Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0001430 (adenoma)
 21,222 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The aim of the study was to confirm earlier reports of the association of amyloid deposits in growth hormone (GH)-producing adenomas of the pituitary and the presence of glycosaminoglycans, basement membrane proteins and apolipoprotein E (apo E). Serial sections from 17 amyloidotic and 11 nonamyloidotic, sparsely granulated, GH-producing adenomas obtained from patients presenting with acromegaly were stained with Congo red and Alcian blue, and also with antisera directed against fibronectin, collagen IV, laminin and apo E. Glycosaminoglycans were found in capillaries of every adenoma and were also related spatially to amyloid deposits. Immunostaining of both nonamyloidotic and amyloidotic adenomas demonstrated the presence of fibronectin, collagen IV and laminin in the basement membranes of surrounding nonadenomatous tissue and tumour vessels. In approximately half the amyloidotic adenomas, each basement membrane protein presented with a distinct spatial relationship to amyloid deposits. Apo E was found in 88% of the amyloidotic adenomas within the amyloid deposits, and in six cases intracellular immunostaining was also evident in folliculo-stellate cells. The results are consistent with the presence of glycosaminoglycans, basement membrane proteins and apo E in the amyloid deposits of pituitary adenomas.
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PMID:Basement membrane proteins, apolipoprotein E and glycosaminoglycans in pituitary adenomas and their correlation to amyloid. 969 22

Having previously demonstrated the association of basement membrane components (BMC), as well as apolipoprotein E and amyloid in growth hormone (GH)-producing pituitary adenomas, the aim of this study was to further analyze this relationship at the ultrastructural level. Ultrathin sections from four amyloidotic sparsely granulated monohormonal GH-producing adenomas previously investigated light microscopically were selected. Immunoelectron microscopy was performed, using a single labeling postembedding on-grid Protein-A gold method with antisera directed against laminin, fibronectin and apolipoprotein E. In all four adenomas, anti-laminin, anti-fibronectin, and anti-apolipoprotein E reacted with amyloid fibrils. No BMC were demonstrated between amyloid deposits, making it likely that synthesis and deposition of BMC may be secondary to the deposition of amyloid. The intimate spatial relationship between BMC as well as apolipoprotein E and amyloid fibrils may indicate morphological evidence of a particular arrangement of amyloid components in GH-secreting adenoma amyloid and a pathophysiological link.
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PMID:Basement membrane proteins and apolipoprotein E in growth hormone secreting adenomas and their correlation to amyloid: an immunoelectron microscopic study. 1530 39

The gp130(F/F) genetically engineered mouse (GEM) model reproducibly and predictably develops a gastric adenoma phenotype resembling the primary lesions of human intestinal-type gastric cancer (GC). Accordingly, changes to the serum proteome of gp130(F/F) mice may uncover early-stage GC biomarkers. Here, we have employed several double and compound mutant GEM strains that display distinct phenotypes with respect to gastric tumour load and inflammatory response, thereby mimicking different states of inflammation-associated early-stage GC in humans. This allowed us to distinguish between proteomic changes associated with tumourigenesis rather than confounding systemic inflammation. The comparative proteomic workflow involved depletion of high abundance proteins, 2D-DIGE analysis and protein identification by LC-MS/MS. The differential expression of 112 2D-DIGE spots specifically correlated with the tumour-bearing phenotype, corresponding to 31 murine proteins and their 28 human orthologues. Eight proteins were selected for validation in GC patient sera versus healthy controls. Significant increases in serum apolipoprotein E and haptoglobin, and decreases in afamin and clusterin, were confirmed by ELISA. Receiver operating characteristic analysis revealed that these proteins may be more sensitive and specific discriminators of GC than the existing clinical marker CA72-4.
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PMID:2D-DIGE analysis of sera from transgenic mouse models reveals novel candidate protein biomarkers for human gastric cancer. 2278 72

Major salivary gland tumours are uncommon neoplasms of the head and neck. The increase of precise pre-operative diagnosis is crucial for their correct management and the identification of molecular markers would surely improve the required accuracy. In this study we performed a comparative proteomic analysis of fine needle aspiration fluids of the most frequent benign neoplasms of major salivary glands, namely pleomorphic adenoma and Warthin's tumour, in order to draw their proteomic profiles and to point out their significant features. Thirty-five patients submitted to parotidectomy were included in the study, 22 were identified to have pleomorphic adenoma and 14 Warthin's tumour. Fine needle aspiration samples were processed using a two-dimensional electrophoresis/mass spectrometry-based approach. A total of 26 differentially expressed proteins were identified. Ingenuity software was used to search the biological processes to which these proteins belong and to construct potential networks. Intriguingly, all Warthin's tumour up-regulated proteins such as Ig gamma-1 chain C region, Ig kappa chain C region and Ig alpha-1 chain C region and S100A9 were correlated to immunological and inflammatory diseases, while pleomorphic adenomas such as annexin A1, annexin A4, macrophage-capping protein, apolipoprotein E and alpha crystalline B chain were associated with cell death, apoptosis and tumorigenesis, showing different features of two benign tumours. Overall, our results shed new light on the potential usefulness of a proteomic approach to study parotid tumours and in particular up regulated proteins are able to discriminate two types of benign parotid lesions.
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PMID:New insight into benign tumours of major salivary glands by proteomic approach. 2420 96