A large family with features of pseudoachondroplasia and multiple epiphyseal dysplasia: exclusion of seven candidate gene loci that encode proteins of the cartilage extracellular matrix

1994 ◽  
Vol 93 (3) ◽  
pp. 236-242 ◽  
Author(s):  
David L. Rimoin ◽  
I. Merete Rasmussen ◽  
Michael D. Briggs ◽  
Peter J. Roughley ◽  
Helen E. Gruber ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Candidate Gene ◽  
Large Family ◽  
Multiple Epiphyseal Dysplasia ◽  
Cartilage Extracellular Matrix ◽  
Epiphyseal Dysplasia

scholarly journals The ECM-Cell Interaction of Cartilage Extracellular Matrix on Chondrocytes

2014 ◽  
Vol 2014 ◽  
pp. 1-8 ◽  
Author(s):  
Yue Gao ◽  
Shuyun Liu ◽  
Jingxiang Huang ◽  
Weimin Guo ◽  
Jifeng Chen ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Large Family ◽  
Type Ii Collagen ◽  
Cell Interaction ◽  
Matrix Remodeling ◽  
Cell Matrix ◽  
Kinase C ◽  
Cartilage Extracellular Matrix ◽  
Adhesive Interactions ◽  
Wnt Signal

Cartilage extracellular matrix (ECM) is composed primarily of the network type II collagen (COLII) and an interlocking mesh of fibrous proteins and proteoglycans (PGs), hyaluronic acid (HA), and chondroitin sulfate (CS). Articular cartilage ECM plays a crucial role in regulating chondrocyte metabolism and functions, such as organized cytoskeleton through integrin-mediated signaling via cell-matrix interaction. Cell signaling through integrins regulates several chondrocyte functions, including differentiation, metabolism, matrix remodeling, responses to mechanical stimulation, and cell survival. The major signaling pathways that regulate chondrogenesis have been identified as wnt signal, nitric oxide (NO) signal, protein kinase C (PKC), and retinoic acid (RA) signal. Integrins are a large family of molecules that are central regulators in multicellular biology. They orchestrate cell-cell and cell-matrix adhesive interactions from embryonic development to mature tissue function. In this review, we emphasize the signaling molecule effect and the biomechanics effect of cartilage ECM on chondrogenesis.

scholarly journals Disruption of Extracellular Matrix Structure May Cause Pseudoachondroplasia Phenotypes in the Absence of Impaired Cartilage Oligomeric Matrix Protein Secretion

2006 ◽  
Vol 281 (43) ◽  
pp. 32587-32595 ◽  
Author(s):  
Markus Schmitz ◽  
Alexander Becker ◽  
Alexander Schmitz ◽  
Christian Weirich ◽  
Mats Paulsson ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Endoplasmic Reticulum ◽  
Cartilage Oligomeric Matrix Protein ◽  
Matrix Protein ◽  
Major Element ◽  
Multiple Epiphyseal Dysplasia ◽  
Transfected Cells ◽  
Primary Chondrocytes ◽  
Cell Matrix ◽  
Epiphyseal Dysplasia

Pseudoachondroplasia and multiple epiphyseal dysplasia are two dominantly inherited chondrodysplasias associated with mutations in cartilage oligomeric matrix protein (COMP). The rarely available patient biopsies show lamellar inclusions in the endoplasmic reticulum. We studied the pathogenesis of these chondrodysplasias by expressing several disease-causing COMP mutations in bovine primary chondrocytes and found that COMP-associated chondrodysplasias are not exclusively storage diseases. Although COMP carrying the mutations D469Δ and D475N was retained within the endoplasmic reticulum, secretion of COMP H587R was only slightly retarded. All pseudoachondroplasia mutations impair cellular viability and cause a disruption of the extracellular matrix formed in alginate culture irrespective of the degree of cellular retention. The mutation D361Y associated with the clinically milder disease multiple epiphyseal dysplasia gave mild retention and limited matrix alterations, but the transfected cells showed normal viability. The effect of mutated COMP on matrix formation and cell-matrix interaction may be a major element in the pathogenesis of COMP-associated chondrodysplasias.

scholarly journals Recessive multiple epiphyseal dysplasia and Stargardt disease in two sisters

2021 ◽  
Author(s):  
Leonardo Gatticchi ◽  
Dominika Vešelényiová ◽  
Jan Miertus ◽  
Paolo Enrico Maltese ◽  
Elena Manara ◽  
...  
Keyword(s):  
Multiple Epiphyseal Dysplasia ◽  
Stargardt Disease ◽  
Epiphyseal Dysplasia

MULTIPLE EPIPHYSEAL DYSPLASIA: A FAMILY STUDY

Rheumatology ◽  
1979 ◽  
Vol 18 (4) ◽  
pp. 239-242 ◽  
Author(s):  
T. GIBSON ◽  
J. HIGHTON
Keyword(s):  
Family Study ◽  
Multiple Epiphyseal Dysplasia ◽  
Epiphyseal Dysplasia

scholarly journals Macromolecular Interactions in Cartilage Extracellular Matrix Vary According to the Cartilage Type and Location

Cartilage ◽  
2021 ◽  
pp. 194760352110008
Author(s):  
Manula S. B. Rathnayake ◽  
Brooke L. Farrugia ◽  
Karyna Kulakova ◽  
Colet E. M. ter Voert ◽  
Gerjo J. V. M. van Osch ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Dry Weight ◽  
Extraction Methods ◽  
Auricular Cartilage ◽  
Nasal Cartilage ◽  
Sulfated Glycosaminoglycan ◽  
Cartilage Extracellular Matrix ◽  
Matrix Interactions ◽  
Anatomic Locations ◽  
Extracellular Matrix Interactions

Objective To investigate GAG-ECM (glycosaminoglycan–extracellular matrix) interactions in different cartilage types. To achieve this, we first aimed to determine protocols for consistent calculation of GAG content between cartilage types. Design Auricular cartilage containing both collagen and elastin was used to determine the effect of lyophilization on GAG depletion activity. Bovine articular, auricular, meniscal, and nasal cartilage plugs were treated using different reagents to selectively remove GAGs. Sulfated glycosaminoglycan (sGAG) remaining in the sample after treatment were measured, and sGAG loss was compared between cartilage types. Results The results indicate that dry weight of cartilage should be measured prior to cartilage treatment in order to provide a more accurate reference for normalization. Articular, meniscal, and nasal cartilage lost significant amounts of sGAG for all reagents used. However, only hyaluronidase was able to remove significant amount of sGAG from auricular cartilage. Furthermore, hyaluronidase was able to remove over 99% of sGAG from all cartilage types except auricular cartilage where it only removed around 76% of sGAG. The results indicate GAG-specific ECM binding for different cartilage types and locations. Conclusions In conclusion, lyophilization can be performed to determine native dry weight for normalization without affecting the degree of GAG treatment. To our knowledge, this is the first study to compare GAG-ECM interactions of different cartilage types using different GAG extraction methods. Degree of GAG depletion not only varied with cartilage type but also the same type from different anatomic locations. This suggests specific structure-function roles for GAG populations found in the tissues.

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