Disease relevance of Utrn

• Genetic strategies to replace defective dystrophin with utrophin in individuals with muscular dystrophy requires full characterization of these proteins [1].
• More than 20 clones covering the entire coding region of utrophin were isolated from a rat C6 glioma cell cDNA library [2].
• Dystrophin immunostaining can be ascribed to dystrophin and/or utrophin as well as the DMD (Duchenne Muscular Dystrophy) gene short products Dp140 and Dp71 as revealed by Western immunoblots of synaptosomes isolated from neurohypophyses of control rats [3].

High impact information on Utrn

• We have identified isoforms of dystrophin and utrophin, a dystrophin homologue, expressed in astrocytes and examined their expression patterns during dibutyryl-cAMP (dBcAMP)-induced morphological differentiation of astrocytes [4].
• Differential expression of dystrophin isoforms and utrophin during dibutyryl-cAMP-induced morphological differentiation of rat brain astrocytes [4].
• Immunocytochemical analyses showed that most utrophin was observed in the cytoplasmic area during astrocyte differentiation, whereas Dp71 was found along the cell membrane of the differentiated astrocytes [4].
• Moreover, aggregates of acetylcholine esterase and utrophin, two additional components of the postsynaptic apparatus, were also reduced [5].
• With immunoelectron microscopy, agrin was found in the glomerular basement membrane, dystroglycan was diffusely found over the entire cell surface of the podocytes, and utrophin was localized in the cytoplasm of the podocyte foot processes [6].

Biological context of Utrn

• Concomitant with this up-regulation, utrophin was enriched at the growth cones in differentiating cells, where it co-localizes with beta-dystroglycan [7].

Anatomical context of Utrn

• We investigated three properties of cultured rat aortic smooth muscle cells: morphology, contractile ability, and expression of dystrophin, utrophin, h-CaD, and 1-CaD [8].
• Here we demonstrate that Dp71 and/or utrophin from rat retinal Müller glial cells form a complex with beta-dystroglycan, delta-sarcoglycan and alpha1-syntrophin [9].
• Alpha-dystroglycan (alpha-DG) is part of a complex of cell surface proteins linked to dystrophin or utrophin, which is distributed over the myofiber surface and is concentrated at neuromuscular junctions [10].
• Confocal microscopy showed that dystrobrevin was expressed around blood vessels and under the pia mater as dystrophin, utrophin and beta-dystroglycan were [11].
• A distinct staining pattern for the N-utrophin was not detectable, although it was expected to localise at the actin stress fibers [2].

Associations of Utrn with chemical compounds

• Its sequence is identical to that of the full-length utrophin, except for the last residue where Cys is replaced by Val [2].
• Dystrophin and utrophin are known to link the intracellular cytoskeleton to the extracellular matrix via a transmembraneous glycoprotein complex [2].
• Our results show that utrophin labelling is closely co-localized with that of acetylcholine receptors throughout postnatal maturation. beta-dystroglycan labelling is present at most sites of high acetylcholine receptors density throughout maturation although it often extends beyond the region of highest acetylcholine receptors labelling density [12].
• Upon binding, laminin interacts with dystroglycan, mobilizes utrophin, and assembles a 'nascent' basement membrane, independent of integrin, that is completed by incorporation of type IV collagen [13].
• Digoxigenin-labeled cRNA probes complementary to N-terminal, rod-domain, and C-terminal encoding sequences of utrophin were used to differentiate between full-length and short C-terminal isoforms [14].

Physical interactions of Utrn

• The CH domain-actin interaction for dystrophin was found to be more complex than for utrophin [1].

Other interactions of Utrn

• Utrophin (a dystrophin-related protein) is an ubiquitous protein whose role is still unclear [8].
• Dystrophin, dystrophin-related protein (DRP, utrophin) and dystroglycan are present not only in muscles but also in the brain [15].

Analytical, diagnostic and therapeutic context of Utrn

• Here, electron microscopy and 3D reconstruction of F-actin decorated with utrophin and dystrophin actin-binding constructs were performed using Utr261 (utrophin's CH domain pair), Utr416 (utrophin's CH domains and first spectrin-repeat) and Dys246 (dystrophin's CH domain pair) [1].
• We examined the expression of dystrophin and utrophin proteins and transcripts in the rat retina at different developmental stages using Western blots and semi-quantitative RT-PCR [16].
• Immunocytochemical staining of C6 glioma cells with antisera specific for different utrophin regions localised full-length utrophin in the submembraneous cortical actin layer as revealed by confocal microscopy [2].
• Expression patterns of utrophin were investigated and compared to those of dystrophin and associated proteins in skeletal muscle of rat embryos from E12 to E21 by immunohistochemistry [17].
• Utrophin is lacking at the neuromuscular junctions in the extraocular muscles of normal cat: artefact or true [18]?

References