Linked Life Data

11153697

Source:http://linkedlifedata.com/resource/pubmed/id/11153697

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
2001-1-10
pubmed:abstractText
Melanocytic dendrites consist of a central core of microtubules (MT) and a subcortical actin network. In previous reports we showed the presence of MT-associated motor proteins kinesin and cytoplasmic dynein on the melanosomal surface, forming a link with MT (Vancoillie et al. J Invest Dermatol 2000;114:421-429; Vancoillie et al. Br J Dermatol 2000;143:258-306). We could also demonstrate the association of kinectin, the kinesin receptor, with melanosomes. The interaction of cytoplasmic dynein with its cargoes is thought to be indirectly mediated by dynactin, a complex that binds to the dynein intermediate chain. Therefore, in this study, we investigated the in vitro expression of dynactin subunits P150Glued and P50 in normal human epidermal melanocytes, keratinocytes, and dermal fibroblasts by reverse transcription-polymerase chain reaction and northern blot analysis. In an attempt to gain an insight into the subcellular localization of dynactin, immunofluorescence and immunoelectron microscopy (IEM) studies were performed. The two isoforms of P150Glued and P50 are expressed in all studied skin cells. Immunofluorescence staining shows punctate distributions for P150Glued and P50 in melanocytes. P150Glued shows a clear centrosomal staining and accentuation in the dendrite tips. P50 is also accentuated in the perinuclear area and dendrite tips. Immunofluorescence double-labeling with a melanosome marker showed apparent colocalization of both P150Glued and P50 with melanosomes. By IEM, P50 is detected on the surface of the majority of melanosomes in melanocytes. The colocalization of different subunits of the dynactin complex with melanosomes is consistent with the earlier finding of cytoplasmic dynein association with melanosomes and supports the hypothesis that this complex could form a link between cytoplasmic dynein and the melanosomal membrane.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0893-5785
pubmed:author
pubmed:issnType
Print
pubmed:volume
13
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
449-57
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:11153697-Blotting, Northern, pubmed-meshheading:11153697-Cell Membrane, pubmed-meshheading:11153697-Cells, Cultured, pubmed-meshheading:11153697-Centrosome, pubmed-meshheading:11153697-Cytoplasm, pubmed-meshheading:11153697-Dyneins, pubmed-meshheading:11153697-Fibroblasts, pubmed-meshheading:11153697-Fluorescent Antibody Technique, Indirect, pubmed-meshheading:11153697-Humans, pubmed-meshheading:11153697-Melanocytes, pubmed-meshheading:11153697-Melanosomes, pubmed-meshheading:11153697-Microscopy, Confocal, pubmed-meshheading:11153697-Microscopy, Fluorescence, pubmed-meshheading:11153697-Microscopy, Immunoelectron, pubmed-meshheading:11153697-Microtubule-Associated Proteins, pubmed-meshheading:11153697-Protein Binding, pubmed-meshheading:11153697-Protein Isoforms, pubmed-meshheading:11153697-RNA, Messenger, pubmed-meshheading:11153697-Reverse Transcriptase Polymerase Chain Reaction, pubmed-meshheading:11153697-Skin, pubmed-meshheading:11153697-Tumor Cells, Cultured
pubmed:year
2000
pubmed:articleTitle
Colocalization of dynactin subunits P150Glued and P50 with melanosomes in normal human melanocytes.
pubmed:affiliation
Department of Dermatology, University Hospital, Ghent, Belgium.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't