NDLI: Characterization of a Pachymedusa dacnicolor-Sauvagine analog as a new high-affinity radioligand for corticotropin-releasing factor receptor studies.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Perrin, Marilyn H. Tan, Laura A. Vaughan, Joan M. Lewis, Kathy A. Donaldson, Cynthia J. Miller, Charleen Erchegyi, Judit Rivier, Jean E. Sawchenko, Paul E.
Description	Author Affiliation: Perrin MH ( Clayton Foundation Laboratories for Peptide Biology (M.H.P., J.M.V., K.A.L., C.J.D., C.M., J.E., J.E.R., P.E.S.) and Laboratory of Neuronal Structure and Function (L.A.T., P.E.S.), The Salk Institute for Biological Studies, La Jolla, California.); Tan LA ( Clayton Foundation Laboratories for Peptide Biology (M.H.P., J.M.V., K.A.L., C.J.D., C.M., J.E., J.E.R., P.E.S.) and Laboratory of Neuronal Structure and Function (L.A.T., P.E.S.), The Salk Institute for Biological Studies, La Jolla, California.); Vaughan JM ( Clayton Foundation Laboratories for Peptide Biology (M.H.P., J.M.V., K.A.L., C.J.D., C.M., J.E., J.E.R., P.E.S.) and Laboratory of Neuronal Structure and Function (L.A.T., P.E.S.), The Salk Institute for Biological Studies, La Jolla, California.); Lewis KA ( Clayton Foundation Laboratories for Peptide Biology (M.H.P., J.M.V., K.A.L., C.J.D., C.M., J.E., J.E.R., P.E.S.) and Laboratory of Neuronal Structure and Function (L.A.T., P.E.S.), The Salk Institute for Biological Studies, La Jolla, California.); Donaldson CJ ( Clayton Foundation Laboratories for Peptide Biology (M.H.P., J.M.V., K.A.L., C.J.D., C.M., J.E., J.E.R., P.E.S.) and Laboratory of Neuronal Structure and Function (L.A.T., P.E.S.), The Salk Institute for Biological Studies, La Jolla, California.); Miller C ( Clayton Foundation Laboratories for Peptide Biology (M.H.P., J.M.V., K.A.L., C.J.D., C.M., J.E., J.E.R., P.E.S.) and Laboratory of Neuronal Structure and Function (L.A.T., P.E.S.), The Salk Institute for Biological Studies, La Jolla, California.); Erchegyi J ( Clayton Foundation Laboratories for Peptide Biology (M.H.P., J.M.V., K.A.L., C.J.D., C.M., J.E., J.E.R., P.E.S.) and Laboratory of Neuronal Structure and Function (L.A.T., P.E.S.), The Salk Institute for Biological Studies, La Jolla, California.); Rivier JE ( Clayton Foundation Laboratories for Peptide Biology (M.H.P., J.M.V., K.A.L., C.J.D., C.M., J.E., J.E.R., P.E.S.) and Laboratory of Neuronal Structure and Function (L.A.T., P.E.S.), The Salk Institute for Biological Studies, La Jolla, California.); Sawchenko PE ( Clayton Foundation Laboratories for Peptide Biology (M.H.P., J.M.V., K.A.L., C.J.D., C.M., J.E., J.E.R., P.E.S.) and Laboratory of Neuronal Structure and Function (L.A.T., P.E.S.), The Salk Institute for Biological Studies, La Jolla, California sawchenko@salk.edu.)
Abstract	The corticotropin-releasing factor (CRF) peptide family comprises the mammalian peptides CRF and the urocortins as well as frog skin sauvagine and fish urophyseal urotensin. Advances in understanding the roles of the CRF ligand family and associated receptors have often relied on radioreceptor assays using labeled CRF ligands. These assays depend on stable, high-affinity CRF analogs that can be labeled, purified, and chemically characterized. Analogs of several of the native peptides have been used in this context, most prominently including sauvagine from the frog Phyllomedusa sauvageii (PS-Svg). Because each of these affords both advantages and disadvantages, new analogs with superior properties would be welcome. We find that a sauvagine-like peptide recently isolated from a different frog species, Pachymedusa dacnicolor (PD-Svg), is a high-affinity agonist whose radioiodinated analog, [(125)ITyr(0)-Glu(1), Nle(17)]-PD-Svg, exhibits improved biochemical properties over those of earlier iodinated agonists. Specifically, the PD-Svg radioligand binds both CRF receptors with comparably high affinity as its PS-Svg counterpart, but detects a greater number of sites on both type 1 and type 2 receptors. PD-Svg is also â¼10 times more potent at stimulating cAMP accumulation in cells expressing the native receptors. Autoradiographic localization using the PD-Svg radioligand shows robust specific binding to rodent brain and peripheral tissues that identifies consensus CRF receptor-expressing sites in a greater number and/or with greater sensitivity than its PS-Svg counterpart. We suggest that labeled analogs of PD-Svg may be useful tools for biochemical, structural, pharmacological, and anatomic studies of CRF receptors.
File Format	HTM / HTML
ISSN	00223565
e-ISSN	15210103
DOI	10.1124/jpet.114.222307
Journal	Journal of Pharmacology and Experimental Therapeutics
Issue Number	2
Volume Number	353
Language	English
Publisher	American Society for Pharmacology and Experimental Therapeutics
Publisher Date	2015-05-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Research Support, N.i.h., Extramural Amino Acid Sequence Cell Line Research Support, Non-u.s. Gov't Amphibian Proteins Molecular Sequence Data Metabolism Discipline Pharmacology Receptors, Corticotropin-releasing Hormone Protein Transport Anura Peptide Hormones Chemistry Animals Discipline Therapeutics Isotope Labeling Ligands Mice Radioligand Assay Kinetics
Content Type	Text
Resource Type	Article
Subject	Molecular Medicine Pharmacology

