The imaging findings in squamous cell carcinoma (SCC) of the oral cavity and oropharynx vary widely, depending on the site of origin of the primary tumor and the extent of its involvement of other regions. Knowledge of the complex anatomy of the oral cavity and oropharynx, as well as the most common routes by which SCC spreads from various anatomic sites, allows the radiologist to accurately determine the extent of disease and help clinicians plan appropriate treatment. SCCs that originate in the oral cavity tend to behave differently than those that originate in the oropharynx, with the latter group exhibiting more aggressive growth. Furthermore, primary tumors in certain anatomic subsites within the oral cavity or oropharynx have a greater propensity to spread by direct extension along muscle, bone, or neurovascular bundles or to be disseminated along lymphatic drainage pathways to regional or distant nodes. Imaging findings of deep muscular, neurovascular, osseous, or nodal involvement are indicative of an advanced stage of disease for which management options are limited.

The molecular chaperone heat shock protein 90 (Hsp90) serves essential roles in the regulation of signaling protein function, trafficking, and turnover. Hsp90 function is intimately linked to intrinsic ATP binding and hydrolysis activities, the latter of which is under the regulatory control of accessory factors. Glucose-regulated protein of 94 kDa (GRP94), the endoplasmic reticulum Hsp90, is highly homologous to cytosolic Hsp90. However, neither accessory factors nor adenosine nucleotides have been clearly implicated in the regulation of GRP94-client protein interactions. In the current study, the structural and regulatory consequences of adenosine nucleotide binding to GRP94 were investigated. We report that apo-GRP94 undergoes a time- and temperature-dependent tertiary conformational change that exposes a site(s) of protein-protein interaction; ATP, ADP, and radicicol markedly suppress this conformational change. In concert with these findings, ATP and ADP act identically to suppress GRP94 homooligomerization, as well as both local and global conformational activity. To identify a role(s) for ATP or ADP in the regulation of GRP94-client protein interactions, immunoglobulin (Ig) heavy chain folding intermediates containing bound GRP94 and immunoglobulin binding protein (BiP) were isolated from myeloma cells, and the effects of adenosine nucleotides on chaperone-Ig heavy chain interactions were examined. Whereas ATP elicited efficient release of BiP from both wild-type and mutant Ig heavy chain intermediates, GRP94 remained in stable association with Ig heavy chains in the presence of ATP or ADP. On the basis of these data, we propose that structural maturation of the client protein substrate, rather than ATP binding or hydrolysis, serves as the primary signal for dissociation of GRP94-client protein complexes.

Osteosarcoma is the classic malignant osteoid-forming bone tumor. The typical clinical presentation, histology, imaging findings, treatment, and prognosis for each subtype of osteosarcoma is provided. Particular emphasis is placed on more current magnetic resonance imaging and nuclear medicine imaging techniques that may soon improve the ability to determine the most appropriate therapy and ultimately improve patient survival.