scholarly journals Extraction of cartilage protein–polysaccharides with inorganic salt solutions

1973 ◽  
Vol 131 (3) ◽  
pp. 535-540 ◽  
Author(s):  
Roger M. Mason ◽  
Robert W. Mayes

1. Bovine nasal cartilage was extracted with inorganic salt solutions of various ionic strengths. The efficiency of extraction of protein–polysaccharide from the tissue was determined for each extraction. The results confirm and enlarge earlier observations (Sajdera & Hascall, 1969). 2. The chloride salts of lanthanide metals extract high yields of protein–polysaccharide from the tissue at much lower concentrations than was achieved with univalent and bivalent salts. 3. The lanthanum salt of extracted protein–polysaccharide precipitates when the concentration of LaCl3 is decreased. Precipitation is complete in the presence of 0.05m-LaCl3. This finding is relevant to the interpretation of earlier observations on the effect of LaCl3 on elastic recovery of articular cartilage after compression (Sokoloff, 1963). 4. A linear relationship was found between the concentration at which a particular salt is maximally effective in solubilizing protein–polysaccharide from the tissue and the enthalpy of hydration of the cation of the salt. On the basis of this relationship a hypothesis is proposed to explain the characteristic protein–polysaccharide-extraction profiles exhibited by inorganic salt solutions.

1989 ◽  
Vol 54 (10) ◽  
pp. 2644-2647 ◽  
Author(s):  
Petr Schneider ◽  
Jiří Rathouský

In porous materials filled with water or water solutions of inorganic salts, water freezes at lower temperatures than under normal conditions; the reason is the decrease of water vapor tension above the convex meniscus of liquid in pores. The freezing point depression is not very significant in pores with radii from 0.05 μm to 10 μm (about 0.01-2.5 K). Only in smaller pores, especially when filled with inorganic salt solutions, this depression is important.


2002 ◽  
Vol 50 (8) ◽  
pp. 1049-1058 ◽  
Author(s):  
Andreas Naumann ◽  
James E. Dennis ◽  
Amad Awadallah ◽  
David A. Carrino ◽  
Joseph M. Mansour ◽  
...  

Cartilage is categorized into three general subgroups, hyaline, elastic, and fibrocartilage, based primarily on morphologic criteria and secondarily on collagen (Types I and II) and elastin content. To more precisely define the different cartilage subtypes, rabbit cartilage isolated from joint, nose, auricle, epiglottis, and meniscus was characterized by immunohistochemical (IHC) localization of elastin and of collagen Types I, II, V, VI, and X, by biochemical analysis of total glycosaminoglycan (GAG) content, and by biomechanical indentation assay. Toluidine blue staining and safranin-O staining were used for morphological assessment of the cartilage subtypes. IHC staining of the cartilage samples showed a characteristic pattern of staining for the collagen antibodies that varied in both location and intensity. Auricular cartilage is discriminated from other subtypes by interterritorial elastin staining and no staining for Type VI collagen. Epiglottal cartilage is characterized by positive elastin staining and intense staining for Type VI collagen. The unique pattern for nasal cartilage is intense staining for Type V collagen and collagen X, whereas articular cartilage is negative for elastin (interterritorially) and only weakly positive for collagen Types V and VI. Meniscal cartilage shows the greatest intensity of staining for Type I collagen, weak staining for collagens V and VI, and no staining with antibody to collagen Type X. Matching cartilage samples were categorized by total GAG content, which showed increasing total GAG content from elastic cartilage (auricle, epiglottis) to fibrocartilage (meniscus) to hyaline cartilage (nose, knee joint). Analysis of aggregate modulus showed nasal and auricular cartilage to have the greatest stiffness, epiglottal and meniscal tissue the lowest, and articular cartilage intermediate. This study illustrates the differences and identifies unique characteristics of the different cartilage subtypes in rabbits. The results provide a baseline of data for generating and evaluating engineered repair cartilage tissue synthesized in vitro or for post-implantation analysis.


