Growth dependent changes in the chemical composition of proximal tibial articular cartilage and growth plate of broiler chickens

1995 ◽  
Vol 75 (3) ◽  
pp. 433-437 ◽  
Author(s):  
T. Nakano ◽  
J. S. Sim
Keyword(s):  
Hyaluronic Acid ◽  
Articular Cartilage ◽  
Sialic Acid ◽  
Chondroitin Sulfate ◽  
Growth Plate ◽  
Broiler Chickens ◽  
Dry Matter ◽  
Broiler Chicken ◽  
Age Groups ◽  
Keratan Sulfate

Chemical composition of the proximal tibial articular cartilage and growth plate of broiler chickens from seven age groups (1, 8, 14, 22, 29, 36, and 43 d old) was studied. In the articular cartilage, the contents of dry matter, collagen measured as hydroxyproline, and keratan sulfate increased (P < 0.05), and the content of sialic acid decreased (P < 0.05) as age advanced. The content of chondroitin sulfate measured as uronic acid and the proportion of hyaluronic acid in total glycosaminoglycan (GAG) were relatively constant (P > 0.05) among the age groups. In the growth plate, the contents of chondroitin sulfate and keratan sulfate increased (P < 0.05) with age, while the contents of dry matter, sialic acid, and collagen were similar among the age groups. The proportion of hyaluronic acid in total GAG decreased at the age of 8 d, and remained relatively constant thereafter. The growth dependent changes observed in the concentration of chondroitin sulfate in the broiler chicken cartilage were different from those in other species which have been reported to show a decrease during early postnatal growth. Key words: Tibia, epiphyseal cartilage, growth plate, broiler chicken, age

CHANGES IN SWINE KNEE ARTICULAR CARTILAGE DURING GROWTH

1979 ◽  
Vol 59 (1) ◽  
pp. 167-179 ◽  
Author(s):  
T. NAKANO ◽  
F. X. AHERNE ◽  
J. R. THOMPSON
Keyword(s):  
Hyaluronic Acid ◽  
Articular Cartilage ◽  
Dry Matter ◽  
Endochondral Ossification ◽  
Keratan Sulfate ◽  
Cartilage Thickness ◽  
Cell Necrosis ◽  
Normal Cartilage ◽  
Age Related ◽  
Age Related Changes

Twenty-five crossbred boars reared under normal conditions were serially slaughtered at the age of 3 days, and 5, 10, 20 and 30 wk. Five boars were slaughtered at each age and morphological, histochemical and biochemical age-related changes in femoral condylar articular cartilage were studied. No osteochondrotic joints were found in pigs 10 wk of age or younger, while 7 of the 10 boars slaughtered at 20 and 30 wk of age were osteochondrotic. Cartilage thickness increased (P < 0.05) until the age of 5 wk and decreased (P < 0.05) thereafter. Cell density decreased (P < 0.05) as age advanced. Age-associated changes found in the chemical composition of the cartilage were an increase in the concentration of dry matter and hydroxyproline and a decrease in the concentration of glycosaminoglycans (GAG) including chondroitin sulfate (ChS), keratan sulfate and hyaluronic acid. The proportions of soluble proteoglycan and 4-sulfated disaccharide from the ChS fraction decreased (P < 0.05) while the proportion of 6-sulfated disaccharide from ChS increased (P < 0.05). Osteochondrosis was observed as a disturbed endochondral ossification, and softening and fracture of the cartilage. The former was accompanied by a loss of intercellular GAG and cell necrosis, and the latter by local losses of GAG and cells. Osteochondrotic cartilage also contained higher proportions of soluble proteoglycan and 6-sulfated disaccharide, and lower proportions of 4-sulfated disaccharide than did the visually normal cartilage.

scholarly journals Intra- and extracellular localization of hyaluronic acid and proteoglycan constituents (chondroitin sulfate, keratan sulfate, and protein core) in articular cartilage of rabbit tibia.

