March 1999
Volume 40, Issue 3
Free
Articles  |   March 1999
Hyaluronan synthase expression in bovine eyes.
Author Affiliations
  • T Usui
    Department of Ophthalmology, University of Tokyo, Japan.
  • K Suzuki
    Department of Ophthalmology, University of Tokyo, Japan.
  • Y Kaji
    Department of Ophthalmology, University of Tokyo, Japan.
  • S Amano
    Department of Ophthalmology, University of Tokyo, Japan.
  • K Miyata
    Department of Ophthalmology, University of Tokyo, Japan.
  • P Heldin
    Department of Ophthalmology, University of Tokyo, Japan.
  • H Yamashita
    Department of Ophthalmology, University of Tokyo, Japan.
Investigative Ophthalmology & Visual Science March 1999, Vol.40, 563-567. doi:
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    • Get Citation

      T Usui, K Suzuki, Y Kaji, S Amano, K Miyata, P Heldin, H Yamashita; Hyaluronan synthase expression in bovine eyes.. Invest. Ophthalmol. Vis. Sci. 1999;40(3):563-567.

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      © ARVO (1962-2015); The Authors (2016-present)

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Abstract

PURPOSE: Hyaluronan (HA), a high-molecular-weight linear glycosaminoglycan, is a component of the extracellular matrix (ECM). It is expressed in eyes and plays important roles in many biologic processes, including cell migration, proliferation, and differentiation. Hyaluronan is produced by HA synthase (HAS), which has three isoforms: HAS1, HAS2, and HAS3. In this study, the HAS expression in the anterior segment of bovine eyes was investigated to determine the significance of HA in eyes. METHODS: To obtain bovine HAS probes, degenerate oligonucleotide primers, based on well-conserved amino acid sequences including the catalytic region of each HAS isoform, were used for reverse transcription-polymerase chain reaction to amplify mRNA from bovine corneal endothelial cells (BCECs). Hyaluronan synthase-1 expression in the anterior segment of bovine eyes at the protein level was investigated by immunohistochemistry. RESULTS: All three HAS isoforms were expressed in BCECs at the mRNA level. Amplified cDNA fragments of HAS1, HAS2, and HAS3 from BCECs can be aligned to human counterparts, showing similarities of 100%, 97.3%, and 100%, respectively, at the amino acid level. Hyaluronan synthase 1 was expressed at the protein level in corneal epithelium, keratocyte, corneal endothelium, conjunctival epithelium, ciliary epithelium, capillary endothelium, and trabecular meshwork. CONCLUSIONS: Hyaluronan synthase isoforms were expressed in the ocular anterior segment and are speculated to be involved in HA production in situ.

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