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Dermatan sulfate domains defined by the novel antibody GD3A12, in normal tissues and ovarian adenocarcinomas

ten Dam, Gerdy B.; Yamada, Shuhei; Kobayashi, Fumi; Purushothaman, Anurag; van de Westerlo, Els M. A.; Bulten, Johan; Malmström, Anders LU ; Sugahara, Kazuyuki; Massuger, Leon F. and van Kuppevelt, Toin H. (2009) In Histochemistry and Cell Biology1995-01-01+01:00 132(1). p.117-127
Abstract
Dermatan sulfate (DS) expression in normal tissue and ovarian cancer was investigated using the novel, phage display-derived antibody GD3A12 that was selected against embryonic glycosaminoglycans (GAGs). Antibody GD3A12 was especially reactive with DS rich in IdoA-GalNAc4S disaccharide units. IdoA residues are important for antibody recognition as DS polymers with low numbers of IdoA residues were less reactive, and expression of the DS epimerase in ovarian carcinoma cells was associated with expression of the GD3A12 epitope. Moreover, staining of antibody GD3A12 was abolished by chondroitinase-B lyase digestion. Expression of DS domains defined by antibody GD3A12 was confined to connective tissue of most organs examined and presented as a... (More)
Dermatan sulfate (DS) expression in normal tissue and ovarian cancer was investigated using the novel, phage display-derived antibody GD3A12 that was selected against embryonic glycosaminoglycans (GAGs). Antibody GD3A12 was especially reactive with DS rich in IdoA-GalNAc4S disaccharide units. IdoA residues are important for antibody recognition as DS polymers with low numbers of IdoA residues were less reactive, and expression of the DS epimerase in ovarian carcinoma cells was associated with expression of the GD3A12 epitope. Moreover, staining of antibody GD3A12 was abolished by chondroitinase-B lyase digestion. Expression of DS domains defined by antibody GD3A12 was confined to connective tissue of most organs examined and presented as a typical fibrillar-type of staining. Differential expression of the DS epitopes recognized by antibodies GD3A12 and LKN1 (4/2,4 di-O-sulfated DS) was best seen in thymus and spleen, indicating differential expression of various DS domains in these organs. In ovarian carcinomas strong DS expression was found in the stromal parts, and occasionally on tumor cells. Partial co-localization in ovarian carcinomas was observed with decorin, versican and type I collagen suggesting a uniform distribution of this specific DS epitope. This unique anti-DS antibody may be instrumental to investigate the function, expression, and localization of specific DS domains in health and disease. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Dermatan sulfate, Glycosaminoglycans, Proteoglycans, Single chain, Ovarian cancer, variable fragment antibodies
in
Histochemistry and Cell Biology1995-01-01+01:00
volume
132
issue
1
pages
117 - 127
publisher
Springer
external identifiers
  • wos:000266822400012
  • scopus:67349286491
ISSN
1432-119X
DOI
10.1007/s00418-009-0592-2
language
English
LU publication?
yes
id
85b43073-139c-4dd9-b4df-711a2445e06f (old id 1443618)
date added to LUP
2009-07-17 12:39:23
date last changed
2017-01-01 04:58:34
@article{85b43073-139c-4dd9-b4df-711a2445e06f,
  abstract     = {Dermatan sulfate (DS) expression in normal tissue and ovarian cancer was investigated using the novel, phage display-derived antibody GD3A12 that was selected against embryonic glycosaminoglycans (GAGs). Antibody GD3A12 was especially reactive with DS rich in IdoA-GalNAc4S disaccharide units. IdoA residues are important for antibody recognition as DS polymers with low numbers of IdoA residues were less reactive, and expression of the DS epimerase in ovarian carcinoma cells was associated with expression of the GD3A12 epitope. Moreover, staining of antibody GD3A12 was abolished by chondroitinase-B lyase digestion. Expression of DS domains defined by antibody GD3A12 was confined to connective tissue of most organs examined and presented as a typical fibrillar-type of staining. Differential expression of the DS epitopes recognized by antibodies GD3A12 and LKN1 (4/2,4 di-O-sulfated DS) was best seen in thymus and spleen, indicating differential expression of various DS domains in these organs. In ovarian carcinomas strong DS expression was found in the stromal parts, and occasionally on tumor cells. Partial co-localization in ovarian carcinomas was observed with decorin, versican and type I collagen suggesting a uniform distribution of this specific DS epitope. This unique anti-DS antibody may be instrumental to investigate the function, expression, and localization of specific DS domains in health and disease.},
  author       = {ten Dam, Gerdy B. and Yamada, Shuhei and Kobayashi, Fumi and Purushothaman, Anurag and van de Westerlo, Els M. A. and Bulten, Johan and Malmström, Anders and Sugahara, Kazuyuki and Massuger, Leon F. and van Kuppevelt, Toin H.},
  issn         = {1432-119X},
  keyword      = {Dermatan sulfate,Glycosaminoglycans,Proteoglycans,Single chain,Ovarian cancer,variable fragment antibodies},
  language     = {eng},
  number       = {1},
  pages        = {117--127},
  publisher    = {Springer},
  series       = {Histochemistry and Cell Biology1995-01-01+01:00},
  title        = {Dermatan sulfate domains defined by the novel antibody GD3A12, in normal tissues and ovarian adenocarcinomas},
  url          = {http://dx.doi.org/10.1007/s00418-009-0592-2},
  volume       = {132},
  year         = {2009},
}