PMID- 10067958
OWN - NLM
STAT- MEDLINE
DCOM- 19990310
LR  - 20171116
IS  - 0146-0404 (Print)
IS  - 0146-0404 (Linking)
VI  - 40
IP  - 3
DP  - 1999 Mar
TI  - Hyaluronan synthase expression in bovine eyes.
PG  - 563-7
AB  - 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.
FAU - Usui, T
AU  - Usui T
AD  - Department of Ophthalmology, University of Tokyo, Japan.
FAU - Suzuki, K
AU  - Suzuki K
FAU - Kaji, Y
AU  - Kaji Y
FAU - Amano, S
AU  - Amano S
FAU - Miyata, K
AU  - Miyata K
FAU - Heldin, P
AU  - Heldin P
FAU - Yamashita, H
AU  - Yamashita H
LA  - eng
PT  - Comparative Study
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Invest Ophthalmol Vis Sci
JT  - Investigative ophthalmology & visual science
JID - 7703701
RN  - 0 (DNA Primers)
RN  - 0 (Isoenzymes)
RN  - 0 (Membrane Proteins)
RN  - 0 (RNA, Messenger)
RN  - 0 (Xenopus Proteins)
RN  - EC 2.- (Transferases)
RN  - EC 2.4.- (Glycosyltransferases)
RN  - EC 2.4.1.17 (Glucuronosyltransferase)
RN  - EC 2.4.1.212 (HAS1 protein, Xenopus)
RN  - EC 2.4.1.212 (Hyaluronan Synthases)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Anterior Eye Segment/*enzymology
MH  - Cattle
MH  - Cells, Cultured
MH  - Ciliary Body/cytology/metabolism
MH  - Conjunctiva/cytology/metabolism
MH  - DNA Primers/chemistry
MH  - Endothelium, Vascular/metabolism
MH  - Epithelium/metabolism
MH  - Glucuronosyltransferase/genetics/*metabolism
MH  - *Glycosyltransferases
MH  - Humans
MH  - Hyaluronan Synthases
MH  - Immunoenzyme Techniques
MH  - Isoenzymes/genetics/metabolism
MH  - *Membrane Proteins
MH  - Molecular Sequence Data
MH  - RNA, Messenger/metabolism
MH  - Reverse Transcriptase Polymerase Chain Reaction
MH  - Sequence Homology, Amino Acid
MH  - Trabecular Meshwork/cytology/metabolism
MH  - *Transferases
MH  - *Xenopus Proteins
EDAT- 1999/03/06 00:00
MHDA- 1999/03/06 00:01
CRDT- 1999/03/06 00:00
PHST- 1999/03/06 00:00 [pubmed]
PHST- 1999/03/06 00:01 [medline]
PHST- 1999/03/06 00:00 [entrez]
PST - ppublish
SO  - Invest Ophthalmol Vis Sci. 1999 Mar;40(3):563-7.