1992 ◽  
Vol 40 (11) ◽  
pp. 1693-1704 ◽  
Author(s):  
A Asari ◽  
S Miyauchi ◽  
K Miyazaki ◽  
A Hamai ◽  
K Horie ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Hyaluronic Acid ◽  
Articular Cartilage ◽  
Chondroitin Sulfate ◽  
Keratan Sulfate ◽  
Positive Staining ◽  
Chondroitinase Abc ◽  
Protein Core ◽  
Rabbit Tibia ◽  
Pre Treatment

To demonstrate the intra- and extracellular localization of hyaluronic acid (HA) in articular cartilage of the rabbit tibia, biotinylated HA binding region, which specifically binds to the HA molecule, was applied to the tissue. In comparison with the localization of HA, that of chondroitin sulfate (CS), keratan sulfate (KS), and the protein core (PC) of the proteoglycan was examined by immunohistochemistry. Strong positive staining for HA was detected in chondrocytes located in the transition between the superficial and middle zones of the tissue. Pre-treatment with chondroitinase ABC, keratanase II, or trypsin enhanced the stainability for HA in peri- and intercellular matrices. Immunohistochemistry with or without enzymatic pre-treatment demonstrated that immunoreactivity for CS, KS, and PC was distinctly discerned in chondrocytes and in the extracellular matrix located in the middle and deep zones. In particular, the immunoreactivity for KS and PC was augmented by pre-treatment with chondroitinase ABC not only in chondrocytes but in the extracellular matrix located in the middle and deep zones. Microbiochemical analysis corresponded well with histochemical and immunohistochemical results. These results suggest that HA is abundantly synthesized and secreted in chondrocytes located in the transition between the superficial and middle zones.

scholarly journals Age-related changes in the composition and structure of human articular-cartilage proteoglycans

1978 ◽  
Vol 176 (3) ◽  
pp. 683-693 ◽  
Author(s):  
M T Bayliss ◽  
S Y Ali
Keyword(s):  
Hyaluronic Acid ◽  
Articular Cartilage ◽  
Age Groups ◽  
Human Articular Cartilage ◽  
Human Cartilage ◽  
Keratan Sulphate ◽  
Age Related ◽  
Composition And Structure ◽  
Normal Human ◽  
Cartilage Proteoglycans

1. Analysis of the purified proteoglycans extracted from normal human articular cartilage with 4M-guanidinium chloride showed that there was an age-related increase in their content of protein and keratan sulphate. 2. The hydrodynamic size of the dissociated proteoglycans also decreased with advancing age, but there was little change in the proportion that could aggregate. 3. Results suggested that some extracts of aged-human cartilage had an increased content of hyaluronic acid compared with specimens from younger patients. 4. Dissociated proteoglycans, from cartilage of all age groups, bind to hyaluronic acid and form aggregates in direct proportion to the hyaluronic acid concentration. 5. Electrophoretic heterogeneity of the dissociated proteoglycans was demonstrated on polyacrylamide/agarose gels. The number of proteoglycan species observed was also dependent on the age of the patient.

Theory of the Short Time Mechanical Relaxation in Articular Cartilage

2011 ◽  
Vol 133 (10) ◽  
Author(s):  
J. W. Ruberti ◽  
J. B. Sokoloff
Keyword(s):  
Hyaluronic Acid ◽  
Articular Cartilage ◽  
Chondroitin Sulfate ◽  
Relaxation Times ◽  
Type Ii Collagen ◽  
Mechanical Relaxation ◽  
Side Chains ◽  
Type Ii ◽  
Interface Area ◽  
Short Time

Articular cartilage is comprised of macromolecules, proteoglycans, with (charged) chondroitin sulfate side-chains attached to them. The proteoglycans are attached to longer hyaluronic acid chains, trapped within a network of type II collagen fibrils. As a consequence of their relatively long persistence lengths, the number of persistence lengths along the chondroitin sulfate and proteoglycan chains is relatively small, and consequently, the retraction times for these side chains are also quite short. We argue that, as a consequence of this, they will not significantly inhibit the reptation of the hyaluronic acid chains. Scaling arguments applied to this model allow us to show that the shortest of the mechanical relaxation times of cartilage, that have been determined by Fyhrie and Barone to be due to reptation of the hyaluronic acid polymers, should have a dependence on the load, i.e., force per unit interface area P, carried by the cartilage, proportional to P3/2.

scholarly journals Localization of hyaluronic acid in human articular cartilage.

