Discrimination of squamous cell carcinoma in situ from seborrheic keratosis by color analysis techniques requires information from scale, scale-crust and surrounding areas in dermoscopy images.

Scale-crust, also termed "keratin crust", appears as yellowish-to-tan scale on the skin's surface. It is caused by hyperkeratosis and parakeratosis in inflamed areas of squamous cell carcinoma in situ (SCCIS, Bowen's disease) and is a critical dermoscopy feature for detecting this skin cancer. In contrast, scale appears as a white-to-ivory detaching layer of the skin, without crust, and is most commonly seen in benign lesions such as seborrheic keratoses (SK). Distinguishing scale-crust from ordinary scale in digital dermoscopy images holds promise for early SCCIS detection and differentiation from SK. Reported here are image analysis techniques that best characterize scale-crust in SCCIS and scale in SK, thereby allowing accurate separation of these two dermoscopic features. Classification using a logistic regression operating on color features extracted from these digital dermoscopy structures can reliably separate SCCIS from SK.

Buffers differentially alter the binding of [3H]rauwolscine and [3H]RX821002 to the alpha-2 adrenergic receptor subtypes.

3H-antagonists are known to bind to the alpha-2A adrenergic receptor with higher affinity in glycylglycine buffer than in Tris buffer. The purpose of this study was to examine the effect of buffers on the binding of antagonists to all four subtypes of the alpha-2 adrenergic receptor. Our approach was to examine the effects of glycylglycine, Tris, sodium phosphate (NaPO4) and potassium phosphate buffers on the binding of [3H]rauwolscine, [3H]RX821002, prazosin and oxymetazoline. We found that the affinities for the different subtypes varied with the buffer and the ligands used. Although the Bmax values varied somewhat with the buffers, they were similar for both radioligands for a specific subtype. The highest affinities and Bmax values for both radioligands were generally obtained with NaPO4 buffer. The affinities of antagonists in Tris buffer were always significantly lower than in either NaPO4 or glycylglycine buffer, and the affinities decreased as the concentration of Tris increased. In contrast, the affinity of norepinephrine for the alpha-2B subtype was higher in Tris than in NaPO4 buffer. The buffer effects did not appear to be dependent on the cell membrane composition. There appeared to be some species differences in the effects of buffers on the alpha-2C subtype. These results indicate that buffers affect the binding of antagonists to alpha-2 adrenergic receptors, that not all subtypes are altered in the same manner and that buffers alter the binding of different antagonists differently. It is generally recommended that NaPO4 buffer be used, and that Tris be avoided, when measuring the binding of antagonists to the alpha-2 adrenergic receptor.