Oncocytoid artifact of the parotid gland: a newly reported artifact.

Electrocautery can induce significant alterations in the connective tissues and epithelium of specimens removed for diagnostic or therapeutic purposes. When electrocautery is used during parotid surgery, it can cause an oncocytoid artifact. The alterations described in this article are enlarged, tightly packed serous acinar cells with coarse to granular eosinophilic cytoplasm, distinct cell borders, and round basal nuclei that on cursory microscopic examination resemble oncocytes with respect to morphology. These changes are seen in conjunction with other, more recognized changes secondary to electrocautery and are believed to occur as a consequence of the electrothermal discharge. On the basis of our findings, this artifact is common is parotid surgical specimens and was misdiagnosed as benign oncocytic lesions in 5 cases.

Mutational analysis of the virus and monoclonal antibody binding sites in MHVR, the cellular receptor of the murine coronavirus mouse hepatitis virus strain A59.

The primary cellular receptor for mouse hepatitis virus (MHV), a murine coronavirus, is MHVR (also referred to as Bgp1a or C-CAM), a transmembrane glycoprotein with four immunoglobulin-like domains in the murine biliary glycoprotein (Bgp) subfamily of the carcinoembryonic antigen (CEA) family. Other murine glycoproteins in the Bgp subfamily, including Bgp1b and Bgp2, also can serve as MHV receptors when transfected into MHV-resistant cells. Previous studies have shown that the 108-amino-acid N-terminal domain of MHVR is essential for virus receptor activity and is the binding site for monoclonal antibody (MAb) CC1, an antireceptor MAb that blocks MHV infection in vivo and in vitro. To further elucidate the regions of MHVR required for virus receptor activity and MAb CC1 binding, we constructed chimeras between MHVR and other members of the CEA family and tested them for MHV strain A59 (MHV-A59) receptor activity and MAb CC1 binding activity. In addition, we used site-directed mutagenesis to introduce selected amino acid changes into the N-terminal domains of MHVR and these chimeras and tested the abilities of these mutant glycoproteins to bind MAb CC1 and to function as MHV receptors. Several recombinant glycoproteins exhibited virus receptor activity but did not bind MAb CC1, indicating that the virus and MAb binding sites on the N-terminal domain of MHVR are not identical. Analysis of the recombinant glycoproteins showed that a short region of MHVR, between amino acids 34 and 52, is critical for MHV-A59 receptor activity. Additional regions of the N-terminal variable domain and the constant domains, however, greatly affected receptor activity. Thus, the molecular context in which the amino acids critical for MHV-A59 receptor activity are found profoundly influences the virus receptor activity of the glycoprotein.

Estrogen and progesterone receptors in salivary gland adenoid cystic carcinoma.

Adenoid cystic carcinomas of salivary glands occur more frequently in women and bear remarkable similarity to adenoid cystic carcinomas of the breast. In addition, breast carcinomas express estrogen and progesterone receptors that impact prognostic significance. This suggests a possible role for sex steroid hormones in the development and progression of salivary gland adenoid cystic carcinoma. On this basis, 12 samples of formalin-fixed, paraffin-embedded salivary gland adenoid cystic carcinomas and 12 samples of normal salivary gland tissue were immunohistochemically evaluated for estrogen and progesterone receptor protein expression. Estrogen receptors were not detected in either group; however, a significantly higher progesterone receptor level was evident in the neoplastic group compared with normal tissue (p < 0.01). These data confirm the presence of progesterone receptors within normal and neoplastic salivary gland tissue. Progesterone receptor expression may be of possible prognostic and therapeutic value in some cases of adenoid cystic carcinoma.