scholarly journals CHARACTERIZATION OF THE PROTEINS OF HUMAN SYNOVIAL FLUID IN CERTAIN DISEASE STATES 1

1956 ◽  
Vol 35 (7) ◽  
pp. 814-824 ◽  
Author(s):  
K. Schmid ◽  
Margaret B. Macnair
2018 ◽  
Author(s):  
Alyssa K. Carlson ◽  
Rachel A. Rawle ◽  
Cameron W. Wallace ◽  
Ellen G. Brooks ◽  
Erik Adams ◽  
...  

AbstractObjectiveOsteoarthritis (OA) is a multifactorial disease with etiological heterogeneity. The objective of this study was to classify OA subgroups by generating metabolic phenotypes of OA from human synovial fluid.DesignPost mortemsynovial fluids (n=75) were analyzed by high performance-liquid chromatography mass spectrometry (HPLC-MS) to measure changes in the global metabolome. Comparisons of healthy (grade 0), early OA (grades I-II), and late OA (grades III-IV) donor populations were considered to reveal phenotypes throughout disease progression.ResultsGlobal metabolomic profiles in synovial fluid were distinct between healthy, early OA, and late OA donors. Pathways differentially activated among these groups included structural deterioration, glycerophospholipid metabolism, inflammation, central energy metabolism, oxidative stress, and vitamin metabolism. Within disease states (early and late OA), subgroups of donors revealed distinct phenotypes. Phenotypes of OA exhibited increased inflammation (early and late OA), oxidative stress (late OA), or structural deterioration (early and late OA) in the synovial fluid.ConclusionThese results revealed distinct metabolic phenotypes of OA in human synovial fluid, provide insight into pathogenesis, represent novel biomarkers and assist in developing personalized interventions for subgroups of OA patients.


2016 ◽  
Vol 34 (11) ◽  
pp. 1960-1968 ◽  
Author(s):  
Anne-Mari Mustonen ◽  
Petteri Nieminen ◽  
Antti Joukainen ◽  
Antti Jaroma ◽  
Tommi Kääriäinen ◽  
...  

1994 ◽  
Vol 31 (9) ◽  
pp. 257 ◽  
Author(s):  
John M. Duffy ◽  
James Grimshaw ◽  
Aine Kane ◽  
Raymond A. B. Mollan ◽  
Peter L. Spedding ◽  
...  

2010 ◽  
Vol 13 (1) ◽  
pp. 68-74 ◽  
Author(s):  
Rie KUROSE ◽  
Sadafumi ICHINOHE ◽  
Goro TAJIMA ◽  
Saburo HORIUCHI ◽  
Akira KUROSE ◽  
...  

1989 ◽  
Vol 105 (3) ◽  
pp. 395-399 ◽  
Author(s):  
Shuntaro Hara ◽  
Ichiro Kudo ◽  
Hyuen Wook Chang ◽  
Kunio Matsuta ◽  
Terumasa Miyamoto ◽  
...  

1972 ◽  
Vol 126 (5) ◽  
pp. 1073-1080 ◽  
Author(s):  
Irwin Scher ◽  
David Hamerman

1. A compound of hyaluronate and protein, called hyaluronate–protein was isolated from pooled human synovial fluids by caesium chloride density-gradient ultracentrifugation. 2. The isolated hyaluronate–protein was labelled with [125I]iodide and the following studies were done. (a) Ultracentrifugation in caesium chloride showed that the protein moiety (125I counts) and hyaluronate (hexuronate) sedimented together in the middle of the gradient. (b) The labelled hyaluronate–protein was treated with trypsin, and ultracentrifugation showed that peptide fragments (125I counts) were dispersed throughout the gradient, indicating proteolytic digestion. Hyaluronate sedimented in the middle of the gradient. (c) The labelled hyaluronate–protein was digested with streptococcal hyaluronidase, and ultracentrifugation showed that hyaluronate fragments were dispersed throughout the gradient, indicating digestion of the polysaccharide. The protein moiety, without attached hyaluronate, now sedimented at the top of the gradient. (d) Ultracentrifugation of labelled hyaluronate–protein in 4m-guanidinium chloride showed that protein and hyaluronate sedimented together. 3. These studies confirm that hyaluronate is combined with a small quantity of protein in normal human synovial fluid. A mild method for the rapid isolation of hyaluronate–protein in good yield is described.


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