In this task, you are given a passage which has a question and the context. You have to generate an answer to the question based on the information present in the context.

Q: Context: Magnetic Resonance Imaging (MRI) allows a detailed "in vivo" macroscopic study of the human brain; previously, it has been demonstrated that Fluid Attenuated Inversion Recovery (FLAIR) sequence shows higher signal intensity of cortices belonging to limbic structures.', 'To measure and compare signal intensities (SI) of cytoarchitectonically different cortical regions.', 'In 22 adult subjects, without psychiatric or neurological diseases, FLAIR sequence was performed in coronal slices, perpendicular to the main hippocampal axis. Signal intensity was measured, with a region-of-interest (ROI) function, in 12 different cortical regions. We compared these values and grouped the cortices into five groups: (1) limbic cortices, (2) paralimbic agranular cortices, (3) paralimbic granular cortices, (4) parietal-type neopallium, (5) frontal-type neopallium. A t-test for comparison of paired samples was performed, considering p</=0.05 as statistically significant.', 'We found statistically significant differences amongst the different groups, with the exception of groups 1 and 2, which did not show differences between them. No statistically significant differences were found among cortices belonging to the same group.\Question: Does magnetic resonance imaging identify cytoarchitectonic subtypes of the normal human cerebral cortex?

A: Structural characteristics of the cerebral cortex cause changes in its signal intensity. Magnetic resonance imaging (FLAIR sequence) allows discrimination of different cytoarchitectonic areas of the human cerebral cortex.
****
Q: Context: In our initial attempt to identify differentiation markers for ocular surface epithelia, we observed a unique staining pattern by a commercial anti-Galphaq antibody. We further isolate and characterize the protein reactive with this anti-Galphaq antibody in human ocular surface epithelia.', 'Human donor corneoscleral buttons were sectioned and stained with a battery of commercial antibodies against Galpha proteins. Western blot analysis of cell lysates of corneal epithelial cells and HEK 293 cells transfected with Galphaq cDNA was used to determine the identity of the protein reactive with the anti-Galphaq antibody (E-17). Comparisons were made with another anti-Galphaq antibody (G4415) and an anti-cytokeratin 12C (J7) antibody. The isolated proteins reactive with E17 and J7 were then analyzed with two dimensional isoelectric focusing. Polypeptide sequences were identified using matrix assisted laser desorption/ionization time of flight mass spectrometry (MALDI-TOF MS) after in-gel protein digestion.', 'The E-17 anti-Galphaq antibody preferentially stained the entire corneal epithelia and the suprabasal layers of the limbus with complete absence of staining in the basal limbus and conjunctiva. Western blot analysis of corneal epithelial cells showed that E-17 antibody identified a protein with a molecular weight of 55 kDa. However, the antibody did not react with the purported antigen, Galphaq protein (42 kDa) produced by Galphaq cDNA. Another anti-Galphaq antibody (G4415) did not react with the 55 kDa protein but did react with the 42 kDa Galphaq protein. Further comparison of the E-17 antibody with the J7 antibody revealed that both recognized the 55 kDa band in one and two dimensional analysis. MALDI-TOF MS analysis confirmed that the 55 kDa protein of interest was actually cytokeratin 12 (CK12), rather than Galphaq protein.\Question: Is cytokeratin 12 in human ocular surface epithelia the antigen reactive with a commercial anti-Galpha q antibody?

A: The commercial E-17 anti-Galphaq antibody did not react with Galphaq protein, its purported antigen. Instead, it recognized a 55 kDa protein, which was characterized to be cytokeratin 12 by isoelectric focusing and peptide fingerprinting with mass spectrometry. Based on its reactivity with CK12, this commercial E-17 can be used as a differentiation marker to study ocular surface epithelia.
****
Q: Context: It has recently been found that detrusor smooth muscle cells and myofibroblasts are coupled via gap junctions. However, gap junctions cannot account for strong physical interaction between cells, which has prompted the search for intercellular adhesion molecules. Cadherin-11 is a candidate for such a molecule, since it mediates the interaction of dermal myofibroblasts in contractile wound granulation tissue. We therefore hypothesised that the physical adhesion between detrusor smooth muscle cells and myofibroblasts is mediated by cadherin-11. The aim of this study was to test this hypothesis.', 'Bladder biopsies from eight radical cystectomy specimens were snap-frozen, sectioned, and stained for E-cadherin; cadherin-11; alpha-catenin; beta-catenin; gamma-catenin; and smooth muscle cell/myofibroblast markers connexin-43, vimentin, desmin, smooth muscle actin, and smoothelin. Specimens were analysed by using binocular epifluorescent and confocal laser-scanning microscopy.', 'Specific positive membranous expression of all adhesion complex molecules except E-cadherin was detected in detrusor suburothelial tissue. All biopsies showed a similar punctate pattern of expression for cadherin-11 within bundles of smooth muscle cells and a suburothelial layer of cells. Cadherin-11 was specifically located at the cell membrane, in distinct linear domains.\Question: Is cadherin-11 expressed in detrusor smooth muscle cells and myofibroblasts of normal human bladder?

A:
To our knowledge this is the first time evidence has been provided for cadherin-mediated smooth muscle and suburothelial myofibroblast cell-cell interaction in the human bladder. Cadherin-11 most probably plays an important role in the intercellular physical coupling of detrusor smooth muscle cells and also of myofibroblasts.
****