Gene regulation during cartilage differentiation: temporal and spatial expression of link protein and cartilage matrix protein in the developing limb

Development ◽  
1989 ◽  
Vol 107 (1) ◽  
pp. 23-33
Author(s):  
N.S. Stirpe ◽  
P.F. Goetinck
Keyword(s):  
Matrix Protein ◽  
Core Protein ◽  
Type Ii Collagen ◽  
Cartilage Matrix ◽  
Type Ii ◽  
Spatial Expression ◽  
Link Protein ◽  
Genes Encoding ◽  
Temporal And Spatial ◽  
And Cartilage

The temporal and spatial expression of link protein and cartilage matrix protein genes was defined during chondrogenesis in the developing chick embryonic wing bud, using RNA in situ hybridization. For comparison, the expression of genes encoding type II collagen and cartilage proteoglycan core protein was also examined. Link protein transcripts are first detected at stage 25 of Hamburger and Hamilton, together with proteoglycan core protein transcripts. Type II collagen transcripts were first detected as early as stage 23 whereas cartilage matrix protein transcripts could not be detected before stage 26. The results of the study indicate that the temporal expression of the genes for cartilage matrix protein and type II collagen are independent of each other and also independent of that for link protein and proteoglycan core protein.

The Formation of Cartilage Extracellular Matrix

1988 ◽  
Vol 46 ◽  
pp. 230-231
Author(s):  
B.M. Vertel
Keyword(s):  
Extracellular Matrix ◽  
Hyaline Cartilage ◽  
Core Protein ◽  
Type Ii Collagen ◽  
Type Ii ◽  
Structural Components ◽  
Normal Cartilage ◽  
Link Protein ◽  
Cartilage Extracellular Matrix ◽  
Compression Type

Normal cartilage function is dependent upon the unique structural properties of the extensive extracellular matrix (ECM). In final assembled form, the ECM of hyaline cartilage is composed of abundant amounts of proteoglycan (PG) and type II collagen. Additional collagens and glycoproteins may be important structural components as well. Through their concentration of negative charges, PGs confer upon the cartilage ECM the ability to retain high levels of hydration and thereby resist compression. Type II collagen fibers contribute to the tensile strength of cartilage.In the cartilage ECM, PG monomers associate with hyaluronic acid and link protein to form large aggregates. In turn, PG aggregates are associated with the fibrous meshwork of type II collagen. Interactions with other ECM molecules may occur as well. The cartilage matrix constituents are themselves large and complex. For example, the PG monomer is 1-5 x 106 daltons in size and contains a core protein of Mr >300K (comprising only 8-10% of the complete monomer).

scholarly journals PSVI-33 Undenatured type II collagen mitigates inflammation and cartilage degeneration in healthy untrained Labrador retrievers after exercise

2020 ◽  
Vol 98 (Supplement_4) ◽  
pp. 313-314
Author(s):  
Jessica L Varney ◽  
Jason W Fowler ◽  
Craig N Coon
Keyword(s):  
Matrix Protein ◽  
Inflammatory Marker ◽  
Type Ii Collagen ◽  
Cartilage Degeneration ◽  
Type Ii ◽  
Cell Counts ◽  
Healthy Dogs ◽  
Labrador Retrievers ◽  
And Cartilage ◽  
Undenatured Type Ii Collagen

Abstract Exercise can cause microtrauma in the tissue and joints of dogs, resulting in a cycle of inflammation and discomfort even in healthy dogs. The aim of this trial was to evaluate the effect of undenatured type II collagen supplemented on inflammation and cartilage degeneration after exercise in untrained, healthy dogs. In this experiment, 40 healthy Labrador retrievers (20m/20f; Range-5-12yrs; Avg-8yrs) were sorted into two groups: undenatured type II collagen group receiving 40mg UC-II® (10mg Collagen Type II/Min. 3% Undenatured Type II Collagen; Lonza Consumer Health, Inc.) and placebo (P) group receiving 40mg maltodextrin daily by capsule. After 2wks supplement loading, all dogs performed a 4.66 ± 0.34km endurance run. Blood was collected at baseline, 1h pre-run, and 24h post-run for hematology/biomarkers including interleukin-6 (IL-6) as an inflammatory marker and cartilage oligomeric matrix protein (COMP) as a cartilage degeneration marker. Undenatured type II collagen supplemented dogs had significantly lower IL-6 vs P at post-run (p< 0.01), as well as significant decreases from pre to post-run (P = 0.03), vs P with no significant change (P = 0.16). COMP was significantly lower in undenatured type II collagen supplemented dogs at 24h post-run compared to pre-run (P = 0.02), with P dogs having no significant differences between timepoints (P = 0.24). At both 1h pre- and 24h post-run undenatured type II collagen supplemented dogs had no significant increases in neutrophil:lymphocyte ratio (NLR; inflammatory marker), but P dogs had significantly higher NLR compared to baseline (P = 0.01). NLR was also significantly lower in undenatured type II collagen supplemented dogs compared to P dogs at pre-run (P < 0.01). Undenatured type II collagen supplemented dogs showed significantly lower white blood cell counts after supplementation compared to P dogs (P < 0.05) (Table 1). In summary, untrained Labrador retrievers supplemented with undenatured type II collagen had decreased inflammation and cartilage degeneration compared to non-supplemented dogs after exercise.

