Matrilin-2, a large, oligomeric matrix protein, is expressed by a great variety of cells and forms fibrillar networks
(1999) In Journal of Biological Chemistry 274(19). p.13353-13361- Abstract
- Matrilin-2 is a member of the protein superfamily with von Willebrand factor type A-like modules. Mouse matrilin-2 cDNA fragments were expressed in 293-EBNA cells, and the protein was purified, characterized, and used to immunize rabbits. The affinity-purified antiserum detects matrilin-2 in dense and loose connective tissue structures, subepithelial connective tissue of the skin and digestive tract, specialized cartilages, and blood vessel walls. In situ hybridization of 35S-labeled riboprobes localizes the matrilin-2 mRNA to fibroblasts of dermis, tendon, ligaments, perichondrium, and periosteum; connective tissue elements in the heart; smooth muscle cells; and epithelia and loose connective tissue cells of the alimentary canal and... (More)
- Matrilin-2 is a member of the protein superfamily with von Willebrand factor type A-like modules. Mouse matrilin-2 cDNA fragments were expressed in 293-EBNA cells, and the protein was purified, characterized, and used to immunize rabbits. The affinity-purified antiserum detects matrilin-2 in dense and loose connective tissue structures, subepithelial connective tissue of the skin and digestive tract, specialized cartilages, and blood vessel walls. In situ hybridization of 35S-labeled riboprobes localizes the matrilin-2 mRNA to fibroblasts of dermis, tendon, ligaments, perichondrium, and periosteum; connective tissue elements in the heart; smooth muscle cells; and epithelia and loose connective tissue cells of the alimentary canal and respiratory tract. RNA blot hybridization and immunoblotting revealed both matrilin-2 mRNA and protein in cultures of a variety of cell types, confirming the tissue distribution. Alternative splicing affects a module unique for matrilin-2 in all of the above RNA sources. SDS-polyacrylamide gel electrophoresis and electron microscopy reveals matrilin-2 from tissue extracts and cell line cultures as a mixture of mono-, di-, tri-, and tetramers. Matrilin-2 is substituted with N-linked oligosaccharides but not with glycosaminoglycans. Because of other, yet unidentified, cell-type dependent posttranslational modifications, the monomer is heterogeneous in size. Immunofluorescence showed that matrilin-2 functions by forming an extracellular, filamentous network. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1115483
- author
- Piecha, D ; Muratoglu, S ; Mörgelin, Matthias LU ; Hauser, N ; Studer, D ; Kiss, I ; Paulsson, M and Deak, F
- organization
- publishing date
- 1999
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Journal of Biological Chemistry
- volume
- 274
- issue
- 19
- pages
- 13353 - 13361
- publisher
- American Society for Biochemistry and Molecular Biology
- external identifiers
-
- pmid:10224097
- scopus:0033531935
- ISSN
- 1083-351X
- language
- English
- LU publication?
- yes
- id
- 5c686158-b895-42d8-890b-68a9cf3f948d (old id 1115483)
- alternative location
- http://www.jbc.org/cgi/content/full/274/19/13353
- date added to LUP
- 2016-04-01 12:24:27
- date last changed
- 2022-04-21 06:59:44
@article{5c686158-b895-42d8-890b-68a9cf3f948d,
abstract = {{Matrilin-2 is a member of the protein superfamily with von Willebrand factor type A-like modules. Mouse matrilin-2 cDNA fragments were expressed in 293-EBNA cells, and the protein was purified, characterized, and used to immunize rabbits. The affinity-purified antiserum detects matrilin-2 in dense and loose connective tissue structures, subepithelial connective tissue of the skin and digestive tract, specialized cartilages, and blood vessel walls. In situ hybridization of 35S-labeled riboprobes localizes the matrilin-2 mRNA to fibroblasts of dermis, tendon, ligaments, perichondrium, and periosteum; connective tissue elements in the heart; smooth muscle cells; and epithelia and loose connective tissue cells of the alimentary canal and respiratory tract. RNA blot hybridization and immunoblotting revealed both matrilin-2 mRNA and protein in cultures of a variety of cell types, confirming the tissue distribution. Alternative splicing affects a module unique for matrilin-2 in all of the above RNA sources. SDS-polyacrylamide gel electrophoresis and electron microscopy reveals matrilin-2 from tissue extracts and cell line cultures as a mixture of mono-, di-, tri-, and tetramers. Matrilin-2 is substituted with N-linked oligosaccharides but not with glycosaminoglycans. Because of other, yet unidentified, cell-type dependent posttranslational modifications, the monomer is heterogeneous in size. Immunofluorescence showed that matrilin-2 functions by forming an extracellular, filamentous network.}},
author = {{Piecha, D and Muratoglu, S and Mörgelin, Matthias and Hauser, N and Studer, D and Kiss, I and Paulsson, M and Deak, F}},
issn = {{1083-351X}},
language = {{eng}},
number = {{19}},
pages = {{13353--13361}},
publisher = {{American Society for Biochemistry and Molecular Biology}},
series = {{Journal of Biological Chemistry}},
title = {{Matrilin-2, a large, oligomeric matrix protein, is expressed by a great variety of cells and forms fibrillar networks}},
url = {{http://www.jbc.org/cgi/content/full/274/19/13353}},
volume = {{274}},
year = {{1999}},
}