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

Characterization of a Pachymedusa dacnicolor–Sauvagine Analog as a New High-Affinity Radioligand for Corticotropin-Releasing Factor Receptor Studies

Surface properties of an amphiphilic peptide hormone and of its analog: corticotropin-releasing factor and sauvagine.

A sauvagine/corticotropin-releasing factor receptor expressed in heart and skeletal muscle.

Structural homology of corticotropin-releasing factor, sauvagine, and urotensin I: circular dichroism and prediction studies.

A single amino acid serves as an affinity switch between the receptor and the binding protein of corticotropin-releasing factor: implications for the design of agonists and antagonists.

Mapping of the ligand-selective domain of the Xenopus laevis corticotropin-releasing factor receptor 1: implications for the ligand-binding site.

Constitutive activation of tethered-peptide/corticotropin-releasing factor receptor chimeras.

Residue 17 of sauvagine cross-links to the first transmembrane domain of corticotropin-releasing factor receptor 1 (CRFR1).

Surface properties of an amphiphilic peptide hormone and of its analog: corticotropin-releasing factor and sauvagine.

Characterization of a Pachymedusa dacnicolor-Sauvagine analog as a new high-affinity radioligand for corticotropin-releasing factor receptor studies.

Similar Documents

Characterization of a Pachymedusa dacnicolor–Sauvagine Analog as a New High-Affinity Radioligand for Corticotropin-Releasing Factor Receptor Studies

Surface properties of an amphiphilic peptide hormone and of its analog: corticotropin-releasing factor and sauvagine.

A sauvagine/corticotropin-releasing factor receptor expressed in heart and skeletal muscle.

Structural homology of corticotropin-releasing factor, sauvagine, and urotensin I: circular dichroism and prediction studies.

A single amino acid serves as an affinity switch between the receptor and the binding protein of corticotropin-releasing factor: implications for the design of agonists and antagonists.

Mapping of the ligand-selective domain of the Xenopus laevis corticotropin-releasing factor receptor 1: implications for the ligand-binding site.

Constitutive activation of tethered-peptide/corticotropin-releasing factor receptor chimeras.

Residue 17 of sauvagine cross-links to the first transmembrane domain of corticotropin-releasing factor receptor 1 (CRFR1).

Surface properties of an amphiphilic peptide hormone and of its analog: corticotropin-releasing factor and sauvagine.

Characterization of a Pachymedusa dacnicolor-Sauvagine analog as a new high-affinity radioligand for corticotropin-releasing factor receptor studies.