Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0598934 (tumor growth)
 58,965 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Myoepithelial cells (MC) were identified and the pattern of their distribution in dysplasia and duct carcinoma of the mammary gland was studied using a monospecific antiserum to smooth-muscle myosin of the human uterus, by the indirect Coons' method under luminescent microscope. Samples of the operation material from 10 patients with fibrous-cystic mastopathy and 26 patients with duct carcinoma were examined. In solid (7 observations) and comedo (4 observations) carcinomas with the structure of cancer in situ, MC were found intact in the periphery. In invasive growth of these tumors as well as in scirrhus (5 observations) and adenocarcinoma (10 observations) MC disappeared from the duct structures and were absent in carcinoma proliferates. Positive immunofluorescence in the conventional location of MC in the alveolar duct system of the mammary gland allows sufficiently valid identification and study of the distribution and changes in these cells. The immunocytochemical verification of MC in dysplasia and duct carcinoma indicates the possibility of using MC as markers of duct carcinoma in situ; MC disappearance from the duct structures characterizes the beginning of the infiltrative tumor growth.
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PMID:[Immunocytochemical study of the myoepithelial cells in fibrocystic disease and ductal carcinoma of the breast]. 629 49

Lymphovascular invasion is an adverse prognostic factor in breast cancer. The lymphatic endothelial marker D2-40 has been shown to improve accuracy in detecting lymphovascular invasion. In addition to marking lymphatic endothelium, D2-40 has been cursorily noted to react with breast myoepithelium. The extent of this expression and the potential for misinterpreting in situ carcinoma as lymphovascular invasion because of D2-40-positive myoepithelium have not been formally addressed. The aim of this study was to determine the scope of breast myoepithelial expression of D2-40 and to identify problematic patterns of expression by in situ carcinoma that could be confused with lymphovascular invasion. We evaluated the distribution and intensity of D2-40 immunohistochemical expression in breast myoepithelium in normal breast (n = 50), proliferative fibrocystic changes (n = 10), ductal carcinoma in situ (n = 35), and lobular carcinoma in situ (n = 5). All cases of normal breast exhibited a variable degree of D2-40 expression by myoepithelium. The distribution was patchy and the intensity was less than that of the adjacent lymphatic endothelium. Larger ducts were more often positive than terminal ducts and lobules. D2-40 marked 77% of ductal carcinoma in situ cases and all lobular carcinoma in situ cases to a variable degree. Only a minority of involved ducts were reactive in each positive case; the intensity was weak to moderate. Although the tumor growth pattern generally enabled distinction of ductal carcinoma in situ from lymphovascular invasion, D2-40 myoepithelial expression in small ducts completely filled by solid-pattern ductal carcinoma in situ mimicked the pattern expected for lymphovascular invasion. Morphology of these myoepithelial cells was not diagnostically helpful as their compressed, stretched-out shape mimicked that of endothelium. Myoepithelial markers (p63 and smooth muscle myosin) confirmed each diagnosis of ductal carcinoma in situ. Lobular carcinoma in situ posed similar problems. The interpretation of D2-40 in the breast requires awareness that myoepithelium may also be immunoreactive. Solid-pattern ductal carcinoma in situ and lobular carcinoma in situ may be misinterpreted as lymphovascular invasion. We recommend that myoepithelial markers be used in conjunction with D2-40 to distinguish solid intralymphatic tumor emboli from solid pattern in situ carcinoma.
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PMID:D2-40 expression by breast myoepithelium: potential pitfalls in distinguishing intralymphatic carcinoma from in situ carcinoma. 1820 95

Myoepithelial neoplasms (MN) are rare and not well-circumstanced entities displaying a heterogeneous spectrum of genetic abnormalities, including EWSR1, FUS and PLAG1 rearrangements. However, in the remaining MN no other fusion gene has been described and knowledge concerning secondary acquired molecular alterations is still poor. Therefore, we screened 5 cases of MN of the soft tissue by RNA sequencing with the aim of identifying novel fusion transcripts. A novel SRF-E2F1 fusion was detected in two cases: one was negative for other fusions while the other showed also the presence of FUS-KLF17. The fusion was validated through independent techniques and, in both cases, SRF-E2F1 was detected only in a subclone of the tumoral mass. SRF-E2F1 maintained the coding frame, thus leading to the translation of a chimeric protein containing the DNA-binding domain of SRF and the trans-activation domain of E2F1. Moreover, ectopical expression of SRF-E2F1 demonstrated that the chimeric transcript is functionally active and could affect tumor growth. Occurrence in two cases and biological relevance of the two genes involved suggest that the SRF-E2F1 fusion might become a helpful diagnostic tool. Further biologic studies are needed to better assess its role in MN biology.
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PMID:Identification of SRF-E2F1 fusion transcript in EWSR-negative myoepithelioma of the soft tissue. 2894 52