1994 ◽  
Vol 42 (4) ◽  
pp. 513-522 ◽  
Author(s):  
A Asari ◽  
S Miyauchi ◽  
S Kuriyama ◽  
A Machida ◽  
K Kohno ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Hyaluronic Acid ◽  
Articular Cartilage ◽  
Dermatan Sulfate ◽  
Keratan Sulfate ◽  
Human Articular Cartilage ◽  
Middle Zone ◽  
Deep Zone ◽  
Weak Staining ◽  
Pre Treatment

To demonstrate localization of hyaluronic acid (HA) in articular cartilage of the human femur, biotinylated HA-binding region, which specifically binds HA molecules, was applied to the tissue. In sections fixed by 2% paraformaldehyde-2% glutaraldehyde, HA staining was detected in lamina splendens and chondrocytes in the middle zone. By pretreatment with trypsin, intense HA staining appeared in the extracellular matrix of the deep zone and weak staining in the superficial and middle zones. Moreover, pre-treatment with chondroitinase ABC (CHase ABC) intensely enhanced the stainability for HA in the superficial and middle zones and weakly in the deeper zone. Combined pre-treatment of trypsin with CHase ABC abolished intra- and extracellular staining for HA in all zones. By microbiochemical study, the concentrations of HA and dermatan sulfate were high in the middle zone, whereas those of chondroitin sulfate and keratan sulfate were high in the deep zone. These results suggest that HA is abundantly synthesized in and secreted from the chondrocytes, particularly in the middle zone, whereas it is largely masked by proteoglycan constituents in the extracellular matrix.

Polysaccharide composition of Australian wheats and the digestibility of their starches in broiler chicken diets

1990 ◽  
Vol 30 (2) ◽  
pp. 183 ◽  
Author(s):  
G Annison
Keyword(s):  
Broiler Chickens ◽  
Dry Matter ◽  
Broiler Chicken ◽  
New South ◽  
Starch Digestibility ◽  
Wheat Varieties ◽  
South Wales ◽  
Wheat Starches ◽  
Polysaccharide Composition ◽  
Matter Basis

The polysaccharide compositions of 20 wheat varieties from New South Wales and Western Australia were determined. Mean pentosan and �-glucan contents ranged from 5.7 1 to 8.18% and from 0.61 to 0.87% respectively, on a dry matter basis. Starch contents ranged from 61.5 to 68.9% and the wheat starches were between 21.1 and 31.8% amylose. The starch digestibility of the wheats was found to be independent of the levels or composition of the polysaccharides when assayed using 5-week-old broiler chickens.

scholarly journals KECERNAAN BAHAN KERING DAN BAHAN ORGANIK KULIT PISANG RAJA TERFERMENTASI DENGAN Rhizopus oligosporus DALAM RANSUM AYAM BROILER

ZOOTEC ◽  
2019 ◽  
Vol 40 (1) ◽  
pp. 134
Author(s):  
Nabenus Wenda ◽  
F.R Wolayan ◽  
I.M. Untu ◽  
H. Liwe
Keyword(s):  
Organic Matter ◽  
Broiler Chickens ◽  
Dry Matter ◽  
Broiler Chicken ◽  
Test Results ◽  
Rhizopus Oligosporus ◽  
Fermented Product ◽  
Banana Flour ◽  
Average Body ◽  
Average Body Weight

DIGESTIBILITY OF DRY MATTER AND ORGANIC MATTER OF RAJA BANANA PEELS WITH Rhizopus oligosporus FERMENTED IN BROILER RATION. This study aims to determine the digestibility of dry matter and organic material rations using the peels of banana Raja fermented with Rhizopus oligosporus in broiler chickens. This research was conducted using 20 broilers of Arbor Acres CP. 707 Strain aged 5 weeks, with an average body weight of ± 1067 grams. The design used was: Student t-test consisting of 2 treatments, each treatment consisted of 10 broilers as a test. The rations used in this study were: Raja Banana peels flour without fermentation and fermented products with Rhizopus oligosporus mold. The t-student test results showed that the digestibility of dry banana skin powder of fermented Raja banana product was significantly different (P<0.01) compared to unripe fermented Raja banana flour which was 62.32% to 71.66% as well as the digestibility of organic matter ie from 66.74% to 73.01%. Based on the results and discussion it can be concluded that the use of raja banana skin peel flour 15% fermented product in the ration gives betterresults to the digestibility of dry matter and organic matter compared to without fermentation. Keywords: Raja Banana Peels, Fermentation, Rhizopus oligosporus, Broiler Chicken.

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