Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
26
pubmed:dateCreated
1994-7-29
pubmed:abstractText
Osteoclast, the bone-resorbing cell, is formed from hematopoietic precursors via cell-cell fusion. To evaluate the possibility that under certain specific conditions mannose residues may be expressed on the mammalian cell surface, we examined the action of pradimicin derivatives, which bind specific sugars such as the mannose residue, on the formation of osteoclast induced in the coculture of mouse spleen cells with mouse stromal cells, a process in which cell-cell fusion is involved. Osteoclast formation was inhibited by treatment of this coculture system with pradimicin at the later stage (day 4-7), and this inhibition was specifically abrogated by mannose-rich yeast mannan. During the 8-day cocultivation, osteoclast formation was blocked by the pradimicin on days 6 and 7, when mononuclear preosteoclasts fused into multinucleated osteoclasts. With an interactive laser cytometer ACAS570, fluorescein isothiocyanate-labeled pradimicin was observed to bind osteoclast progenitors at the fusion stage and to have no binding affinity for osteoclast progenitors at the early stage (day 0-3) or for osteoclasts, which were formed after performing fusion between mononuclear preosteoclasts. These results suggest that mannose residues were expressed on outer membranes of monocytes under pathophysiological conditions and that they were involved in the osteoclast formation via cellular membrane fusion events.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
269
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
17572-6
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
Expression on outer membranes of mannose residues, which are involved in osteoclast formation via cellular fusion events.
pubmed:affiliation
Department of Physiological Chemistry, Graduate School, Tokyo Medical and Dental University, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't