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.

scholarly journals Marathon Running Increases Synthesis and Decreases Catabolism of Joint Cartilage Type II Collagen Accompanied by High-Energy Demands and an Inflamatory Reaction

2021 ◽  
Vol 12 ◽  
Author(s):  
José A. Hernández-Hermoso ◽  
Lexa Nescolarde ◽  
Emma Roca ◽  
Elena Revuelta-López ◽  
Jordi Ara ◽  
...  
Keyword(s):  
Inflammatory Reaction ◽  
Matrix Protein ◽  
Chondroitin Sulphate ◽  
Type Ii Collagen ◽  
Serum Levels ◽  
High Energy ◽  
Marathon Running ◽  
Type Ii ◽  
Energy Demands ◽  
And Cartilage

Objective: To determine the effect of marathon running on serum levels of inflammatory, high energy, and cartilage matrix biomarkers and to ascertain whether these biomarkers levels correlate.Design: Blood samples from 17 Caucasian male recreational athletes at the Barcelona Marathon 2017 were collected at the baseline, immediately and 48 h post-race. Serum C reactive protein (CRP), creatin kinase (CK), and lactate dehydrogenase (LDH) were determined using an AU-5800 chemistry analyser. Serum levels of hyaluronan (HA), cartilage oligomeric matrix protein (COMP), aggrecan chondroitin sulphate 846 (CS846), glycoprotein YKL-40, human procollagen II N-terminal propeptide (PIINP), human type IIA collagen N-propeptide (PIIANP), and collagen type II cleavage (C2C) were measured by sandwich enzyme-linked immune-sorbent assay (ELISA).Results: Medians CK and sLDH levels increased (three-fold, two-fold) post-race [429 (332) U/L, 323 (69) U/L] (p < 0.0001; p < 0.0001) and (six-fold, 1.2-fold) 48 h post-race [658 (1,073) U/L, 218 (45) U/L] (p < 0.0001; p < 0.0001). Medians CRP increased (ten-fold) after 48 h post-race [6.8 (4.1) mg/L] (p < 0.0001). Mean sHA levels increased (four-fold) post-race (89.54 ± 53.14 ng/ml) (p < 0.0001). Means PIINP (9.05 ± 2.15 ng/ml) levels increased post-race (10.82 ± 3.44 ng/ml) (p = 0.053) and 48 h post-race (11.00 ± 2.96 ng/ml) (p = 0.001). Mean sC2C levels (220.83 ± 39.50 ng/ml) decreased post-race (188.67 ± 38.52 ng/ml) (p = 0.002). In contrast, means COMP, sCS846, sPIIANP, and median sYKL-40 were relatively stable. We found a positive association between sCK levels with sLDH pre-race (r = 0.758, p < 0.0001), post-race (r = 0.623, p = 0.008) and 48-h post-race (r = 0.842, p < 0.0001); sHA with sCRP post-race vs. 48 h post-race (r = 0.563, p = 0.019) and sPIINP with sCK pre-race vs. 48-h post-race (r = 0.499, p = 0.044) and with sLDH 48-h pre-race vs. post-race (r = 0.610, p = 0.009) and a negative correlation of sPIIANP with sCRP 48-h post-race (r = −0.570, p = 0.017).Conclusion: Marathon running is an exercise with high-energy demands (sCK and sLDH increase) that provokes a high and durable general inflammatory reaction (sCRP increase) and an immediately post-marathon mechanism to protect inflammation and cartilage (sHA increase). Accompanied by an increase in type II collagen cartilage fibrils synthesis (sPIINP increase) and a decrease in its catabolism (sC2C decrease), without changes in non-collagenous cartilage metabolism (sCOMP, sC846, and sYKL-40). Metabolic changes on sPIINP and sHA synthesis may be related to energy consumption (sCK, sLDH) and the inflammatory reaction (sCRP) produced.

scholarly journals Kinetics of intracellular processing of chondroitin sulfate proteoglycan core protein and other matrix components.

