Ablation of collagen IX and COMP disrupts epiphyseal cartilage architecture

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Ablation of collagen IX and COMP disrupts epiphyseal cartilage architecture. / Blumbach, Katrin; Niehoff, Anja; Paulsson, Mats; Zaucke, Frank.

In: Matrix biology : journal of the International Society for Matrix Biology, Vol. 27, No. 4, 01.05.2008, p. 306-318.

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@article{70604deedefd4134ac7cf28423204a08,
title = "Ablation of collagen IX and COMP disrupts epiphyseal cartilage architecture",
abstract = "Chondrodysplasias are a genetically heterogeneous group of skeletal disorders. Mutations in genes coding for cartilage oligomeric matrix protein (COMP), collagen IX and matrilin-3 have been described to cause the autosomal dominantly inherited form of multiple epiphyseal dysplasia (MED). Even though there is clear evidence that these cartilage matrix proteins interact with each other, their exact functions in matrix organisation and bone development still need to be elucidated. We generated a mouse model lacking both collagen IX and COMP to study the potential complementary role of these proteins in skeletal development. Mice deficient in both proteins exhibit shortened and widened long bones as well as an altered bone structure. They display severe growth plate abnormalities with large hypocellular areas in the central parts of the tibia. In addition, chondrocytes in the proliferative and hypertrophic zones do not show their typical columnar arrangement. These phenotypical traits were not observed in mice deficient only in COMP, while mice lacking only collagen IX showed similar growth plate disturbances and shorter and wider tibiae. The contribution of COMP to the phenotype of mice deficient in both collagen IX and COMP appears minor, even though clear differences in the deposition of matrilin-3 were detected.",
keywords = "Aging, Animals, Body Patterning, Bone and Bones, Collagen Type IX, Extracellular Matrix Proteins, Gene Expression Regulation, Developmental, Glycoproteins, Growth Plate, Matrilin Proteins, Mice, Mice, Inbred C57BL, Mice, Knockout",
author = "Katrin Blumbach and Anja Niehoff and Mats Paulsson and Frank Zaucke",
year = "2008",
month = "5",
day = "1",
doi = "10.1016/j.matbio.2007.11.007",
language = "English",
volume = "27",
pages = "306--318",
journal = "Matrix biology : journal of the International Society for Matrix Biology",
issn = "0945-053X",
publisher = "Elsevier",
number = "4",

}

RIS

TY - JOUR

T1 - Ablation of collagen IX and COMP disrupts epiphyseal cartilage architecture

AU - Blumbach, Katrin

AU - Niehoff, Anja

AU - Paulsson, Mats

AU - Zaucke, Frank

PY - 2008/5/1

Y1 - 2008/5/1

N2 - Chondrodysplasias are a genetically heterogeneous group of skeletal disorders. Mutations in genes coding for cartilage oligomeric matrix protein (COMP), collagen IX and matrilin-3 have been described to cause the autosomal dominantly inherited form of multiple epiphyseal dysplasia (MED). Even though there is clear evidence that these cartilage matrix proteins interact with each other, their exact functions in matrix organisation and bone development still need to be elucidated. We generated a mouse model lacking both collagen IX and COMP to study the potential complementary role of these proteins in skeletal development. Mice deficient in both proteins exhibit shortened and widened long bones as well as an altered bone structure. They display severe growth plate abnormalities with large hypocellular areas in the central parts of the tibia. In addition, chondrocytes in the proliferative and hypertrophic zones do not show their typical columnar arrangement. These phenotypical traits were not observed in mice deficient only in COMP, while mice lacking only collagen IX showed similar growth plate disturbances and shorter and wider tibiae. The contribution of COMP to the phenotype of mice deficient in both collagen IX and COMP appears minor, even though clear differences in the deposition of matrilin-3 were detected.

AB - Chondrodysplasias are a genetically heterogeneous group of skeletal disorders. Mutations in genes coding for cartilage oligomeric matrix protein (COMP), collagen IX and matrilin-3 have been described to cause the autosomal dominantly inherited form of multiple epiphyseal dysplasia (MED). Even though there is clear evidence that these cartilage matrix proteins interact with each other, their exact functions in matrix organisation and bone development still need to be elucidated. We generated a mouse model lacking both collagen IX and COMP to study the potential complementary role of these proteins in skeletal development. Mice deficient in both proteins exhibit shortened and widened long bones as well as an altered bone structure. They display severe growth plate abnormalities with large hypocellular areas in the central parts of the tibia. In addition, chondrocytes in the proliferative and hypertrophic zones do not show their typical columnar arrangement. These phenotypical traits were not observed in mice deficient only in COMP, while mice lacking only collagen IX showed similar growth plate disturbances and shorter and wider tibiae. The contribution of COMP to the phenotype of mice deficient in both collagen IX and COMP appears minor, even though clear differences in the deposition of matrilin-3 were detected.

KW - Aging

KW - Animals

KW - Body Patterning

KW - Bone and Bones

KW - Collagen Type IX

KW - Extracellular Matrix Proteins

KW - Gene Expression Regulation, Developmental

KW - Glycoproteins

KW - Growth Plate

KW - Matrilin Proteins

KW - Mice

KW - Mice, Inbred C57BL

KW - Mice, Knockout

U2 - 10.1016/j.matbio.2007.11.007

DO - 10.1016/j.matbio.2007.11.007

M3 - Journal articles

C2 - 18191556

VL - 27

SP - 306

EP - 318

JO - Matrix biology : journal of the International Society for Matrix Biology

JF - Matrix biology : journal of the International Society for Matrix Biology

SN - 0945-053X

IS - 4

ER -

ID: 21505