NDLI: Chloroform extract of hog barn dust modulates skeletal muscle ryanodine receptor calcium-release channel (RyR1)

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Tian, Chengju Shao, Chun Hong Fenster, Danielle S. Mixan, Mark Romberger, Debra J. Toews, Myron L. Bidasee, Keshore R.
Description	Country affiliation: United States Author Affiliation: Tian C ( Department of Pharmacology and Experimental Neuroscience, University of Nebraska Medical Center, Omaha, NE 68198-5800, USA.)
Abstract	Skeletal muscle weakness is a reported ailment in individuals working in commercial hog confinement facilities. To date, specific mechanisms responsible for this symptom remain undefined. The purpose of this study was to assess whether hog barn dust (HBD) contains components that are capable of binding to and modulating the activity of type 1 ryanodine receptor Ca2+-release channel (RyR1), a key regulator of skeletal muscle function. HBD collected from confinement facilities in Nebraska were extracted with chloroform, filtered, and rotary evaporated to dryness. Residues were resuspended in hexane-chloroform (20:1) and precipitates, referred to as HBDorg, were air-dried and studied further. In competition assays, HBDorg dose-dependently displaced [3H]ryanodine from binding sites on RyR1 with an IC50 of 1.5±0.1 microg/ml (Ki=0.4±0.0 microg/ml). In single-channel assays using RyR1 reconstituted into a lipid bilayer, HBDorg exhibited three distinct dose-dependent effects: first it increased the open probability of RyR1 by increasing its gating frequency and dwell time in the open state, then it induced a state of reduced conductance (55% of maximum) that was more likely to occur and persist at positive holding potentials, and finally it irreversibly closed RyR1. In differentiated C2C12 myotubes, addition of HBD triggered a rise in intracellular Ca2+ that was blocked by pretreatment with ryanodine. Since persistent activation and/or closure of RyR1 results in skeletal muscle weakness, these new data suggest that HBD is responsible, at least in part, for the muscle ailment reported by hog confinement workers.
File Format	HTM / HTML
ISSN	87507587
e-ISSN	15221601
DOI	10.1152/japplphysiol.00123.2010
Journal	Journal of Applied Physiology
Issue Number	3
Volume Number	109
Language	English
Publisher	American Physiological Society
Publisher Date	2010-09-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Discipline Physiology Calcium Channel Agonists Pharmacology Calcium Channel Blockers Chloroform Chemistry Housing, Animal Ion Channel Gating Drug Effects Muscle, Skeletal Ryanodine Receptor Calcium Release Channel Solvents Agricultural Workers' Diseases Chemically Induced Animals Binding Sites Binding, Competitive Calcium Metabolism Adverse Effects Isolation & Purification Cell Line Chromatography, Thin Layer Dose-response Relationship, Drug Membrane Potentials Mice Muscle Fibers, Skeletal Muscle Weakness Occupational Health Rabbits Risk Assessment Ryanodine Sus Scrofa Research Support, N.i.h., Extramural Research Support, U.s. Gov't, P.h.s.
Content Type	Text
Resource Type	Article
Subject	Physiology Physiology (medical) Sports Science

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

Chloroform extract of hog barn dust modulates skeletal muscle ryanodine receptor calcium-release channel (RyR1)

Dust from hog confinement facilities impairs $Ca^{2+}$ mobilization from sarco(endo)plasmic reticulum by inhibiting ryanodine receptors

Use-dependent inhibition of the skeletal muscle ryanodine receptor by the suramin analogue NF676

$Ca^{2+}-calmodulin$ can activate and inactivate cardiac ryanodine receptors

Evidence for novel caffeine and $Ca^{2+}$ binding sites on the lobster skeletal ryanodine receptor

Scorpion toxins targeted against the sarcoplasmic reticulum Ca(2+)-release channel of skeletal and cardiac muscle.

Skeletal muscle calcium channel ryanodine and the development of pale, soft, and exudative meat in poultry.

Oxygen-coupled Redox Regulation of the Skeletal Muscle Ryanodine $Receptor/Ca^{2+}$ Release Channel (RyR1): SITES AND NATURE OF OXIDATIVE MODIFICATION

Regulation of the Skeletal Muscle Ryanodine $Receptor/Ca^{2+}-release$ Channel RyR1 by S-Palmitoylation

Chloroform extract of hog barn dust modulates skeletal muscle ryanodine receptor calcium-release channel (RyR1)

Similar Documents

Chloroform extract of hog barn dust modulates skeletal muscle ryanodine receptor calcium-release channel (RyR1)

Dust from hog confinement facilities impairs $Ca^{2+}$ mobilization from sarco(endo)plasmic reticulum by inhibiting ryanodine receptors

Use-dependent inhibition of the skeletal muscle ryanodine receptor by the suramin analogue NF676

$Ca^{2+}-calmodulin$ can activate and inactivate cardiac ryanodine receptors

Evidence for novel caffeine and $Ca^{2+}$ binding sites on the lobster skeletal ryanodine receptor

Scorpion toxins targeted against the sarcoplasmic reticulum Ca(2+)-release channel of skeletal and cardiac muscle.

Skeletal muscle calcium channel ryanodine and the development of pale, soft, and exudative meat in poultry.

Oxygen-coupled Redox Regulation of the Skeletal Muscle Ryanodine $Receptor/Ca^{2+}$ Release Channel (RyR1): SITES AND NATURE OF OXIDATIVE MODIFICATION

Regulation of the Skeletal Muscle Ryanodine $Receptor/Ca^{2+}-release$ Channel RyR1 by S-Palmitoylation

Chloroform extract of hog barn dust modulates skeletal muscle ryanodine receptor calcium-release channel (RyR1)