関: lauroylsarcosine

English Journal

Detection of EPO-Fc fusion protein in human blood: screening and confirmation protocols for sports drug testing.

Reichel C, Thevis M.SourceDoping Control Laboratory, AIT Seibersdorf Laboratories, A-2444 Seibersdorf, Austria. christian.reichel@seibersdorf-laboratories.at
Drug testing and analysis.Drug Test Anal.2012 Nov;4(11):818-29. doi: 10.1002/dta.1381. Epub 2012 Jul 5.
The neonatal Fc receptor (FcRn) has been under investigation for several years as a pharmaceutical drug target. Clinical studies have shown that fusion proteins consisting of human recombinant erythropoietin (rhEPO) and the Fc-part of IgG can be transported after pulmonary administration via FcRn ac
PMID 22764129

Functional reconstitution and characterization of the Arabidopsis Mg(2+) transporter AtMRS2-10 in proteoliposomes.

Ishijima S, Shigemi Z, Adachi H, Makinouchi N, Sagami I.AbstractMagnesium (Mg(2+)) plays critical role in many physiological processes. The mechanism of Mg(2+) transport has been well documented in bacteria; however, less is known about Mg(2+) transporters in eukaryotes. The AtMRS2 family, which consists of 10 Arabidopsis genes, belongs to a eukaryotic subset of the CorA superfamily proteins. Proteins in this superfamily have been identified by a universally conserved GlyMetAsn motif and have been characterized as Mg(2+) transporters. Some members of the AtMRS2 family, including AtMRS2-10, may complement bacterial mutants or yeast mutants that lack Mg(2+) transport capabilities. Here, we report the purification and functional reconstitution of AtMRS2-10 into liposomes. AtMRS2-10, which contains an N-terminal His-tag, was expressed in Escherichia coli and solubilized with sarcosyl. The purified AtMRS2-10 protein was reconstituted into liposomes. AtMRS2-10 was inserted into liposomes in a unidirectional orientation. Direct measurement of Mg(2+) uptake into proteoliposomes revealed that reconstituted AtMRS2-10 transported Mg(2+) without any accessory proteins. Mutation in the GMN motif, M400 to I, inactivated Mg(2+) uptake. The AtMRS2-10-mediated Mg(2+) influx was blocked by Co(III)hexamine, and was independent of the external pH from 5 to 9. The activity of AtMRS2-10 was inhibited by Co(2+) and Ni(2+); however, it was not inhibited by Ca(2+), Fe(2+), or Fe(3+). While these results indicate that AtMRS2-10 has similar properties to the bacterial CorA proteins, unlike bacterial CorA proteins, AtMRS2-10 was potently inhibited by Al(3+). These studies demonstrate the functional capability of the AtMRS2 proteins in proteoliposomes to study structure-function relationships.
Biochimica et biophysica acta.Biochim Biophys Acta.2012 Sep;1818(9):2202-8. doi: 10.1016/j.bbamem.2012.04.015. Epub 2012 Apr 26.
Magnesium (Mg(2+)) plays critical role in many physiological processes. The mechanism of Mg(2+) transport has been well documented in bacteria; however, less is known about Mg(2+) transporters in eukaryotes. The AtMRS2 family, which consists of 10 Arabidopsis genes, belongs to a eukaryotic subset of
PMID 22560897

GSPE interferes with tau aggregation in vivo: implication for treating tauopathy.

Santa-Maria I, Diaz-Ruiz C, Ksiezak-Reding H, Chen A, Ho L, Wang J, Pasinetti GM.SourceDepartment of Neurology, Mount Sinai School of Medicine, New York, NY 10029, USA.
Neurobiology of aging.Neurobiol Aging.2012 Sep;33(9):2072-81. doi: 10.1016/j.neurobiolaging.2011.09.027. Epub 2011 Nov 4.
Tauopathies are characterized by progressive neurodegeneration caused by intracellular accumulation of hyperphosphorylated tau protein aggregates in the brain. The present study was designed to test whether a grape seed polyphenolic extract (GSPE) previously shown to inhibit tau protein aggregation
PMID 22054871