---
pmid: '15836428'
title: 'Identification and characterization of photomedins: novel olfactomedin-domain-containing
  proteins with chondroitin sulphate-E-binding activity.'
authors:
- Furutani Y
- Manabe R
- Tsutsui K
- Yamada T
- Sugimoto N
- Fukuda S
- Kawai J
- Sugiura N
- Kimata K
- Hayashizaki Y
- Sekiguchi K
journal: Biochem J
year: '2005'
full_text_available: false
pmcid: PMC1180717
doi: 10.1042/BJ20050120
pubmed_publication_types:
- Journal Article
- Research Support, Non-U.S. Gov't
publication_type: PRIMARY_RESEARCH
---

# Identification and characterization of photomedins: novel olfactomedin-domain-containing proteins with chondroitin sulphate-E-binding activity.
**Authors:** Furutani Y, Manabe R, Tsutsui K, Yamada T, Sugimoto N, Fukuda S, Kawai J, Sugiura N, Kimata K, Hayashizaki Y, Sekiguchi K
**Journal:** Biochem J (2005)
**DOI:** [10.1042/BJ20050120](https://doi.org/10.1042/BJ20050120)
**PMC:** [PMC1180717](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1180717/)

## Abstract

1. Biochem J. 2005 Aug 1;389(Pt 3):675-84. doi: 10.1042/BJ20050120.

Identification and characterization of photomedins: novel
olfactomedin-domain-containing proteins with chondroitin sulphate-E-binding
activity.

Furutani Y(1), Manabe R, Tsutsui K, Yamada T, Sugimoto N, Fukuda S, Kawai J,
Sugiura N, Kimata K, Hayashizaki Y, Sekiguchi K.

Author information:
(1)Sekiguchi Biomatrix Signaling Project, Exploratory Research for Advanced
Technology (ERATO), Japan Science and Technology Agency, Aichi Medical
University, Nagakute, Aichi, 480-1195, Japan.

We screened more than 60000 RIKEN mouse cDNAs for novel ECM (extracellular
matrix) proteins by extensive computational screening followed by recombinant
expression and immunohistochemical characterization. We identified two novel
olfactomedin-family proteins characterized by the presence of tandem CXCXCX9C
motifs in the N-terminal region, a coiled-coil domain and an olfactomedin domain
in the C-terminal region. These proteins, named photomedin-1 and photomedin-2,
were secreted as disulphide-bonded dimers (photomedin-1) or oligomers/multimers
(photomedin-2) with O-linked carbohydrate chains, although photomedin-1 was
proteolytically processed in the middle of the molecule after secretion. In the
retina, photomedin-1 was selectively expressed in the outer segment of
photoreceptor cells and photomedin-2 was expressed in all retinal neurons. Among
a panel of ECM components, including glycosaminoglycans, photomedins
preferentially bound to chondroitin sulphate-E and heparin. These results,
together, indicate that photomedins are novel olfactomedin-domain-containing
extracellular proteins capable of binding to proteoglycans containing these
glycosaminoglycan chains.

DOI: 10.1042/BJ20050120
PMCID: PMC1180717
PMID: 15836428 [Indexed for MEDLINE]