Publications by authors named "Elizabeth Blaney"

Amyloidosis is a heterogeneous disease that can cause a wide array of nonspecific symptoms when the gastrointestinal (GI) tract is involved, including weight loss, early satiety, change in bowel habits with diarrhea, constipation, or alternating bowel pattern. Endoscopy with biopsy for Congo red staining establishes the diagnosis and fibril subtyping helps to guide targeted treatment options. Light chain amyloidosis is the most frequent subtype found throughout the GI tract.

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Intestinal inertia is a severe form of gut dysmotility that may require surgical resection. Loss of myenteric ganglion cells has been proposed as a possible etiology. Preclinical models have also suggested that virus infection-associated ganglionitis may be an alternative pathogenic factor.

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Objectives: Despite the fact that the most effective treatment for morbid obesity today is gastric bypass surgery, some patients develop life-threatening nutritional complications associated with their weight loss.

Methods: Here we examine the influence of the altered anatomy and digestive physiology on pancreatic secretion and fat absorption. Thirteen post Roux-en-Y gastric bypass (RYGB) patients who had lost >100 lbs in the first year following surgery and who gave variable histories of gastrointestinal (GI) dysfunction, were selected for study.

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The glycosidase alpha-amylase is responsible for the hydrolysis of alpha(1-->4) glycosidic linkages found in dietary starch as one means for controlling blood sugar level. The effect of alpha-amylase is detrimental, however, in the disease state diabetes mellitus, where blood glucose levels are elevated due to a biochemical defect. Inhibition of the enzyme's activity would reduce glucose absorption by the small intestine.

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Peptide analogues of Tendamistat which include the most essential residues linked by novel omega-amino acids (X,Y,Z: H2N-(CH2)n-CO(2)H, where n=2-10) were designed, synthesized (Ac-Tyr(15)-X-Trp(18)-Arg(19)-Tyr(20)-Y-Thr(55)-Z-Asp(58)-Gly(59)-Tyr(60)-Ile(61)-Gly(62)-NH2), and analyzed for alpha-amylase inhibitory activity. Native dipeptide spacers sometimes were left intact at X and Z. Analogues demonstrated competitive inhibition with K(i) values ranging from 23 to 767 microM.

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