1988 ◽  
Vol 106 (6) ◽  
pp. 2191-2202 ◽  
Author(s):  
S C Campbell ◽  
N B Schwartz
Keyword(s):  
Core Protein ◽  
Type Ii Collagen ◽  
Subcellular Fractionation ◽  
Type Ii ◽  
Link Protein ◽  
The Core ◽  
Intracellular Processing ◽  
Collagen Secretion ◽  
Golgi Region ◽  
Kinetics Of

Pulse-chase labeling techniques are used in conjunction with subcellular fractionation and quantitative immunoprecipitation to define the kinetics of intracellular translocation and secretion of proteoglycan core protein, along with link protein and type II collagen. In embryonic chick chondrocytes the core protein is processed very rapidly, exhibiting a t 1/2 in both the rough endoplasmic reticulum and golgi region of less than 10 min. Link protein appears to be processed as rapidly as the core protein, but the kinetics of type II collagen secretion is 3-4 times slower. These results are consistent with possible segregation and coordinate intracellular processing of link protein and core protein, macromolecules which are known to associate extracellularly. In contrast, rat chondrosarcoma chondrocytes translocated and secreted the core protein much more slowly (t 1/2 = 40 min) than the chick cells, perhaps due to the significantly reduced levels of galactosyltransferase I observed in the transformed chondrocytes.

scholarly journals Oligomeric forms of the 148 kDa cartilage matrix protein

1997 ◽  
Vol 328 (2) ◽  
pp. 665-668 ◽  
Author(s):  
Reema ZEINELDIN ◽  
Suzanne EKBORG ◽  
John BAKER
Keyword(s):  
Molecular Mass ◽  
Matrix Protein ◽  
Type Ii Collagen ◽  
Cartilage Matrix ◽  
Type Ii ◽  
Age Related ◽  
Sds Page ◽  
Self Association ◽  
Chromatography Step ◽  
Oligomeric Forms

The 148 kDa cartilage matrix protein (CMP), composed of three disulphide-bonded subunits, is a cartilage-specific glycoprotein found in association with fibrils of type II collagen and possibly with aggrecan. It is probable that CMP serves a structural role. As cartilage ages, an increasing proportion of the CMP becomes insoluble and resistant to extraction. In the present study, the isolation of CMP has been improved by inclusion of a hydrophobic chromatography step, thereby removing the remaining traces of collagen and proteoglycan. Evidence of self-association of CMP is presented. Higher-molecular-mass forms of CMP, ranging in apparent molecular mass from 270 to 510 kDa and separated by SDS/PAGE, were located using a specific anti-CMP monoclonal antibody. Both CMP and its oligomeric forms are reducible to 52 kDa subunits, and only trace amounts of other proteins. The formation of oligomers, which may constitute 23% of the total cartilage matrix protein, could occur as a byproduct of the normal biosynthetic trimerization of subunits. Alternatively, the oligomers may represent a step toward the age-related cross-linking and insolubilization of CMP.

scholarly journals Undenatured type II collagen mitigates inflammation and cartilage degeneration in healthy Labrador Retrievers during an exercise regimen

2021 ◽  
Author(s):  
J L Varney ◽  
J W Fowler ◽  
C N Coon
Keyword(s):  
Matrix Protein ◽  
Type Ii Collagen ◽  
Cartilage Degeneration ◽  
Mean Corpuscular Hemoglobin ◽  
Type Ii ◽  
Exercise Regimen ◽  
Collagen Group ◽  
Labrador Retrievers ◽  
And Cartilage ◽  
Undenatured Type Ii Collagen

Abstract The aim of this experiment was to evaluate the effect of undenatured type II collagen supplementation on inflammation and cartilage degeneration after exercise in healthy dogs. Forty healthy Labrador Retrievers (20 male/20 female; Range 5-12yrs; Avg 8yrs) were sorted into two groups: undenatured type II collagen group receiving 40mg UC-II (10mg Collagen Type II/Min. 3% Undenatured Type II Collagen; Lonza Consumer Health, Inc.) and placebo group receiving 40mg maltodextrin daily by capsule. After 2-weeks loading, all dogs began an 11-week endurance exercise regimen consisting of two weekly runs, starting at 5km and increasing incrementally to 8km, with one final 16km run. Blood samples were collected at baseline, pre and post first 5km run, and pre and post 16km run. Activity per kilometer was greater in male undenatured type II collagen vs male placebo over all runs (P=0.004), and average moving speed was greater in all undenatured type II collagen dogs compared with placebo over all runs (P<0.001). Hematology analysis indicated that during the first insult, undenatured type II collagen dogs had a greater lymphocyte count (P<0.001) and lymphocyte percentage (P=0.001) vs placebo dogs. Undenatured type II collagen dogs had a lesser neutrophil percentage (P=0.042) and neutrophil to lymphocyte ratios (P=0.001) compared to placebo dogs. For the final insult, undenatured type II collagen dogs had greater lymphocyte percentage (P=0.013) and lesser mean corpuscular hemoglobin concentration (P=0.043) compared with placebo dogs. Both groups had significant changes between timepoints for several hematological parameters. Biomarker IL-6 was lesser in undenatured type II collagen dogs compared with placebo at post 5km (P=0.037). Cartilage oligomeric matrix protein (COMP) was lesser in undenatured type II collagen dogs at post 16km (P=0.023), and only the placebo dogs had a significant increase in COMP from pre to post 16km (P=0.021). In summary, Labrador Retrievers supplemented with undenatured type II collagen had decreased inflammation and cartilage degeneration compared with non-supplemented dogs during exercise.

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