Polydispersity and heterogeneity of squid cranial cartilage proteoglycans as assessed by immunochemical methods and electron microscopy
(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:
https://lup.lub.lu.se/record/1117853
- author
- Vynios, D H ; Mörgelin, Matthias LU ; Papageorgakopoulou, N ; Tsilemou, A ; Spyracopoulou, G ; Zafira, M and Tsiganos, C P
- organization
- publishing date
- 2000
- 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
- 2016-04-01 12:00:49
- date last changed
- 2022-01-26 21:34:00
@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}},
doi = {{10.1016/S0300-9084(00)01156-1}},
volume = {{82}},
year = {{2000}},
}