Incorporation of Structurally Defective Type II Collagen into Cartilage Matrix in Kniest Chondrodysplasia

1998 ◽  
Vol 355 (2) ◽  
pp. 282-290 ◽  
Author(s):  
Russell J. Fernandes ◽  
Douglas J. Wilkin ◽  
Mary Ann Weis ◽  
William R. Wilcox ◽  
Daniel H. Cohn ◽  
...  
Keyword(s):  
Type Ii Collagen ◽  
Cartilage Matrix ◽  
Type Ii

scholarly journals Turnover of type II collagen and aggrecan in cartilage matrix at the onset of inflammatory arthritis in humans: Relationship to mediators of systemic and local inflammation

2003 ◽  
Vol 48 (11) ◽  
pp. 3085-3095 ◽  
Author(s):  
Alexander Fraser ◽  
Ursula Fearon ◽  
R. Clark Billinghurst ◽  
Mirela Ionescu ◽  
Richard Reece ◽  
...  
Keyword(s):  
Inflammatory Arthritis ◽  
Type Ii Collagen ◽  
Cartilage Matrix ◽  
Type Ii ◽  
Local Inflammation

Achondrogensis type II: A heterozygous point mutation prevents deposition of type II collagen into the cartilage matrix

1994 ◽  
Vol 14 (5) ◽  
pp. 389
Author(s):  
Danny Chan ◽  
C.W. Chow ◽  
William G. Cole ◽  
John F. Bateman
Keyword(s):  
Point Mutation ◽  
Type Ii Collagen ◽  
Cartilage Matrix ◽  
Type Ii

Disproportionate micromelia (Dmm): an incomplete dominant mouse dwarfism with abnormal cartilage matrix

Development ◽  
1981 ◽  
Vol 62 (1) ◽  
pp. 165-182
Author(s):  
Kenneth S. Brown ◽  
Robert E. Cranley ◽  
Robert Greene ◽  
Hynda K. Kleinman ◽  
John P. Pennypacker
Keyword(s):  
Type Ii Collagen ◽  
Cartilage Matrix ◽  
Type Ii ◽  
Cartilage Growth ◽  
Normal Cartilage ◽  
The Matrix ◽  
Collagen Antibodies ◽  
Biochemical Analyses ◽  
Cartilage Proteoglycans ◽  
Cartilage Growth Plate

This paper describes a new autosomal incomplete dominant dwarfism, disproportionate micromelia, which has been characterized genetically and phenotypically, and the cartilage of homozygotes, and heterozygotes has been examined by histochemical, immunofluorescence and biochemical methods. Homozygotes, which die at birth, are disproportionately short and have cleft palates. The heterozygotes appear normal at birth but beginning at 1 week of age dwarfism is apparent and increases during growth. Histochemical and biochemical analyses of the cartilage rudiments of homozygotes at day 18 of gestation demonstrate that the cartilage growth plate is disorganized and that the matrix components, collagen and proteoglycan, are altered. Total collagen synthesis is reduced by approximately 30% and the amount of type II collagen is greatly reduced. By immunofluorescence staining with collagen antibodies, it appears that type II collagen is located primarily near the cell surface of chondrocytes but is poorly distributed throughout the remainder of the matrix. The amount of proteoglycan in the cartilage matrix is reduced by approximately 70% as determined by chemical analysis of hexosamines and by [35S]sulfate incorporation. Although the proteoglycans synthesized by the mutant are normal in size and in glycosaminoglycan composition, they were more easily extractable from the matrix than were normal cartilage proteoglycans. Heterozygotes had reduced cartilage matrix proteoglycan by histochemical methods, but the organization of the epiphyseal cartilage was not abnormal. These data suggest that a reduced or abnormal cartilage matrix is the cause of the dwarfism.

Type II collagen Pro-α-chains containing a Gly574Ser mutation are not incorporated into the cartilage matrix of transgenic mice

1997 ◽  
Vol 16 (3) ◽  
pp. 93-103 ◽  
Author(s):  
B.Kerry Maddox ◽  
Silvio Garofalo ◽  
Douglas R. Keene ◽  
Chad Smith ◽  
William A. Horton
Keyword(s):  
Transgenic Mice ◽  
Type Ii Collagen ◽  
Cartilage Matrix ◽  
Type Ii

scholarly journals Extracellular matrix formation by chondrocytes in monolayer culture.

1981 ◽  
Vol 90 (1) ◽  
pp. 78-83 ◽  
Author(s):  
W Dessau ◽  
B M Vertel ◽  
H von der Mark ◽  
K von der Mark
Keyword(s):  
Extracellular Space ◽  
Monolayer Culture ◽  
Spherical Shape ◽  
Type Ii Collagen ◽  
Cartilage Matrix ◽  
Pericellular Matrix ◽  
Type Ii ◽  
Culture Dish ◽  
Immunofluorescence Labeling ◽  
Matrix Characteristic

In previous studies were have reported on the secretion and extracellular deposition of type II collagen and fibronectin (Dessau et al., 1978, J. Cell Biol., 79:342-355) and chondroitin sulfate proteoglycan (CSPG) (Vertel and Dorfman, 1979, Proc. Natl. Acad. Sci. U. S. A. 76:1261-1264) in chondrocyte cultures. This study describes a combined effort to compare sequence and pattern of secretion and deposition of all three macromolecules in the same chondrocyte culture experiment. By immunofluorescence labeling experiments, we demonstrate that type II collagen, fibronectin, and CSPG reappear on the cell surface after enzymatic release of chondrocytes from embryonic chick cartilage but develop different patterns in the pericellular matrix. When chondrocytes spread on the culture dish, CSPG is deposited in the extracellular space as an amorphous mass and fibronectin forms fine, intercellular strands, whereas type II collagen disappears from the chondrocyte surface and remains absent from the extracellular space in early cultures. Only after cells in the center of chondrocyte colonies shape reassume spherical shape does the immunofluorescence reveal type II collagen in the refractile matrix characteristic of differentiated cartilage. By immunofluorescence double staining of the newly formed cartilage matrix, we demonstrate that CSPG spreads farther out into the extracellular space that type II collagen. Fibronectin finally disappears from the cartilage matrix.

scholarly journals The calcification of cartilage matrix in chondrocyte culture: studies of the C-propeptide of type II collagen (chondrocalcin).

