419565
has license	cc-by
sha1sum (hex)	8b47882ebbc8d2e9d217dcc10b2328eff5bf8b46
schema:url	https://doi.org/10.1371/journal.pone.0112986
resource representing a document's title	Cell Surface Protein Disulfide Isomerase Regulates Natriuretic Peptide Generation of Cyclic Guanosine Monophosphate
has PubMed Central identifier	PMC4242536
has PubMed identifier	25419565
schema:publication	PLoS One
resource representing a document's body	covid:8b47882ebbc8d2e9d217dcc10b2328eff5bf8b46#body_text
is schema:about of	named entity 'surface' named entity 'cellular membrane' named entity 'PDI' named entity 'aortic' named entity 'smooth muscle cells' named entity 'Addition' named entity 'natriuretic' named entity 'renal' named entity 'inhibition' named entity 'system' named entity 'Disulfide' named entity 'ABILITY' named entity 'CELL SURFACE' named entity 'GENERATE' named entity 'GC-B' named entity 'NATRIURETIC PEPTIDES' named entity 'A CELL' named entity 'FAMILY' named entity 'GUANYLYL CYCLASE' named entity 'CONCLUSION' named entity 'CELL SURFACE PROTEIN' named entity 'THE CELL' named entity 'INTRACELLULAR' named entity 'TIME' named entity 'DIFFERENTIAL' named entity 'POTENTIAL' named entity 'B-TYPE NATRIURETIC PEPTIDE' named entity 'PROTEIN DISULFIDE ISOMERASE' named entity 'CYCLIC GUANOSINE MONOPHOSPHATE' named entity 'PARACRINE' named entity 'GENERATION' named entity 'HUMAN UMBILICAL VEIN ENDOTHELIAL CELLS' named entity 'CNP' named entity 'CELL FREE SYSTEM' named entity 'DIVERSE' named entity 'MEDIATED' named entity 'SURFACE PLASMON RESONANCE' named entity 'GC-A' named entity 'LOCALIZE' named entity 'RECEPTORS' named entity 'DEMONSTRATED' named entity 'ATRIAL NATRIURETIC PEPTIDE' named entity 'ACTIONS' named entity 'HOMEOSTASIS' named entity 'IN VITRO' named entity 'LIGANDS' named entity 'METHODS' named entity 'INCLUDING' named entity 'FUNCTION' named entity 'ADDITION' named entity 'CULTURED' named entity 'CYCLIC GUANOSINE MONOPHOSPHATE' named entity 'ITS' named entity 'BOUND' named entity 'CGMP' named entity 'SURFACE' named entity 'BNP' named entity 'MODELS' named entity 'REGULATORY ROLE' named entity 'CONTAIN' named entity 'IMPORTANT' named entity 'ATTENUATED' named entity 'BINDING' named entity 'C-TYPE NATRIURETIC PEPTIDE' named entity 'IMMUNOHISTOCHEMISTRY' named entity 'CAPACITY' named entity 'INCREASED' named entity 'WHERE' named entity 'GENERATION' named entity 'CELL SURFACE PROTEIN' named entity 'REGULATING' named entity 'CELLS' named entity 'OBJECTIVE' named entity 'AUTOCRINE'

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