Your browser doesn't support javascript.
loading
Show: 20 | 50 | 100
Results 1 - 4 de 4
Filter
Add more filters










Database
Publication year range
1.
Scand J Med Sci Sports ; 23(1): 15-22, 2013 Feb.
Article in English | MEDLINE | ID: mdl-22288718

ABSTRACT

The life situation of many patients changes after an anterior cruciate ligament (ACL) rupture and subsequent reconstruction, and this may affect their health-related quality of life in many ways. It is well known that the overall clinical results after ACL reconstruction are considered good, but pre-operative predictive factors for a good post-operative clinical outcome after ACL reconstruction have not been studied in as much detail. The purpose of this study was to identify pre-operative factors that predict a good post-operative outcome as measured by the Short Form 36 (SF-36) and Knee Osteoarthritis Outcome Score (KOOS) 3-6 years after ACL reconstruction. Seventy-three patients scheduled for ACL reconstruction were clinically examined pre-operatively. The SF-36 and KOOS questionnaires were sent by mail to these patients 3-6 years after reconstruction. Predictive factors for health-related quality of life were investigated using a stepwise regression analysis. In conclusion, pre-operative factors, such as pivot shift, knee function, and range of motion, may predict a good post-operative outcome and explain up to 25% in terms of health-related quality of life after ACL reconstruction. Furthermore, it appears that the patients' pre-injury and pre-operative Tegner activity levels are important predictors of post-operative health-related quality of life.


Subject(s)
Anterior Cruciate Ligament Reconstruction/rehabilitation , Quality of Life , Range of Motion, Articular/physiology , Recovery of Function/physiology , Adolescent , Adult , Anterior Cruciate Ligament Reconstruction/methods , Female , Humans , Knee Joint/physiology , Male , Motor Activity/physiology , Multivariate Analysis , Pain Measurement , Preoperative Period , Prognosis , Regression Analysis , Sickness Impact Profile , Young Adult
2.
J Biol Chem ; 266(23): 14869-72, 1991 Aug 15.
Article in English | MEDLINE | ID: mdl-1714447

ABSTRACT

The specificity of endothelial cell leukocyte adhesion molecule-1, ELAM-1, for binding to a panel of carbohydrate structures was determined by a sensitive cell binding assay with immobilized synthetic glycoconjugates. ELAM-1 cDNA transfectants were found to bind Sialyl Lea (sialylated lacto-N-fucopentaose II) or sialylated Lewis a antigen (NeuAc alpha 2-3Gal beta 1-3(Fuc alpha 1-4)GlcNAc), as well as or slightly better than Sialyl Lex (sialylated lacto-N-fucopentaose III) or sialylated Lewis X antigen (NeuAc alpha 2-3 Gal beta 1-4(Fuc alpha 1-3)GlcNAc). A monoclonal antibody, HECA-452, which has been identified recently as recognizing ELAM-1 ligands in addition to those containing Sialyl Lex, was also found to bind both Sialyl Lex and Sialyl Lea. Hard sphere exo-anomeric (HSEA) calculations were performed on these two hexasaccharides. The conformations indicate that Sialyl Lea and Sialyl Lex show a high degree of similarity in both the nonreducing and reducing termini. As Lea and Lex show much weaker reactivity, the determinants recognized by ELAM-1 and HECA-452 probably involve neuraminic acid and fucose residues which on one face of both Sialyl Lex and Sialyl Lea can be similarly positioned. The finding that Sialyl Lea is a potent ligand for ELAM-1 is important, as circulating Sialyl Lea and Sialyl Lex containing mucins which are elevated in the serum of many cancer patients may block leukocyte interactions with ELAM-1 and may contribute to the pathological immunodepression observed in these patients.


Subject(s)
Carbohydrate Metabolism , Cell Adhesion Molecules/metabolism , Lewis X Antigen/metabolism , Membrane Glycoproteins/metabolism , Oligosaccharides/metabolism , Animals , Antigens, Neoplasm/immunology , Antigens, Neoplasm/metabolism , Binding Sites , Binding, Competitive , Carbohydrate Sequence , Cell Line , DNA/genetics , E-Selectin , Lewis X Antigen/immunology , Mice , Molecular Sequence Data , Oligosaccharides/immunology , Transfection
3.
Arch Biochem Biophys ; 269(2): 678-89, 1989 Mar.
Article in English | MEDLINE | ID: mdl-2919890

ABSTRACT

Complete structures are described for three urinary oligodextrins from one patient with type II and one patient with type III glycogen storage disease. GLC-MS, direct probe MS, and 1H NMR demonstrate two heptasaccharides and one hexasaccharide containing only alpha 1-4 and alpha 1-6 linkages. The observation that all three oligosaccharides were present in urine of both patients and the occurrence of alpha 1-4 and alpha 1-6 linkages in characteristic sequences indicates that the oligodextrins are limit dextrins derived from alpha-amylolytic degradation of glycogen. The binding affinities of the oligodextrins for a monoclonal antibody (401/6) raised against Glc alpha 1-6Glc alpha 1-4Glc alpha 1-4Glc, were determined by frontal analysis. The highest affinity was exhibited by Glc alpha 1-6Glc alpha 1-4Glc alpha 1-4Glc followed by the two heptasaccharides and the hexasaccharide. The results from quantitative affinity measurements agree with results of structural analysis by physical methods in that all oligodextrins containing the nonreducing terminal sequence, Glc alpha 1-6Glc alpha 1-4Glc . . . , are specifically bound by the antibody with similar affinities, but the affinity is somewhat higher for chains containing the tetrasaccharide sequence Glc alpha 1-6Glc alpha 1-4Glc alpha 1-4Glc at the nonreducing terminal. Utilization of affinity methods offers clear advantages for isolation and characterization of oligosaccharides with very similar structures.


Subject(s)
Dextrins/urine , Oligosaccharides/urine , Starch/urine , Antibodies, Monoclonal , Carbohydrate Conformation , Carbohydrate Sequence , Chromatography, Affinity/methods , Dextrins/immunology , Dextrins/isolation & purification , Gas Chromatography-Mass Spectrometry , Glycogen Storage Disease Type II/urine , Humans , Magnetic Resonance Spectroscopy , Methylation , Models, Molecular , Oligosaccharides/immunology , Oligosaccharides/isolation & purification
SELECTION OF CITATIONS
SEARCH DETAIL
...