Matrilin-2 interacts with itself and with other extracellular matrix proteins
(2002) In Biochemical Journal 367(3). p.715-721- Abstract
- Matrilin-2 is a component of extracellular filamentous networks. To study the interactions by which it can be integrated into such assemblies, full-length and truncated forms of matrilin-2 were recombinantly expressed in HEK-293 cells and purified from conditioned medium. The recombinant proteins, when used in interaction assays, showed affinity to matrilin-2 itself, but also to other collagenous and non-collagenous extracellular matrix proteins. The interaction between matrilin-2 and collagen I was studied in greater detail and could be shown to occur at distinct sites on the collagen I molecule and to have a K-D of about 3 x 10(-8) M. Interactions with some non-collagenous protein ligands were even stronger, with matrilin-2 binding to... (More)
- Matrilin-2 is a component of extracellular filamentous networks. To study the interactions by which it can be integrated into such assemblies, full-length and truncated forms of matrilin-2 were recombinantly expressed in HEK-293 cells and purified from conditioned medium. The recombinant proteins, when used in interaction assays, showed affinity to matrilin-2 itself, but also to other collagenous and non-collagenous extracellular matrix proteins. The interaction between matrilin-2 and collagen I was studied in greater detail and could be shown to occur at distinct sites on the collagen I molecule and to have a K-D of about 3 x 10(-8) M. Interactions with some non-collagenous protein ligands were even stronger, with matrilin-2 binding to fibrillin-2, fibronectin and laminin-1-nidogen-1 complexes, with K-D values in the range of 10(-8)-10(-11) M. Co-localization of matrilin-2 with these ligands in the dermal-epidermal basement membrane, in the microfibrils extending from the basement membrane into the dermis, and in the dermal extracellular matrix, indicates a physiological relevance of the interactions in the assembly of supramolecular extracellular matrix structures. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/324313
- author
- Piecha, D ; Wiberg, C ; Mörgelin, Matthias LU ; Reinhardt, DP ; Deak, F ; Maurer, P and Paulsson, M
- organization
- publishing date
- 2002
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- fibronectin, collagen, fibrillin, laminin, skin
- in
- Biochemical Journal
- volume
- 367
- issue
- 3
- pages
- 715 - 721
- publisher
- Portland Press
- external identifiers
-
- wos:000179177900016
- pmid:12180907
- scopus:0036847005
- pmid:12180907
- ISSN
- 0264-6021
- DOI
- 10.1042/BJ20021069
- language
- English
- LU publication?
- yes
- id
- 10041d46-3d4c-49f4-9614-d1a970a78daf (old id 324313)
- date added to LUP
- 2016-04-01 15:40:39
- date last changed
- 2022-01-28 06:33:00
@article{10041d46-3d4c-49f4-9614-d1a970a78daf,
abstract = {{Matrilin-2 is a component of extracellular filamentous networks. To study the interactions by which it can be integrated into such assemblies, full-length and truncated forms of matrilin-2 were recombinantly expressed in HEK-293 cells and purified from conditioned medium. The recombinant proteins, when used in interaction assays, showed affinity to matrilin-2 itself, but also to other collagenous and non-collagenous extracellular matrix proteins. The interaction between matrilin-2 and collagen I was studied in greater detail and could be shown to occur at distinct sites on the collagen I molecule and to have a K-D of about 3 x 10(-8) M. Interactions with some non-collagenous protein ligands were even stronger, with matrilin-2 binding to fibrillin-2, fibronectin and laminin-1-nidogen-1 complexes, with K-D values in the range of 10(-8)-10(-11) M. Co-localization of matrilin-2 with these ligands in the dermal-epidermal basement membrane, in the microfibrils extending from the basement membrane into the dermis, and in the dermal extracellular matrix, indicates a physiological relevance of the interactions in the assembly of supramolecular extracellular matrix structures.}},
author = {{Piecha, D and Wiberg, C and Mörgelin, Matthias and Reinhardt, DP and Deak, F and Maurer, P and Paulsson, M}},
issn = {{0264-6021}},
keywords = {{fibronectin; collagen; fibrillin; laminin; skin}},
language = {{eng}},
number = {{3}},
pages = {{715--721}},
publisher = {{Portland Press}},
series = {{Biochemical Journal}},
title = {{Matrilin-2 interacts with itself and with other extracellular matrix proteins}},
url = {{http://dx.doi.org/10.1042/BJ20021069}},
doi = {{10.1042/BJ20021069}},
volume = {{367}},
year = {{2002}},
}