Linked Life Data

19291362

Source:http://linkedlifedata.com/resource/pubmed/id/19291362

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2009-4-3
pubmed:abstractText
Galectin-3 binds beta-galactoside-containing sugars and is a chemoattractant for monocytes, macrophages, and neutrophils. Galectin-3 was identified by mass spectrometry from an anti-gI affinity column; however, we determined that galectin-3 did not bind gI, but rather that HSV-1 infection increased galectin-3 binding to carbohydrate residues on IgG. Our conclusions are based on the following observations: (1) galectin-3 from cells infected with a gI-deleted HSV-1 mutant virus bound anti-gI IgG; (2) galectin-3 from wild-type HSV-1 infected cells bound nonimmune IgG; (3) more galectin-3 from infected than uninfected cells bound IgG; and (4) binding to IgG was blocked by lactose, a competitive inhibitor of galectin-3 carbohydrate binding. HSV-1 infection did not increase galectin-3 expression, but did increase its secretion. We propose that increased carbohydrate binding and secretion of galectin-3 contribute to an early pro-inflammatory innate immune response to HSV-1 infection.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1432-8798
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
154
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
609-18
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
Herpes simplex virus type 1 infection increases the carbohydrate binding activity and the secretion of cellular galectin-3.
pubmed:affiliation
University of Pennsylvania, Philadelphia, 19104-6073, USA. rdking@mail.med.upenn.edu
pubmed:publicationType
Journal Article, Research Support, N.I.H., Extramural