Mice lacking the extracellular matrix adaptor protein matrilin-2 develop without obvious abnormalities
(2004) In Matrix Biology 23(3). p.195-204- Abstract
- Matrilins are putative adaptor proteins of the extracellular matrix (ECM) which can form both collagen-dependent and collagen-independent filamentous networks. While all known matrilins (matrilin-1, -2, -3, and -4) are expressed in cartilage, only matrilin-2 and matrilin-4 are abundant in non-skeletal tissues. To clarify the biological role of matrilin-2, we have developed a matrilin-2-deficient mouse strain. Matrilin-2 null mice show no gross abnormalities during embryonic or adult development, are fertile, and have a normal lifespan. Histological and ultrastructural analyses indicate apparently normal structure of all organs and tissues where matrilin-2 is expressed. Although matrilin-2 co-localizes with matrilin-4 in many tissues,... (More)
- Matrilins are putative adaptor proteins of the extracellular matrix (ECM) which can form both collagen-dependent and collagen-independent filamentous networks. While all known matrilins (matrilin-1, -2, -3, and -4) are expressed in cartilage, only matrilin-2 and matrilin-4 are abundant in non-skeletal tissues. To clarify the biological role of matrilin-2, we have developed a matrilin-2-deficient mouse strain. Matrilin-2 null mice show no gross abnormalities during embryonic or adult development, are fertile, and have a normal lifespan. Histological and ultrastructural analyses indicate apparently normal structure of all organs and tissues where matrilin-2 is expressed. Although matrilin-2 co-localizes with matrilin-4 in many tissues, Northern hybridization, semiquantitative RT-PCR, immunohistochemistry and biochemical analysis reveal no significant alteration in the steady-state level of matrilin-4 expression in homozygous mutant mice. Immunostaining of wild-type and mutant skin samples indicate no detectable differences in the expression and deposition of matrilin-2 binding partners including collagen I, laminin-nidogen complexes, fibrillin-2 and fibronectin. In addition, electron microscopy reveals an intact basement membrane at the epidermal-dermal junction and normal organization of the dermal collagen fibrils in mutant skin. These data suggest that either matrilin-2 and matrilin-2-mediated matrix-matrix interactions are dispensable for proper ECM assembly and function, or that they are efficiently compensated by other matrix components including wild-type levels of matrilin-4. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/269479
- author
- Mates, L ; Nicolae, C ; Mörgelin, Matthias LU ; Deak, F ; Kiss, I and Aszodi, A
- organization
- publishing date
- 2004
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- extracellular matrix, matrilin, cartilage, skin
- in
- Matrix Biology
- volume
- 23
- issue
- 3
- pages
- 195 - 204
- publisher
- Elsevier
- external identifiers
-
- wos:000223315700007
- scopus:3843080738
- ISSN
- 1569-1802
- DOI
- 10.1016/j.matbio.2004.05.003
- language
- English
- LU publication?
- yes
- id
- 34a7ba4a-4efa-4d4d-8006-8f524ea7ee70 (old id 269479)
- date added to LUP
- 2016-04-01 16:03:27
- date last changed
- 2022-01-28 17:00:45
@article{34a7ba4a-4efa-4d4d-8006-8f524ea7ee70,
abstract = {{Matrilins are putative adaptor proteins of the extracellular matrix (ECM) which can form both collagen-dependent and collagen-independent filamentous networks. While all known matrilins (matrilin-1, -2, -3, and -4) are expressed in cartilage, only matrilin-2 and matrilin-4 are abundant in non-skeletal tissues. To clarify the biological role of matrilin-2, we have developed a matrilin-2-deficient mouse strain. Matrilin-2 null mice show no gross abnormalities during embryonic or adult development, are fertile, and have a normal lifespan. Histological and ultrastructural analyses indicate apparently normal structure of all organs and tissues where matrilin-2 is expressed. Although matrilin-2 co-localizes with matrilin-4 in many tissues, Northern hybridization, semiquantitative RT-PCR, immunohistochemistry and biochemical analysis reveal no significant alteration in the steady-state level of matrilin-4 expression in homozygous mutant mice. Immunostaining of wild-type and mutant skin samples indicate no detectable differences in the expression and deposition of matrilin-2 binding partners including collagen I, laminin-nidogen complexes, fibrillin-2 and fibronectin. In addition, electron microscopy reveals an intact basement membrane at the epidermal-dermal junction and normal organization of the dermal collagen fibrils in mutant skin. These data suggest that either matrilin-2 and matrilin-2-mediated matrix-matrix interactions are dispensable for proper ECM assembly and function, or that they are efficiently compensated by other matrix components including wild-type levels of matrilin-4.}},
author = {{Mates, L and Nicolae, C and Mörgelin, Matthias and Deak, F and Kiss, I and Aszodi, A}},
issn = {{1569-1802}},
keywords = {{extracellular matrix; matrilin; cartilage; skin}},
language = {{eng}},
number = {{3}},
pages = {{195--204}},
publisher = {{Elsevier}},
series = {{Matrix Biology}},
title = {{Mice lacking the extracellular matrix adaptor protein matrilin-2 develop without obvious abnormalities}},
url = {{http://dx.doi.org/10.1016/j.matbio.2004.05.003}},
doi = {{10.1016/j.matbio.2004.05.003}},
volume = {{23}},
year = {{2004}},
}