Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0017168 (gastroesophageal reflux disease)
 11,783 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Barrett's oesophagus (BE) is the precursor lesion to adenocarcinoma of the oesophagus. Understanding of the molecular alterations in this multistage process may contribute to improved diagnosis and treatment. Secreted protein acidic and rich in cysteine (SPARC) is a matricellular protein that modulates cell adhesion and growth. Alterations in SPARC expression have been observed in a variety of solid tumours. The aim of this study was to assess the prevalence and timing of SPARC mRNA expression in Barrett's multistage disease and to investigate the impact of SPARC alterations on the development and progression of this disease. SPARC mRNA expression was measured using a quantitative real-time RT-PCR method in 108 specimens from 19 patients with BE without carcinoma, 20 patients with Barrett's-associated adenocarcinoma (EA), and a control group (CG) of 10 patients without evidence of gastro-oesophageal reflux disease. The median SPARC mRNA expression was significantly upregulated in BE tissues compared to paired normal oesophagus (NE) tissues for the BE group (P=0.004) and for the EA group (P<0.001). The SPARC mRNA expression was significantly higher in adenocarcinoma of the oesophagus compared to matching NE tissue and compared to Barrett's tissues in the EA group (P<0.001). Furthermore, SPARC expression values were significantly different between metaplastic and dysplastic Barrett's tissues (P=0.014). In histologically normal squamous oesophagus tissues obtained from carcinoma patients (EA group), the SPARC mRNA expression was significantly higher compared to NE mucosa from the BE group and the CG group (P=0.03). These findings suggest that the upregulation of SPARC mRNA expression is an early event in the development and progression of BE and EA, and that high SPARC expression may be a clinically useful biomarker for the detection of occult adenocarcinoma, and that a widespread 'field effect' is present in the NE of patients with oesophageal adenocarcinoma.
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PMID:Differential SPARC mRNA expression in Barrett's oesophagus. 1456 24

Fibrillar collagens provide the most fundamental platform in the vertebrate organism for the attachment of cells and matrix molecules. We have identified specific sites in collagens to which cells can attach, either directly or through protein intermediaries. Using Toolkits of triple-helical peptides, each peptide comprising 27 residues of collagen primary sequence and overlapping with its neighbours by nine amino acids, we have mapped the binding of receptors and other proteins on to collagens II or III. Integrin alpha2beta1 binds to several GXX'GER motifs within the collagens, the affinities of which differ sufficiently to control cell adhesion and migration independently of the cellular regulation of the integrin. The platelet receptor, Gp (glycoprotein) VI binds well to GPO (where O is hydroxyproline)-containing model peptides, but to very few Toolkit peptides, suggesting that sequence in addition to GPO triplets is important in defining GpVI binding. The Toolkits have been applied to the plasma protein vWF (von Willebrand factor), which binds to only a single sequence, identified by truncation and amino acid substitution within Toolkit peptides, as GXRGQOGVMGFO in collagens II and III. Intriguingly, the receptor tyrosine kinase, DDR2 (discoidin domain receptor 2) recognizes three sites in collagen II, including its vWF-binding site, although the amino acids that support the interaction differ slightly within this motif. Furthermore, the secreted protein BM-40 (basement membrane protein 40) also binds well to this same region. Thus the availability of extracellular collagen-binding proteins may be important in regulating and facilitating direct collagen-receptor interaction.
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PMID:Cell-collagen interactions: the use of peptide Toolkits to investigate collagen-receptor interactions. 1836 67

Enteral nutrition is beneficial support administered as oral supplements or via tube feeding for patients with long-term inability to meet nutritional requirements orally. However, because of the high volumes administered, vomiting and gastroesophageal reflux are often encountered in patients receiving enteral nutrition. EN-P05 is a novel, highly concentrated enteral nutrition formula that was developed to reduce dosing volume and that satisfies the Japanese recommended daily allowance for most vitamins and trace elements, even in patients who require low-calorie control, such as home-care patients. However, whether EN-P05 can provide nutritional management equivalent to that provided by approved formulas has remained unknown. To investigate the nutritional effectiveness of EN-P05, we evaluated body weight gain, serum chemistry parameters, nitrogen balance, and fat absorption in 7-week-old gastrostomized rats that received either EN-P05 or OSN-001 for 2 weeks. No difference in organ or carcass weight was found between the groups. No significant between-group differences were observed in serum albumin, total protein, triglycerides, or total cholesterol, nor in nitrogen retention or fat absorption rate. No adverse effects associated with administration of EN-P05 were found. These results suggest that EN-P05 can provide the same nutritional management as approved formulas, even when administered in smaller volume.
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PMID:A novel highly concentrated enteral nutrition formula, EN-P05, shows nutritional effectiveness comparable to the approved OSN-001 in gastrostomized rats. 3132 90