scholarly journals Proteomic Analysis of Potential Keratan Sulfate, Chondroitin Sulfate A, and Hyaluronic Acid Molecular Interactions

2010 ◽  
Vol 51 (9) ◽  
pp. 4500 ◽  
Author(s):  
Abigail H. Conrad ◽  
Yuntao Zhang ◽  
Elena S. Tasheva ◽  
Gary W. Conrad
Keyword(s):  
Hyaluronic Acid ◽  
Chondroitin Sulfate ◽  
Molecular Interactions ◽  
Proteomic Analysis ◽  
Keratan Sulfate ◽  
Chondroitin Sulfate A

scholarly journals Ultrastructural cytochemistry and immunocytochemistry of proteoglycans associated with epiphyseal cartilage calcification.

1983 ◽  
Vol 31 (9) ◽  
pp. 1089-1100 ◽  
Author(s):  
M Takagi ◽  
R T Parmley ◽  
F R Denys
Keyword(s):  
Chondroitin Sulfate ◽  
Tannic Acid ◽  
Keratan Sulfate ◽  
Matrix Vesicles ◽  
Enzyme Digestion ◽  
Epiphyseal Cartilage ◽  
Fe Method ◽  
Cartilage Calcification ◽  
Testicular Hyaluronidase ◽  
Chondroitin Sulfate A

Proteoglycans (PGs) are closely associated with cartilage calcification. We have examined the hypertrophic zone of rat epiphyseal cartilage, in which calcification is occurring, using the high-iron diamine-thiocarbohydrazide-silver proteinate (HID-TCH-SP) method for sulfated glycosaminoglycans, an immunoferritin method specific for chondroitin sulfate A, and the tannic acid-ferric chloride (TA-Fe) method to stain cartilage matrix granules (MGs) presumed to be PG monomers. HID-TCH-SP produced stain deposits with a diameter of 11.2 +/- 3.2 nm (mean +/- SD; n = 200) in the MGs. However, HID-TCH-SP staining was not discernible in membrane-limited matrix vesicles (MVs). In areas of advanced calcification, partially disrupted MVs and globular bodies (GBs), derived in part from disrupted and/or degenerated MVs, contained a few too many small HID-TCH-SP stain deposits. Further down the epiphyseal cartilage, intact MVs markedly decreased and the GBs, containing many small HID-TCH-SP stain deposits, significantly increased in number. These GBs were found exclusively in the longitudinal septa rather than in the transverse septa. After enzyme digestion with testicular hyaluronidase, small (7.2 +/- 1.2 nm in diameter) stain deposits remained in the MGs and GBs, presumably localized to keratan sulfate. Immunoferritin localizing chondroitin sulfate strongly stained MGs, whereas MVs and GBs lacked staining. TA-Fe staining of glycoconjugates in the GBs demonstrated a striking decrease in the diameter of MGs associated with calcification in the GBs as compared with those in the noncalcifying area around the GBs. These results indicate that the GBs containing needle-like apatite crystals in morphologic preparations represent sites of chondroitin sulfate degradation. Testicular hyaluronidase-resistant sulfated glycosaminoglycans presumed to be keratan sulfate and partially degraded PGs selectively remain within the GBs as a probable requisite for expansion of the initial calcification in MVs.

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

SCLEREDEMA "ADULTORUMIS" IN CHILDREN

PEDIATRICS ◽  
1963 ◽  
Vol 32 (6) ◽  
pp. 1044-1054 ◽  
Author(s):  
Lawrence M. Greenberg ◽  
Charles Geppert ◽  
Howard G. Worthen ◽  
Robert A. Good
Keyword(s):  
Hyaluronic Acid ◽  
Chondroitin Sulfate ◽  
Clinical Features ◽  
High Frequency ◽  
Collagen Fibers ◽  
Scleredema Adultorum ◽  
Chondroitin Sulfate A

The literature on scleredema adultorum of Buschke "acute scleriasis" of Piffard) is reviewed, pointing out the clinical features, course, pathology, and therapy of the disease. Three cases of scleredema adultorum occurring in children are described, and the relatively high frequency of the disease in children is emphasized. Histochemical studies demonstrate a probable accumulation of a mucopolysaccharide into and between the collagen fibers of the dermis. The observations suggest that the material is either chondroitin sulfate A or hyaluronic acid. A basis for the accumulation of the increased amounts of the mucopolysaccharides is considered.

scholarly journals Inhibition of Adhesion of Plasmodium falciparum-Infected Erythrocytes by Structurally Defined Hyaluronic Acid Dodecasaccharides

2001 ◽  
Vol 69 (1) ◽  
pp. 420-425 ◽  
Author(s):  
Wengang Chai ◽  
James G. Beeson ◽  
Heide Kogelberg ◽  
Graham V. Brown ◽  
Alexander M. Lawson
Keyword(s):  
Plasmodium Falciparum ◽  
Hyaluronic Acid ◽  
Chondroitin Sulfate ◽  
Specific Interaction ◽  
Minimum Size ◽  
Dependent Manner ◽  
Compelling Evidence ◽  
Size Dependent ◽  
Maximum Inhibition ◽  
Chondroitin Sulfate A

ABSTRACT We recently reported that Plasmodium falciparum-infected erythrocytes (IRBCs) can adhere to hyaluronic acid (HA), which appears to be a receptor, in addition to chondroitin sulfate A (CSA), for parasite sequestration in the placenta. Further investigations of the nature and specificity of this interaction indicate that HA oligosaccharide fragments competitively inhibit parasite adhesion to immobilized purified HA in a size-dependent manner, with dodecasaccharides being the minimum size for maximum inhibition. Rigorously purified and structurally defined HA dodecasaccharides, free of contamination by CSA or other glycosaminoglycans, effectively inhibited IRBC adhesion to HA but not CSA, providing compelling evidence of a specific interaction between IRBCs and HA.

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.

Sign in / Sign up

Export Citation Format

Share Document