2019 ◽  
Vol 35 (2) ◽  
pp. 141-145 ◽  
Author(s):  
Riou KAWAMURA ◽  
Momoka SATOU ◽  
Takuya YONESAKA ◽  
Akio YUCHI

2010 ◽  
Vol 69 (12) ◽  
pp. 2189-2198 ◽  
Author(s):  
Matt J Barter ◽  
Wang Hui ◽  
Rachel L Lakey ◽  
John B Catterall ◽  
Tim E Cawston ◽  
...  

ObjectiveTo investigate if statins prevent cartilage degradation and the production of collagenases and gelatinases in bovine nasal and human articular cartilage after proinflammatory cytokine stimulation.MethodsIn a cartilage degradation model, the effects of several statins were assessed by measuring proteoglycan degradation and collagen degradation, while collagenolytic and gelatinolytic activity in culture supernatants were determined by collagen bioassay and gelatin zymography. The production of matrix metalloproteinases (MMPs) in cartilage and chondrocytes were analysed by real-time reverse transcriptase PCR and immunoassay. Cytokine-induced signalling pathway activation was studied by immunoblotting.ResultsSimvastatin and mevastatin significantly inhibited interleukin 1 (IL-1)+oncostatin M (OSM)-induced collagen degradation; this was accompanied with a marked decrease in collagenase and gelatinase activity from bovine nasal cartilage. The cholesterol pathway intermediate mevalonic acid reversed the simvastatin-mediated protection of cartilage degradation, and the expression and production of collagenase (MMP-1 and MMP-13) and gelatinase (MMP-2 and MMP-9). Statins also significantly decreased MMP-1 and MMP-13 expression in human articular cartilage and chondrocytes stimulated with IL-1+OSM, and blocked the activation of critical proinflammatory signalling pathways required for MMP expression. The loss of the isoprenoid intermediate geranylgeranyl pyrophosphate due to statin treatment accounted for the inhibition of MMP expression and signalling pathway activation.ConclusionsThis study shows, for the first time, that lipophilic statins are able to block cartilage collagen breakdown induced by proinflammatory cytokines, by downregulating key cartilage-degrading enzymes. This demonstrates a possible therapeutic role for statins in acting as anti-inflammatory agents and in protecting cartilage from damage in joint diseases.


2012 ◽  
Vol 9 (2) ◽  
pp. 35-39 ◽  
Author(s):  
O Nepal ◽  
J P Rao

Background While it is well known that hypotonic solutions of sodium chloride induce hemolysis, the effects of other salt solutions on human erythrocytes have not been well documented. Objective The study is to compare the effects of other salt solutions on human red cells. Methods Iso-osmotic and hypo-osmotic solutions of various salts were prepared after taking into account their molecular weight and osmotic pressure. Five healthy volunteers between the age of 22-30 years were randomly selected and ten blood samples were collected from them. The study was conducted from January 2009 to February 2009. Blood was collected from subjects by venepuncture into heparinised tubes. 20 ?l of blood was pipetted into 1 ml of each solution and incubated for one hour at 37ºC in a water bath. The solutions were centrifuged and the colour of the supernatant was read in a spectrophotometer. Supernatant from blood added to distilled water was considered 100% hemolysed. Results Iso-osmotic salt solutions were free of hemolysis. Among chloride salts, sodium chloride showed the least hemolysis and potassium chloride and nickel chloride resulted into greater hemolysis. Among potassium salts, potassium bromate caused highest amount of hemolysis whereas potassium sulphate showed the least. Conclusion The significant differences in hemolytic pattern in hypo-osmotic salts solutions suggest that the hypo-osmotic stress causes morphological changes in red cells that alter their permeability to various ions leading to hemolysis. This probably occurs through opening of volume sensitive channels. DOI: http://dx.doi.org/10.3126/kumj.v9i2.6285Kathmandu Univ Med J 2011;9(2):35-9


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