Given a passage, construct a question on the basis of the information present in the passage. Construct the question in such a way that (i) it is unambiguous, (ii) it is answerable from the passage, (iii) its answer is unique (iv) it answer uses text phrases from the passage. Avoid creating questions that (i) can't be answered correctly without actually understanding the passage and (ii) uses the same words or phrases given in the passage.

Input: Consider Input: Cadherins are calcium-dependent cell-to-cell adhesion glycoproteins playing a critical role in the formation and maintenance of normal tissue architecture. In normal mammary gland, E-cadherin is expressed by luminal epithelial cells, while P-cadherin is restricted to myoepithelial cells. Changes in the expression of classical E- and P-cadherins have been observed in mammary lesions and related to mammary carcinogenesis. P-cadherin and E-cadherin expressions were studied in a series of feline normal mammary glands, hyperplastic/dysplastic lesions, benign and malignant tumours by immunohistochemistry and double-label immunofluorescence.', 'In normal tissue and in the majority of hyperplastic/dysplastic lesions and benign tumours, P-cadherin was restricted to myoepithelial cells, while 80% of the malignant tumours expressed P-cadherin in luminal epithelial cells. P-cadherin expression was significantly related to high histological grade of carcinomas (p <0.0001), tumour necrosis (p = 0.001), infiltrative growth (p = 0.0051), and presence of neoplastic emboli (p = 0.0401). Moreover, P-cadherin positive carcinomas had an eightfold likelihood of developing neoplastic emboli than negative tumours. Cadherins expression profile in high grade and in infiltrative tumours was similar, the majority expressing P-cadherin, regardless of E-cadherin expression status. The two cadherins were found to be co-expressed in carcinomas with aberrant P-cadherin expression and preserved E-cadherin.

Output: Is aberrant P-cadherin expression associated to aggressive feline mammary carcinomas?


Input: Consider Input: Corticosteroid treatment affects muscle protein and glutamine metabolism. In the present study we aimed to clarify to what extent anorexia, weight loss and corticosteroids determine protein and glutamine metabolism in muscle.', 'The study was performed in Wistar rats (300-350 g, n = 40) given triamcinolone (0.25 mg/kg/day i.m.) treatment (CS group) for 14 days, sham treated free fed (FF group), sham treated pair fed (PF group) and sham treated pair weight (PW group). In vivo protein and glutamine turnover were measured using L-[2,6-3H]phenylalanine and L-[3,4-3H]glurtamine as tracer in a three compartment model across the hindquarter.', 'Corticosteroid treatment decreased total body weight to a greater extent than can be explained by decreased food intake only, justifying the need for pair weight controls. Muscle weight loss was relatively greater in the corticosteroid treated rats than in the pair weight controls indicating specific corticosteroid induced changes in muscle protein metabolism. Pair weight rats increased muscle net protein breakdown rates from -5 +/- 3 nmol x 100 g body weight(-1) x min(-1) to -15 +/- 3 nmol x 100 g body weight(-1) x min(-1) (P < 0.05 vs FF). In the corticosteroid treated rats net protein breakdown rates increased to -22 +/- 4 nmol x 100 g body weight(-1) x min(-1) (P < 0.01 CS vs FF/PF) Net protein breakdown in corticosteroid treated rats was accompanied by increased glutamine efflux from the hindquarter (P < 0.05, CS vs FF/PF/PW). The latter could predominantly be explained by de novo synthesis. Furthermore, corticosteroid treatment induced a loss of plasma to free muscle glutamine gradient indicating down regulation of glutamine membrane transport rates into muscle. This effect was, however, similar in the pair weight control group and can thus be fully accounted for by the muscle weight loss.

Output: Is de novo glutamine synthesis induced by corticosteroids in vivo in rats secondary to weight loss?


Input: Consider Input: To study bcl-2 expression in ductular proliferation cholangiocytes and hepatic stellate cell activation in liver biopsies from patients with autoimmune cholangitis and primary biliary cirrhosis.', 'Twenty-four primary biliary cirrhosis patients and 11 autoimmune cholangitis patients were included. Thirty-four females, average age: 52.5+/-12.6 years. We studied the presence of ductular proliferation, cholestasis, florid ductal lesion, granulomata, ductopenia and histologic stage. Patients were classified in primary biliary cirrhosis or autoimmune cholangitis according to antimitochondrial antibodies, antinuclear antibodies, smooth muscle antibody, antiGP210 and antiSP100 autoantibodies. We studied the presence of bcl-2 by monoclonal antibcl-2 antibody (clon 100, BioGenex). The presence of activated (specific antialpha-actin antibodies) and independent lobular, periportal and portal hepatic stellate cell was assessed using a semiquantitative scale.', "Interlobular ducts bcl-2 was seen in 18 (51.4%) patients. Activated periportal hepatic stellate cell correlated with Ludwig's stage (r=0.43; n=35; p=0.01). Ten out of 15 (66.6%) patients with ductular proliferation showed positive interlobular ducts bcl-2 while bcl-2 was negative in 8 out of 20 (40%) patients without ductular proliferation; p<0.05. Bcl-2 positive patients in ductular proliferation showed a more advanced Ludwig's stage (2.33+/-0.77 versus 1.26+/-1.05; p<0.05) and a higher periportal hepatic stellate cell activation index (0.83+/-0.78 versus 0.23+/-0.43; p=0.009). No relationship was found among periportal hepatic stellate cell activation and the presence of florid ductal lesion, cholestasis, granulomata or biliary erosive necrosis. Hepatic stellate cell activation was similar in patients with either autoimmune cholangitis or primary biliary cirrhosis.


Output: Is expression of bcl-2 in ductular proliferation related to periportal hepatic stellate cell activation and fibrosis progression in patients with autoimmune cholestasis?