Linked Life Data

15140192

Source:http://linkedlifedata.com/resource/pubmed/id/15140192

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2004-5-13
pubmed:abstractText
Prestin is a motor protein of outer hair cells (OHC) that plays a crucial role in mammalian hearing. Prestin is a putative N-glycoprotein with three potential N-linked glycosylation sites. It is not known whether glycosylation affects the function and activity of prestin. Therefore, the effects of N-glycosylation were investigated by producing single-point (N163Q and N166Q) or double-point mutations (NN163/166QQ and NN163/166AA) at putative N-glycosylation sites. Further, treatment with tunicamycin or glycopeptidase-F was used to determine the consequences of removing N-linked glycosylation in wild-type prestin. We determined the effects of these manipulations on prestin's cell surface expression, molecular mass, glycosylation pattern, and electrophysiological properties in different cell-types. Data indicate that prestin is a glycoprotein with N-linked glycosylation sites at N163 and N166. N163 and N166 may have differential programs for synthesis and trimming of the glycans. The N166 site appears to have greater extent of glycosylation than its companion. N-linked glycosylation is not required for plasma membrane targeting of prestin. Both glycosylated and deglycosylated prestin demonstrate non-linear capacitance, a signature of prestin's motor function. Compared to glycosylated prestin, the fully de-glycosylated protein has altered electrophysiological function, with a change in membrane potential at most effective charge transfer to more depolarized values. These data suggest that glycosylation of prestin may quantitatively affect OHC electromotility.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0022-3042
pubmed:author
pubmed:issnType
Print
pubmed:volume
89
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
928-38
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed-meshheading:15140192-Animals, pubmed-meshheading:15140192-Anion Transport Proteins, pubmed-meshheading:15140192-Binding Sites, pubmed-meshheading:15140192-Cell Membrane, pubmed-meshheading:15140192-Cells, Cultured, pubmed-meshheading:15140192-Cricetinae, pubmed-meshheading:15140192-Electrophysiology, pubmed-meshheading:15140192-Fluorescent Antibody Technique, pubmed-meshheading:15140192-Gerbillinae, pubmed-meshheading:15140192-Glycoproteins, pubmed-meshheading:15140192-Glycosylation, pubmed-meshheading:15140192-Hair Cells, Auditory, Outer, pubmed-meshheading:15140192-Humans, pubmed-meshheading:15140192-Molecular Motor Proteins, pubmed-meshheading:15140192-Mutagenesis, Site-Directed, pubmed-meshheading:15140192-Opossums, pubmed-meshheading:15140192-Protein Transport, pubmed-meshheading:15140192-Proteins, pubmed-meshheading:15140192-Receptors, Neuropeptide, pubmed-meshheading:15140192-Receptors, Pituitary Hormone-Regulating Hormone, pubmed-meshheading:15140192-Structure-Activity Relationship, pubmed-meshheading:15140192-Transfection
pubmed:year
2004
pubmed:articleTitle
N-linked glycosylation sites of the motor protein prestin: effects on membrane targeting and electrophysiological function.
pubmed:affiliation
Auditory Physiology Laboratory, Department of Communication Sciences and Disorders, Northwestern University, Evanston, Illinois 60208, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.