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 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

A Mutation in the Amino-Terminal End of the Triple Helix of Type II Collagen Causing Severe Osteochondrodysplasia

Genomics ◽  
1993 ◽  
Vol 16 (1) ◽  
pp. 282-285 ◽  
Author(s):  
Miikka Vikkula ◽  
Pertti Ritvaniemi ◽  
Alpo F. Vuorio ◽  
Ilkka Kaitila ◽  
Leena Ala-Kokko ◽  
...  
Keyword(s):  
Triple Helix ◽  
Type Ii Collagen ◽  
Type Ii ◽  
Amino Terminal

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

scholarly journals Human cathepsin K cleaves native type I and II collagens at the N-terminal end of the triple helix

1998 ◽  
Vol 331 (3) ◽  
pp. 727-732 ◽  
Author(s):  
Wa'el KAFIENAH ◽  
Dieter BRÖMME ◽  
David J. BUTTLE ◽  
Lisa J. CROUCHER ◽  
Anthony P. HOLLANDER
Keyword(s):  
Cleavage Site ◽  
Triple Helix ◽  
Type I Collagen ◽  
Cathepsin K ◽  
Type Ii Collagen ◽  
Collagenolytic Activity ◽  
Type I ◽  
Type Ii ◽  
Helical Domain ◽  
N Terminus

Cathepsin K (EC 3.4.22.38) is a recently described enzyme that has been shown to cleave type I collagen in its triple helix. The aim of this study was to determine if it also cleaves type II collagen in the triple helix and to identify the helical cleavage site(s) in types I and II collagens. Soluble human and bovine type II collagen, and rat type I collagen, were incubated with cathepsin K before the reaction was stopped with trans-epoxysuccinyl-l-leucylamido-(4-guanidino)butane (E-64). Analysis by SDS/PAGE of the collagen digests showed that optimal activity of cathepsin K against native type II collagen was between pH 5.0 and 5.5 and against denatured collagen between pH 4.0 and 7.0. The enzyme cleaved telopeptides as well as the α1(II) chains, generating multiple fragments in the range 90–120 kDa. The collagenolytic activity was not due to a contaminating metalloenzyme or serine proteinase as it was not inhibited by 1,10-phenanthroline, EDTA or 3,4-dichloroisocoumarin. Western blotting with anti-peptide antibodies to different regions of the α1(II) chain suggested that cathepsin K cleaved native α1(II) chains in the N-terminal region of the helical domain rather than at the well-defined collagenase cleavage site. This was confirmed by N-terminal sequencing of one of the fragments, revealing cleavage at a Gly-Lys bond, 58 residues from the N-terminus of the helical domain. By using a similar approach, cathepsin K was found to cleave native type I collagen close to the N-terminus of its triple helix. These results indicate that cathepsin K could have a role in the turnover of type II collagen, as well as type I collagen.

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.

Photo-crosslinked mono-component type II collagen hydrogel as a matrix to induce chondrogenic differentiation of bone marrow mesenchymal stem cells

2017 ◽  
Vol 5 (44) ◽  
pp. 8707-8718 ◽  
Author(s):  
Ke Yang ◽  
Jing Sun ◽  
Dan Wei ◽  
Lu Yuan ◽  
Jirong Yang ◽  
...  
Keyword(s):  
Stem Cells ◽  
Bone Marrow ◽  
Triple Helix ◽  
Chondrogenic Differentiation ◽  
Type Ii Collagen ◽  
Type Ii ◽  
Collagen Hydrogel ◽  
Component Type ◽  
Marrow Mesenchymal Stem Cells ◽  
P Type

Type II collagen methacrylamide with a triple helix was developed for 3D construction of a cartilaginous ECM-like microenvironment to induce chondrogenic differentiation of BMSCs.

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