ABSTRACT
BACKGROUND: A distal tibia osteochondral allograft is a potential graft option for glenoid reconstruction because the distal tibia may have a similar radius of curvature (ROC) as the glenoid. This study evaluated ROC mismatch as measured on computed tomography (CT) scans between the glenoid, distal tibia, and humeral head. METHODS: Bilateral CT images were formatted for 10 decedents from the Office of the Medical Investigator database, giving 20 specimens per anatomic location. The ROCs of the glenoid, distal tibia, and humeral head were measured. A statistical model was generated to assess ROC mismatch of randomly paired distal tibias and glenoids. RESULTS: The mean ± standard deviation ROC was 2.9 ± 0.25 cm for the glenoid, 2.3 ± 0.21 cm for the distal tibia, and 2.5 ± 0.12 cm for the humeral head. No differences were found in laterality, intraobserver, or interobserver measurements. The least-squares difference in the ROC between the glenoid and tibia was 0.57 cm, glenoid and humerus was 0.40 cm, and humerus and tibia was 0.17 cm. Only 22% of randomly paired distal tibias and glenoids had a difference in ROC of 0.3 cm or less. CONCLUSION: CT measurement of the ROC of the glenoid, distal tibia, and humeral head is reliable and reproducible. The probability of obtaining a random distal tibia allograft with a similar ROC to the glenoid is low. Obtaining ROC measurements of the injured glenoid and the distal tibia allograft specimen before use for glenoid reconstruction may be useful.
Subject(s)
Humeral Head/diagnostic imaging , Shoulder Joint/diagnostic imaging , Tibia/diagnostic imaging , Adult , Female , Humans , Humeral Head/anatomy & histology , Least-Squares Analysis , Male , Middle Aged , Reproducibility of Results , Retrospective Studies , Tibia/anatomy & histology , Tomography, X-Ray Computed , Young AdultABSTRACT
Lectins are invaluable tools for chemical biology because they recognize carbohydrate arrays. Multivalent carbohydrate binding by lectins is important for processes such as bacterial and viral adhesion and cancer metastasis. A better understanding of mammalian lectin binding to carbohydrate arrays is critical for controlling these and other cellular recognition processes. Plant lectins are excellent model systems for the study of multivalent protein-carbohydrate interactions because of their robustness and ready availability. Here, we describe binding studies of mannose-functionalized poly(amidoamine) (PAMAM) dendrimers to a mitogenic lectin from Pisum sativum (pea lectin). Hemagglutination and precipitation assays were performed, and results were compared to those obtained from concanavalin A (Con A), a lectin that has been studied in more detail. Isothermal titration calorimetry (ITC) experiments are also described.
Subject(s)
Mannose/chemistry , Pisum sativum/chemistry , Plant Lectins/chemistry , Plant Lectins/chemical synthesis , Bacterial Adhesion , Binding Sites , Calorimetry , Concanavalin A/chemistry , Dendrimers , Hemagglutination Tests , Models, Biological , Models, Molecular , Polyamines/chemistry , Protein Conformation , Structure-Activity RelationshipABSTRACT
Manalpha1-2Man functionalized G(3) and G(4)-PAMAM dendrimers have been synthesized and characterized by MALDI-TOF MS and NMR spectroscopy. Precipitation assays to assess the binding of the dimannose-functionalized dendrimers to Cyanovirin-N, a HIV-inactivating protein that blocks virus-to-cell fusion through high mannose mediated interactions, are presented.
