Advanced

Polydispersity and heterogeneity of squid cranial cartilage proteoglycans as assessed by immunochemical methods and electron microscopy

Vynios, D H; Mörgelin, Matthias LU ; Papageorgakopoulou, N; Tsilemou, A; Spyracopoulou, G; Zafira, M and Tsiganos, C P (2000) In Biochimie 82(8). p.773-782
Abstract
The three populations of squid cranial cartilage proteoglycans, D1D1A, D1D1B and D1D2 appeared to have a high degree of polydispersity. Gel electrophoresis and immunoblotting analysis showed that polydispersity was mainly due to the variable size of chondroitin sulphate E chains. This was further ascertained after rotary shadowing electron microscopy of proteoglycan core proteins and glycosaminoglycan side chains and statistical analysis of the sizes measured for both components. Enzymic treatment of the proteoglycan core proteins produced different peptides from each population, suggesting that the observed heterogeneity of the proteoglycans is due to their core proteins. Antibodies were raised in rabbits against all proteoglycans and... (More)
The three populations of squid cranial cartilage proteoglycans, D1D1A, D1D1B and D1D2 appeared to have a high degree of polydispersity. Gel electrophoresis and immunoblotting analysis showed that polydispersity was mainly due to the variable size of chondroitin sulphate E chains. This was further ascertained after rotary shadowing electron microscopy of proteoglycan core proteins and glycosaminoglycan side chains and statistical analysis of the sizes measured for both components. Enzymic treatment of the proteoglycan core proteins produced different peptides from each population, suggesting that the observed heterogeneity of the proteoglycans is due to their core proteins. Antibodies were raised in rabbits against all proteoglycans and enzyme-linked immunosorbent analysis of proteoglycan core proteins revealed that the proteoglycans, even heterogeneous, shared many common epitopes. Part of the common proteoglycan epitopes were found to be located in chondroitin sulphate E chains. Heterogeneity of squid proteoglycans was also investigated by studying their interactions with collagen and it was found that only the two populations of high molecular mass, D1D1A and D1D2, were able to interact with only collagen type I, the latter stronger than the former. (Less)
Please use this url to cite or link to this publication:
author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Biochimie
volume
82
issue
8
pages
773 - 782
publisher
Elsevier
external identifiers
  • pmid:11018295
  • scopus:0033809450
ISSN
1638-6183
DOI
10.1016/S0300-9084(00)01156-1
language
English
LU publication?
yes
id
ff4368ba-b494-4a2a-8e5e-f6a08d36707b (old id 1117853)
date added to LUP
2008-06-25 09:06:32
date last changed
2017-01-01 04:45:18
@article{ff4368ba-b494-4a2a-8e5e-f6a08d36707b,
  abstract     = {The three populations of squid cranial cartilage proteoglycans, D1D1A, D1D1B and D1D2 appeared to have a high degree of polydispersity. Gel electrophoresis and immunoblotting analysis showed that polydispersity was mainly due to the variable size of chondroitin sulphate E chains. This was further ascertained after rotary shadowing electron microscopy of proteoglycan core proteins and glycosaminoglycan side chains and statistical analysis of the sizes measured for both components. Enzymic treatment of the proteoglycan core proteins produced different peptides from each population, suggesting that the observed heterogeneity of the proteoglycans is due to their core proteins. Antibodies were raised in rabbits against all proteoglycans and enzyme-linked immunosorbent analysis of proteoglycan core proteins revealed that the proteoglycans, even heterogeneous, shared many common epitopes. Part of the common proteoglycan epitopes were found to be located in chondroitin sulphate E chains. Heterogeneity of squid proteoglycans was also investigated by studying their interactions with collagen and it was found that only the two populations of high molecular mass, D1D1A and D1D2, were able to interact with only collagen type I, the latter stronger than the former.},
  author       = {Vynios, D H and Mörgelin, Matthias and Papageorgakopoulou, N and Tsilemou, A and Spyracopoulou, G and Zafira, M and Tsiganos, C P},
  issn         = {1638-6183},
  language     = {eng},
  number       = {8},
  pages        = {773--782},
  publisher    = {Elsevier},
  series       = {Biochimie},
  title        = {Polydispersity and heterogeneity of squid cranial cartilage proteoglycans as assessed by immunochemical methods and electron microscopy},
  url          = {http://dx.doi.org/10.1016/S0300-9084(00)01156-1},
  volume       = {82},
  year         = {2000},
}