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Kinesin and kinectin can associate with the melanosomal surface and form a link with microtubules in normal human melanocytes

Garnet Vancoillie, Jo Lambert UGent, Aat Mulder, Henk K Koerten, A Mieke Mommaas, Patric Van Oostveldt UGent and Jean-Marie Naeyaert (2000) JOURNAL OF INVESTIGATIVE DERMATOLOGY. 114(3). p.421-429
abstract
Microtubuli play an important role in the organization of organelles and membrane traffic. They are present in melanocytic dendrites through which melanosomes are transported towards keratinocytes. Besides the actin-based motility systems, microtubuli-associated motor proteins also play a critical role in melanosome movement, as has recently been confirmed in mouse melanocytes. We investigated the in vitro expression of two forms of human conventional kinesin and its receptor kinectin in normal human epidermal melanocytes, keratinocytes, and dermal fibroblasts by reverse transcription polymerase chain reaction and northern blot analysis. In an attempt to gain insight into the subcellular distribution of kinesin and kinectin in melanocytes, double immunofluorescent staining and immunogold electron microscopy were performed. In all studied skin cells ubiquitous and neuronal kinesin are expressed, as well as the kinectin receptor. Immunofluorescent staining shows distinct but partially overlapping distributions for kinesin heavy chain and melanosomes, suggesting that kinesin is associated with some but not all of the melanosomes. Similar observations for kinectin indicate that this receptor can colocalize with melanosomes, which was confirmed by immunoelectron microscopy. The latter technique allowed us to demonstrate a close association between kinesin heavy chain, microtubuli, and melanosomes. The combined data from reverse transcription polymerase chain reaction, northern blot analysis, double immunofluorescent staining, and immunogold electron microscopy suggest that kinesins and kinectin have an important role in microtubuli-based melanosome transport in human melanocytes.
Please use this url to cite or link to this publication:
author
organization
year
type
journalArticle (original)
publication status
published
subject
journal title
JOURNAL OF INVESTIGATIVE DERMATOLOGY
J. Invest. Dermatol.
volume
114
issue
3
pages
421 - 429
Web of Science type
Article
Web of Science id
000086187800004
ISSN
0022-202X
DOI
10.1046/j.1523-1747.2000.00896.x
language
English
UGent publication?
yes
classification
A1
copyright statement
I have transferred the copyright for this publication to the publisher
id
134139
handle
http://hdl.handle.net/1854/LU-134139
date created
2004-01-14 13:37:00
date last changed
2016-12-19 15:38:05
@article{134139,
  abstract     = {Microtubuli play an important role in the organization of organelles and membrane traffic. They are present in melanocytic dendrites through which melanosomes are transported towards keratinocytes. Besides the actin-based motility systems, microtubuli-associated motor proteins also play a critical role in melanosome movement, as has recently been confirmed in mouse melanocytes. We investigated the in vitro expression of two forms of human conventional kinesin and its receptor kinectin in normal human epidermal melanocytes, keratinocytes, and dermal fibroblasts by reverse transcription polymerase chain reaction and northern blot analysis. In an attempt to gain insight into the subcellular distribution of kinesin and kinectin in melanocytes, double immunofluorescent staining and immunogold electron microscopy were performed. In all studied skin cells ubiquitous and neuronal kinesin are expressed, as well as the kinectin receptor. Immunofluorescent staining shows distinct but partially overlapping distributions for kinesin heavy chain and melanosomes, suggesting that kinesin is associated with some but not all of the melanosomes. Similar observations for kinectin indicate that this receptor can colocalize with melanosomes, which was confirmed by immunoelectron microscopy. The latter technique allowed us to demonstrate a close association between kinesin heavy chain, microtubuli, and melanosomes. The combined data from reverse transcription polymerase chain reaction, northern blot analysis, double immunofluorescent staining, and immunogold electron microscopy suggest that kinesins and kinectin have an important role in microtubuli-based melanosome transport in human melanocytes.},
  author       = {Vancoillie, Garnet and Lambert, Jo and Mulder, Aat and Koerten, Henk K and Mommaas, A Mieke and Van Oostveldt, Patric and Naeyaert, Jean-Marie},
  issn         = {0022-202X},
  journal      = {JOURNAL OF INVESTIGATIVE DERMATOLOGY},
  language     = {eng},
  number       = {3},
  pages        = {421--429},
  title        = {Kinesin and kinectin can associate with the melanosomal surface and form a link with microtubules in normal human melanocytes},
  url          = {http://dx.doi.org/10.1046/j.1523-1747.2000.00896.x},
  volume       = {114},
  year         = {2000},
}

Chicago
Vancoillie, Garnet, Jo Lambert, Aat Mulder, Henk K Koerten, A Mieke Mommaas, Patric Van Oostveldt, and Jean-Marie Naeyaert. 2000. “Kinesin and Kinectin Can Associate with the Melanosomal Surface and Form a Link with Microtubules in Normal Human Melanocytes.” Journal of Investigative Dermatology 114 (3): 421–429.
APA
Vancoillie, Garnet, Lambert, J., Mulder, A., Koerten, H. K., Mommaas, A. M., Van Oostveldt, P., & Naeyaert, J.-M. (2000). Kinesin and kinectin can associate with the melanosomal surface and form a link with microtubules in normal human melanocytes. JOURNAL OF INVESTIGATIVE DERMATOLOGY, 114(3), 421–429.
Vancouver
1.
Vancoillie G, Lambert J, Mulder A, Koerten HK, Mommaas AM, Van Oostveldt P, et al. Kinesin and kinectin can associate with the melanosomal surface and form a link with microtubules in normal human melanocytes. JOURNAL OF INVESTIGATIVE DERMATOLOGY. 2000;114(3):421–9.
MLA
Vancoillie, Garnet, Jo Lambert, Aat Mulder, et al. “Kinesin and Kinectin Can Associate with the Melanosomal Surface and Form a Link with Microtubules in Normal Human Melanocytes.” JOURNAL OF INVESTIGATIVE DERMATOLOGY 114.3 (2000): 421–429. Print.