PMID- 17006643
OWN - NLM
STAT- MEDLINE
DCOM- 20070411
LR  - 20220716
IS  - 0282-0080 (Print)
IS  - 0282-0080 (Linking)
VI  - 23
IP  - 7-8
DP  - 2006 Nov
TI  - Detection of oligosaccharide ligands for hepatocyte growth factor/scatter factor 
      (HGF/SF), keratinocyte growth factor (KGF/FGF-7), RANTES and heparin cofactor II 
      by neoglycolipid microarrays of glycosaminoglycan-derived oligosaccharide 
      fragments.
PG  - 513-23
AB  - Neoglycolipid technology is eminently adaptable for microarray design for 
      high-throughput detection and specificity assignments of carbohydrate-protein 
      interactions. Dermatan sulfate (DS) is known to play an important role because of 
      its ability to bind growth factors as well as chemokines and to modulate their 
      biological activities during inflammation and response to injury. We prepared 
      various iduronic acid-rich fragments from DS by complete digestion with 
      chondroitinase ACI, and investigated whether the DS-binding proteins, such as 
      HGF/SF, RANTES, KGF/FGF-7 and HCII, can detect their oligosaccharide ligands in a 
      neoglycolipid microarray. First, a comparison of the intensity of binding signals 
      obtained from chondroitin oligosaccharides with those of heparin oligosaccharides 
      showed that our microarray system is feasible not only to single-out the 
      oligosaccharide ligands, but also to detect the difference between an intrinsic 
      interaction unrelated only to electrostatic interaction and non-specific 
      electrostatic interaction. Second, HGF/SF, KGF/FGF-7 and HCII showed preferential 
      binding to iduronic acid-rich fragments of DS oligosaccharides that are greater 
      than 8-mers in lengths. In contrast, RANTES binding seemed to depend only on the 
      negative charges; their binding intensity towards the DS oligosaccharides was 
      somewhat stronger than the binding of HGF/SF, KGF/FGF-7 and HCII. Third, the use 
      of polyvinylpyrrolidone-40 (PVP-40), ovalbumin (OV) and Tween 20 in place of BSA 
      as a blotting agent was useful in these glycosaminoglycan dependent reactions to 
      minimize background due to non-specific interactions.
FAU - Yamaguchi, Keiko
AU  - Yamaguchi K
AD  - Department of Biotechnology, Faculty of Engineering, Kyoto Sangyo University, 
      Motoyama, Kita-ku, Kyoto, 603-8555, Japan.
FAU - Tamaki, Hirotoshi
AU  - Tamaki H
FAU - Fukui, Shigeyuki
AU  - Fukui S
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Glycoconj J
JT  - Glycoconjugate journal
JID - 8603310
RN  - 0 (Chemokine CCL5)
RN  - 0 (FGF7 protein, human)
RN  - 0 (Fluorescent Dyes)
RN  - 0 (Glycosaminoglycans)
RN  - 0 (HGF protein, human)
RN  - 0 (Ligands)
RN  - 0 (Oligosaccharides)
RN  - 0 (Recombinant Proteins)
RN  - 126469-10-1 (Fibroblast Growth Factor 7)
RN  - 67256-21-7 (Hepatocyte Growth Factor)
RN  - 81604-65-1 (Heparin Cofactor II)
RN  - 9005-49-6 (Heparin)
RN  - EC 4.2.2.- (Chondroitinases and Chondroitin Lyases)
RN  - EC 4.2.2.7 (Heparin Lyase)
SB  - IM
MH  - Animals
MH  - Cattle
MH  - Chemokine CCL5/*metabolism
MH  - Chondroitinases and Chondroitin Lyases
MH  - Fibroblast Growth Factor 7/*metabolism
MH  - Fluorescent Dyes
MH  - Glycosaminoglycans/chemistry/metabolism
MH  - Heparin/chemistry/metabolism
MH  - Heparin Cofactor II/*metabolism
MH  - Heparin Lyase
MH  - Hepatocyte Growth Factor/*metabolism
MH  - Humans
MH  - In Vitro Techniques
MH  - Ligands
MH  - Mice
MH  - Microarray Analysis/*methods
MH  - Oligosaccharides/chemistry/*metabolism
MH  - Protein Binding
MH  - Rabbits
MH  - Recombinant Proteins/metabolism
EDAT- 2006/09/29 09:00
MHDA- 2007/04/12 09:00
CRDT- 2006/09/29 09:00
PHST- 2005/08/21 00:00 [received]
PHST- 2006/01/12 00:00 [accepted]
PHST- 2006/01/09 00:00 [revised]
PHST- 2006/09/29 09:00 [pubmed]
PHST- 2007/04/12 09:00 [medline]
PHST- 2006/09/29 09:00 [entrez]
AID - 10.1007/s10719-006-7151-z [doi]
PST - ppublish
SO  - Glycoconj J. 2006 Nov;23(7-8):513-23. doi: 10.1007/s10719-006-7151-z.