Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UMLS:C0268596 (EMA)
 2,520 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

This study was devoted to a peculiar population of argyrophilic cells present among various stratified squamous epithelia. The purpose of the study was to determine the distribution and the nature of these argyrophilic cells, and to reappraise their degree of analogy with the Merkel cells of epidermis. Examples of squamous epithelia from skin, exocervix, anal canal and dermoid cyst of ovary were investigated using histochemical, immunohistochemical and ultrastructural techniques. Melanin-containing cells as well as peculiar argyrophilic cells were revealed in each series of specimens. These peculiar argyrophilic cells expressed EMA, chromogranin A and NCL-5D3 (cytokeratins 19, 18, 8) immunoreactivities. By contrast, they were serotonin negative. An intense staining for EMA was observed. These cells were obviously endocrine cells. Ultrastructural studies confirmed the presence of endocrine cells within the anal canal and the exocervix; moreover, in anal canal, some of these cells appeared to have contacts with a nerve terminal. Through the epidermis, these cells can only correspond to Merkel cells, because of their chromogranin positivity. Throughout other squamous epithelia, this population of endocrine cells (serotonin negative) bear some analogies with Merkel cells of epidermis. Their distribution, morphology, EMA immunoreactivity and ultrastructural appearance were reminiscent of those of the Merkel cells. They could be named Merkel-type cells. Additional studies, using other characteristic or specific markers of Merkel cells, are clearly required to determine the exact degree of analogy between these types of cells. Merkel-type cells could be largely distributed through stratified squamous epithelia from various tissues. They can be easily visualized by their strong EMA immunoreactivity and must be distinguished from Paget cells.
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PMID:[Endocrine cells and Malpighian epithelium. Merkel-type cells? Immunohistochemical and ultrastructural study]. 208 58

In the study below we introduced certain conclusions from bone marrow analysis in patient with ovarian cancer in the presence of epithelial cells. The study included cytological bone marrow slides taken from 31 patients. We analyzed the cellular antigen expression using immuno-histological chemistry technic with NCL-CA 125, NCL-EMA and NCL-C11 antibodies. In the material drived from 3 patients with advanced neoplastic changes, we detected the presence of cells that were stained positively. In order to define the actual frequency of cell presence with tested antigen expression in bone marrow as well as to signify the diagnostic and prognostic value of their detection requires a larger study group as well as using other examination technics such as PCR or transluscent photometry.
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PMID:[Bone marrow involvement in ovarian cancer by immunohistochemical assessment]. 1073 59

MUC1 glycoprotein that is overexpressed in aberrant forms in epithelial cancers has been used for diagnosis, staging and therapy. As normal prostate and prostate cancer tissues express MUC1, it represents a potential target, but MUC1 epitopes specific to prostate cancer have not been well characterized. In order to assess MUC1 epitopes in prostate cancer, and their correlation with Gleason grades, binding of 7 well-characterized anti-MUC1 monoclonal antibodies (MAbs) (BrE-3, SM3, BC2, EMA, B27.29, HMFG-1 and NCL MUC1 core), were studied on a prostate tissue microarray. This microarray contained 197 prostate tissue cores representing: i) normal/benign prostate; ii) prostatic intraepithelial neoplasia and Gleason grades 1 and 2; and iii) Gleason grades 3-5. These MAbs bind the MUC1 extracellular domain, but have variable sensitivity to MUC1 glycosylation. To further characterize the effect of glycosylation on their binding, MAb reactivities with unglycosylated MUC1 core peptide and breast and prostate cancer cell lysates were compared. These studies demonstrated strong binding of BrE-3, BC2 and EMA to the peptide core and recognition by BrE-3, SM3, BC2 and EMA of hypoglycosylated MUC1. The results for the microarray indicated that higher Gleason grades were associated with markedly increased cellular staining by MAbs that preferentially recognize less glycosylated MUC1 (BrE-3, p<0.001; SM3, p<0.004; EMA, p=0.009; and BC2, p<0.001). Staining by MAbs that bind preferentially to hyperglycosylated MUC1 (B27.29, p=0.33; HMFG-1, p=0.89; and NCL MUC1 core, p=0.96) did not correlate with Gleason grade. These results demonstrated that hypoglycosylated MUC1 expression increased with Gleason grade, thus supporting the targeting of hypoglycosylated MUC1 epitopes in prostate cancer for more specific imaging and therapy applications.
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PMID:Characterization of MUC1 glycoprotein on prostate cancer for selection of targeting molecules. 1677 84