|Drosophila lysyl oxidases Dmloxl-1 and Dmloxl-2 are differentially expressed and the active DmLOXL-1 influences gene expression and development.|
|PMID: 15811848 Owner: NLM Status: MEDLINE|
|Mammalian lysyl oxidase (LOX) is essential for the catalysis of lysyl-derived cross-links in fibrillar collagens and elastin in the extracellular matrix and has also been implicated in cell motility, differentiation, and tumor cell invasion. The active LOX has been shown to translocate to the nuclei of smooth muscle cells and regulate chromatin structure and transcription. It is difficult to interpret the role of the LOX protein as it is co-expressed with other members of the LOX amine oxidase family in most mammalian cells. To investigate the function of the LOX proteins, we have characterized the Drosophila lysyl oxidases Dmloxl-1 and Dmloxl-2. We present the gene, domain structure, and expression pattern of Dmloxl-1 and Dmloxl-2 during development. In early development, only Dmloxl-1 was expressed, which allowed functional studies. We have expressed Dmloxl-1 in S2 cells and determined that it is a catalytically active enzyme, inhibited by beta-amino-proprionitrile (BAPN), a specific LOX inhibitor. We localized DmLOXL-1 in the nuclei in embryos and in adult salivary gland cells in the nuclei, cytoplasm, and cell surface, using immunostaining and a DmLOXL-1 antibody. To address the biological function of Dmloxl-1, we raised larvae under BAPN inhibitory conditions and over-expressed Dmloxl-1 in transgenic Drosophila. DmLOXL-1 inhibition resulted in developmental delay and a shift in sex ratio; over-expression in the w(m4) variegating strain increased drosopterin production, demonstrating euchromatinization. Our previous data on the transcriptional down-regulation of seven ribosomal genes and the glue gene under inhibitory conditions and the current results collectively support a nuclear role for Dmloxl-1 in euchromatinization and gene regulation.|
|Janos Molnar; Zsuzsanna Ujfaludi; Sheri F T Fong; John A Bollinger; Girma Waro; Ben Fogelgren; David M Dooley; Matyas Mink; Katalin Csiszar|
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|Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, U.S. Gov't, P.H.S. Date: 2005-04-04|
|Title: The Journal of biological chemistry Volume: 280 ISSN: 0021-9258 ISO Abbreviation: J. Biol. Chem. Publication Date: 2005 Jun|
|Created Date: 2005-06-13 Completed Date: 2005-07-19 Revised Date: 2007-11-14|
Medline Journal Info:
|Nlm Unique ID: 2985121R Medline TA: J Biol Chem Country: United States|
|Languages: eng Pagination: 22977-85 Citation Subset: IM|
|Cardiovascular Research Center, John A. Burns School of Medicine, University of Hawaii, Honolulu, 96822, USA.|
|Data Bank Information|
Bank Name/Acc. No.:
|GENBANK/AC007802; AC007803; AC008287; AC009349; AI260913; AJ295625; AJ295626; BT001394; M94054|
|APA/MLA Format Download EndNote Download BibTex|
Active Transport, Cell Nucleus
Amino Acid Sequence
Aminopropionitrile / pharmacology
Animals, Genetically Modified
Cell Membrane / metabolism
Cell Nucleus / metabolism
Chromatin / chemistry, metabolism
Collagen / chemistry
Cytoplasm / metabolism
DNA Primers / chemistry
DNA, Complementary / metabolism
Elastin / chemistry
Euchromatin / metabolism
Extracellular Matrix / metabolism
Gene Expression Regulation, Developmental*
Gene Expression Regulation, Enzymologic*
Molecular Sequence Data
Muscle, Smooth / cytology
Polymerase Chain Reaction
Protein Structure, Tertiary
Protein-Lysine 6-Oxidase / biosynthesis*, chemistry*
RNA, Messenger / metabolism
Recombinant Proteins / chemistry
Saliva / metabolism
Salivary Glands / metabolism
Sequence Homology, Amino Acid
|AR47713/AR/NIAMS NIH HHS; GM27659/GM/NIGMS NIH HHS; RR03061/RR/NCRR NIH HHS|
|0/Chromatin; 0/DNA Primers; 0/DNA, Complementary; 0/Euchromatin; 0/RNA, Messenger; 0/Recombinant Proteins; 151-18-8/Aminopropionitrile; 9007-34-5/Collagen; 9007-58-3/Elastin; EC 188.8.131.52/Protein-Lysine 6-Oxidase|
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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