Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes.

Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes. Research Abstract Details 

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Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes. Abstract Text:

An Chi,Julio C Valencia,Zhang-Zhi Hu,Hidenori Watabe,Hiroshi Yamaguchi,Nancy J Mangini,Hongzhan Huang,Victor A Canfield,Keith C Cheng,Feng Yang,Riichiro Abe,Shoichi Yamagishi,Jeffrey Shabanowitz,Vincent J Hearing,Cathy Wu,Ettore Appella,Donald F Hunt,

Melanin, which is responsible for virtually all visible skin, hair, and eye pigmentation in humans, is synthesized, deposited, and distributed in subcellular organelles termed melanosomes. A comprehensive determination of the protein composition of this organelle has been obstructed by the melanin present. Here, we report a novel method of removing melanin that includes in-solution digestion and immobilized metal affinity chromatography (IMAC). Together with in-gel digestion, this method has allowed us to characterize melanosome proteomes at various developmental stages by tandem mass spectrometry. Comparative profiling and functional characterization of the melanosome proteomes identified approximately 1500 proteins in melanosomes of all stages, with approximately 600 in any given stage. These proteins include 16 homologous to mouse coat color genes and many associated with human pigmentary diseases. Approximately 100 proteins shared by melanosomes from pigmented and nonpigmented melanocytes define the essential melanosome proteome. Proteins validated by confirming their intracellular localization include PEDF (pigment-epithelium derived factor) and SLC24A5 (sodium/potassium/calcium exchanger 5, NCKX5). The sharing of proteins between melanosomes and other lysosome-related organelles suggests a common evolutionary origin. This work represents a model for the study of the biogenesis of lysosome-related organelles.

Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes. Publishing Authors By Initials

A Chi,JC Valencia,ZZ Hu,H Watabe,H Yamaguchi,NJ Mangini,H Huang,VA Canfield,KC Cheng,F Yang,R Abe,S Yamagishi,J Shabanowitz,VJ Hearing,C Wu,E Appella,DF Hunt,

For similar enzymes and coenzymes: enzymes: hydrolases: peptide hydrolases: endopeptidases: serine endopeptidases: trypsin research abstracts see: enzymes and coenzymes: enzymes: hydrolases: peptide hydrolases: endopeptidases: serine endopeptidases: trypsin research

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Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Journal of proteome research

VOLUME: 5

Page Numbers: 3135-44

Journal Abbreviation: J. Proteome Res.

ISSN: 1535-3893

DAY: 3

MONTH: Nov

YEAR: 2006

Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 101128775

Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes. Keywords Mesh Terms:

KEYWORDS: Trypsin

MESH TERMS: methods

Chemical & Substance for Abstract: Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes. Information

Substance Name: Trypsin

Registry Number: EC 3.4.21.4

Grant and Affiliation Information for Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes.

AFFILIATION: Department of Chemistry, University of Virginia, Charlottesville, Virginia 22904, USA.

Country: United States

AGENCY: United States NHGRI

GRANT: U01-HG02712

ACRONYM: HG

MEDLINETA: J Proteome Res

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