1987 ◽  
Vol 104 (5) ◽  
pp. 1435-1441 ◽  
Author(s):  
A Hinek ◽  
A Reiner ◽  
A R Poole
Keyword(s):  
Growth Plate ◽  
Type Ii Collagen ◽  
Close Correlation ◽  
Cartilage Matrix ◽  
Type Ii ◽  
Growth Plate Chondrocytes ◽  
Culture Studies ◽  
Chondrocyte Culture ◽  
Intracellular Content ◽  
Bovine Fetuses

We have shown that when chondrocytes are isolated by collagenase digestion of hyaline cartilage from growth plate, nasal, and epiphyseal cartilages of bovine fetuses they rapidly elaborate an extracellular matrix in culture. Only growth plate chondrocytes can calcify this matrix as ascertained by incorporation of 45Ca2+, detection of mineral with von Kossa's stain and electron microscopy. There is an extremely close direct correlation between 45Ca2+ incorporation in the first 24 h of culture and the content of the C-propeptide of type II collagen, measured by radioimmunoassay, at the time of isolation and during culture. Moreover, growth plate cells have an increased intracellular content of the C-propeptide per deoxyribonucleic acid and, during culture, per hydroxyproline (as a measure of helical collagen) compared with nasal and epiphyseal chondrocytes. In growth plate chondrocytes 24,25-dihydroxycholecalciferol (24,25-[OH]2D3), but not 1,25-dihydroxycholecalciferol alone, stimulates the net synthesis of the C-propeptide and calcification; proteoglycan net synthesis is unaffected. Together, these metabolites of vitamin D further stimulate C-propeptide net synthesis but do not further increase calcification stimulated by 24,25-(OH)2D3. These observations further demonstrate the close correlation between the C-propeptide of type II collagen and the calcification of cartilage matrix.

scholarly journals Chondrocalcin is identical with the C-propeptide of type II procollagen

1986 ◽  
Vol 237 (3) ◽  
pp. 923-925 ◽  
Author(s):  
M Van der Rest ◽  
L C Rosenberg ◽  
B R Olsen ◽  
A R Poole
Keyword(s):  
Primary Structure ◽  
Triple Helix ◽  
Type Ii Collagen ◽  
Cartilage Matrix ◽  
Type Ii ◽  
Sequence Analyses ◽  
Tryptic Peptides ◽  
Cartilage Calcification ◽  
Matrix Molecule

The primary structure of the cartilage matrix molecule chondrocalcin has been found to be identical with that of the C-propeptide of type II procollagen by comparing sequence analyses of the N-terminal regions and of tryptic peptides derived from chondrocalcin. This implies that in type II collagen the C-propeptide of type II collagen is employed not only in the assembly of the triple helix of type II collagen, as demonstrated previously, but in calcifying cartilage it may also be involved in those events leading to cartilage calcification, as earlier indicated.

scholarly journals Cartilage matrix protein forms a type II collagen-independent filamentous network: analysis in primary cell cultures with a retrovirus expression system.

1995 ◽  
Vol 6 (12) ◽  
pp. 1743-1753 ◽  
Author(s):  
Q Chen ◽  
D M Johnson ◽  
D R Haudenschild ◽  
M M Tondravi ◽  
P F Goetinck
Keyword(s):  
Growth Factor ◽  
Matrix Protein ◽  
Expression System ◽  
Type Ii Collagen ◽  
Cartilage Matrix ◽  
Type Ii ◽  
Tail Domain ◽  
Filament Formation ◽  
Wild Type ◽  
Epidermal Growth

Cartilage matrix protein (CMP) is expressed specifically in mature cartilage and consists of two von Willebrand factor A domains (CMP-A1 and CMP-A2) that are separated by an epidermal growth factor-like domain, and a coiled-coil tail domain at the carboxyl terminal end. We have shown previously that CMP interacts with type II collagen-containing fibrils in cartilage. In this study, we describe a type II collagen-independent CMP filament and we analyze the structural requirement for the formation of this type of filament. Recombinant wild-type CMP and two mutant forms were expressed in chick primary cell cultures using a retrovirus expression system. In chondrocytes, the wild-type virally encoded CMP is able to form disulfide bonded trimers and to assemble into filaments. Filaments also form with CMP whose Cys455 and Cys457 in the tail domain were mutagenized to prevent interchain disulfide bond formation. Therefore, intermolecular disulfide bonds are not necessary for the assembly of CMP into filaments. Both the wild-type and the double cysteine mutant also form filaments in fibroblasts, indicating that chondrocyte-specific factors are not required for filament formation. A truncated form of CMP that consists only of the CMP-A2 domain and the tail domain can form trimers but fails to form filaments, indicating that the deleted CMP-A1 domain and/or the epidermal growth factor domain are necessary for filament assembly but not for trimer formation. Furthermore, the expression of the virally encoded truncated CMP in chondrocyte culture disrupts endogenous CMP filament formation. Together these data suggest a role for CMP in cartilage matrix assembly by forming filamentous networks that require participation and coordination of individual domains of CMP.

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