October 1995
Volume 36, Issue 11
Free
Articles  |   October 1995
Sequence, molecular properties, and chromosomal mapping of mouse lumican.
Author Affiliations
  • J L Funderburgh
    Division of Biology, Kansas State University, Manhattan 66506-4901, USA.
  • M L Funderburgh
    Division of Biology, Kansas State University, Manhattan 66506-4901, USA.
  • N D Hevelone
    Division of Biology, Kansas State University, Manhattan 66506-4901, USA.
  • M E Stech
    Division of Biology, Kansas State University, Manhattan 66506-4901, USA.
  • M J Justice
    Division of Biology, Kansas State University, Manhattan 66506-4901, USA.
  • C Y Liu
    Division of Biology, Kansas State University, Manhattan 66506-4901, USA.
  • W W Kao
    Division of Biology, Kansas State University, Manhattan 66506-4901, USA.
  • G W Conrad
    Division of Biology, Kansas State University, Manhattan 66506-4901, USA.
Investigative Ophthalmology & Visual Science October 1995, Vol.36, 2296-2303. doi:
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      J L Funderburgh, M L Funderburgh, N D Hevelone, M E Stech, M J Justice, C Y Liu, W W Kao, G W Conrad; Sequence, molecular properties, and chromosomal mapping of mouse lumican.. Invest. Ophthalmol. Vis. Sci. 1995;36(11):2296-2303.

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Abstract

PURPOSE: Lumican is a major proteoglycan of vertebrate cornea. This study characterizes mouse lumican, its molecular form, cDNA sequence, and chromosomal localization. METHODS: Lumican sequence was determined from cDNA clones selected from a mouse corneal cDNA expression library using a bovine lumican cDNA probe. Tissue expression and size of lumican mRNA were determined using Northern hybridization. Glycosidase digestion followed by Western blot analysis provided characterization of molecular properties of purified mouse corneal lumican. Chromosomal mapping of the lumican gene (Lcn) used Southern hybridization of a panel of genomic DNAs from an interspecific murine backcross. RESULTS: Mouse lumican is a 338-amino acid protein with high-sequence identity to bovine and chicken lumican proteins. The N-terminus of the lumican protein contains consensus sequences for tyrosine sulfation. A 1.9-kb lumican mRNA is present in cornea and several other tissues. Antibody against bovine lumican reacted with recombinant mouse lumican expressed in Escherichia coli and also detected high molecular weight proteoglycans in extracts of mouse cornea. Keratanase digestion of corneal proteoglycans released lumican protein, demonstrating the presence of sulfated keratan sulfate chains on mouse corneal lumican in vivo. The lumican gene (Lcn) was mapped to the distal region of mouse chromosome 10. The Lcn map site is in the region of a previously identified developmental mutant, eye blebs, affecting corneal morphology. CONCLUSIONS: This study demonstrates sulfated keratan sulfate proteoglycan in mouse cornea and describes the tools (antibodies and cDNA) necessary to investigate the functional role of this important corneal molecule using naturally occurring and induced mutants of the murine lumican gene.

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