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Background<br />Gastric carcinoma (GC) is the most common non-skin malignancy in Iranian men and the second leading cause of cancer-related mortality. Invasion and metastasis are considered as the major causes of cancer-related morbidity and mortality. Proteinases such as matrix metalloproteinases play an important role in tumor progression and mediating extracellular matrix remodeling. CD10 is a 90-110kd cell surface zinc-dependent metalloproteinase and there is evidence that this membrane protein may facilitate invasion and/or metastasis of tumoral cells. The objective of this study was to determine the frequency of CD10 expression in the stromal cells of GC and determine its relationship with survival and clinicopathological factors. <br /><br />Methods<br />A cross-sectional study was performed involving 50 patients with histopathologic diagnosis of GC. CD10 expression was determined by immunohistochemistry (IHC). Survival of the patients as well as the grade and stage of the tumors and demographic variables were documented. The Kaplan-Meier test was used for data analysis.<br /><br />Results<br />Stromal CD10 was detected in 46% of the GC stromal cells. No immunoreactivity was identified in the stromal cells of normal adjacent tissue. Stromal CD10 expression in gastric carcinoma did not correlate with the age and gender of the cases as well as the size and location of the tumor, and lymph node involvement but correlated with tumor stage (p=0.01), tumor grade(p=0.01) and patients’ survival (p=0.02). <br /><br />Conclusion<br />Stromal CD10 expression is correlated with tumor differentiation, clinical stage and survival in GC. CD10 expression could be considered as a negative prognostic factor for gastric carcinoma.

Background & objective: The histologic distinction of small cell from non-small cell lung carcinoma and correct identification of all subtype s of lung carcinoma are very important in treatment management. The main method for histologic classification of lung tumors is based on morphology. However, in small bronchoscopic biopsies in particular, distinction is very difficult upon morphology alone. The current study aimed at evaluating the utility of a panel of antibodies, consisting of thyroid transcription factor (TTF-1), P63, high molecular weight keratin [HMWK (34βE12)], cytokeratin (CK7), and cluster of differentiation (CD56) for accurate distinction of bronchogenic carcinomas. Methods: Bronchoscopic biopsies of 60 lung carcinoma cases including 20 small cell carcinomas, 20 adenocarcinomas, and 20 squamous cell carcinomas (SCCs) with typical morphologic features were selected. All these cases were immunohistochemically stained for TTF-1, P63, HMWK (34βE12), CK7, and CD56. All immunostained slides were scored as either positive or negative. Results: The mean age of the patients was 60 years; ranged from 35 to 81. Sixteen patients were female and 44 were male. All adenocarcinomas were positive for CK7 and most of them (18/20; 90%) were positive for TTF-1. Most of small cell lung carcinomas were positive for TTF-1 (17/20; 85%), and CD56 (18/20; 90%). All squamous cell carcinomas (SCCs) were negative for TTF-1, but most of them were positive for HMWK (34βE12) and P63. Conclusion: The obtained data showed that TTF-1, P63, CK7, CD56 and/or 34βE12 represent a useful panel of antibodies to identify lung carcinoma subtypes in small bronchoscopic biopsies.

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Background: Human Epidermal Growth factor Receptor 2 (HER2), also known as ErbB2 is a 185 kDa protein belonging to the Human Epidermal Receptor (HER) family of tyrosine kinase receptors overexpressed in 20% -30% of patients with breast cancer. Similar to other members of the HER family, HER2 glycoprotein comprises of multiple domains including an extracellular ligand-binding domain, a single transmembrane domain and a cytoplasmic domain with tyrosine kinase activity. The extracellular domain of HER2 with 632 amino acids is composed of four subdomains (I -IV); subdomains I and III form a ligand binding site, and cysteine-rich subdomains II and IV play an important role in dimerization of the receptor. Objectives: In this study we aimed to produce murine Monoclonal Antibodies (MAbs) with the ability of specific recognition of the HER2 dimerization arm. Materials and Methods: Primarily, BALB/c mice were immunized with a 30-aminoacid peptide as a part of the human HER2 subdomain II. Splenocytes from hyperimmunized mice were fused with myeloma cells (SP2/0), selected in hypoxanthine-aminopterin-thymidine (HAT) medium, and screened by indirect Enzyme-Linked Immunosorbent Assay (ELISA). Secreted MAbs were characterized according to isotypes, reactions with the native HER2 in SKBR3 cells by western blotting, and in tissue sections from HER2 positive breast cancer specimens by Immunohistochemistry (IHC). Results: Isotype of 1F1 clone was determined to be IgG1, which reacted with native protein in the western blot experiment and stained 20% of the membrane of neoplastic cells overexpressing HER2 with 3+ grade. However, 3L5 clone showed a low reaction (10%) with native HER2 in immunohistochemistry. Conclusions:The results of both western blotting and Immunohistochemistry showed that native HER2 can be detected with 1F1 monoclonal antibody.