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Major intrinsic protein is a member of the water-transporting aquaporins as well as the original member of the MIP family of channel proteins. Additionally we are shipping MIP Kits (16) and many more products for this protein.
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The proposed schematic models illustrate that cell-to-cell adhesion elicited by AQP0 is vital for lens transparency and homeostasis.
A concentration signal could trigger a regulatory change in AQP0 water permeability.
Cataractogenesis in Mip(Nat (show BRD2 Antibodies)) mutants are caused by defects in MIP expression.
These data suggest that while relatively few genes ( approximately 1.5% of the transcriptome) were differentially regulated >2-fold in the Mip-/- lens, calpain hyper-activation acts as a terminal pathogenic event during lens fiber cell death and cataract formation.
hypothesize that AQP0, with its prolific expression at the fiber cell membrane, could provide anchorage for cytoskeletal structures like BFs and together they help to confer fiber cell shape, architecture and integrity
In summary, lens transparency, CTCA and compact packing of fiber cells were affected due to the loss of 50% AQP0 leading to larger extracellular space, more water content and SA, possibly due to alteration in RING.
Post-translational truncation of N- or C-terminal end amino acids does not alter the basal water permeability of AQP0 or its adhesive functions.
Data show that Ca(V) 1.2 and 1.3 channels are expressed in lens, regulating phosphorylation of aquaporin-0 and myosin light chain and expression of connexins 50 and 46.
The additional negative charge introduced by phosphoserine 235 perturbs electrostatic interactions between aquaporin-0 and calmodulin (show Calm2 Antibodies) to favour water influx through the channel.
increased water permeability through AQP1 (show AQP1 Antibodies) does not compensate for loss of AQP0 expression in TgAQP1(+/+)/AQP0(-/-) mice. Fiber cell AQP0 expression is required to maintain their organization, which is a requisite for lens transparency
Kynurenine might inhibit FGF2 (show FGF2 Antibodies)-mediated fiber cell differentiation by preventing expression of crystallins and MIP26.
MIP has essential roles in the establishment and maintenance of uniform fiber structure, and the organization of fibers, and as such is essential for lens function.
The data evidence a broad lipidation profile of AQP0 that is both species and site independent, suggesting a chemical-based ester aminolysis mechanism to explain such modifications.
A novel MIP (show TNPO1 Antibodies) frame-shift mutation in familial congenital nuclear cataract patient
defects in AQP-0 permeability may be a cause for presbyopia.
the p.D150H mutation is a novel disease-causing mutation in MIP (show TNPO1 Antibodies), which leads to congenital progressive cortical punctate cataract by impairing the trafficking mechanism of AQP0.
Authors identified a novel nonsense mutation in MIP (show TNPO1 Antibodies) (c.657 C>G; p.Y219*) (major intrinsic protein gene) that segregates with congenital posterior polar cataract in a Chinese family.
Functional evidence linking the new MIP (show TNPO1 Antibodies) mutation of G215D to autosomal dominant congenital cataracts.
A novel donor splice-site mutation (c.606+1G>A) in the MIP (show TNPO1 Antibodies) gene causes congenital cataract in a Chinese family.
the first nonsense mutation of MIP (show TNPO1 Antibodies) identified in autosomal dominant congenital cataracts
Mutation of this conserved glycine residue leads to improper trafficking of AQP0-G165D and loss of water channel (show AQP4 Antibodies) function.
Aquaporin 0 R233K mutation did not affect the expression, location and trafficking of the protein but did influence the interaction between AQP0 and CaM (show CALM1 Antibodies).
In the presence of alpha-crystallin, this conversion to beta-sheet is minimized, suggesting that the protein structure that binds to the molecular chaperone (show HSP90AA1 Antibodies) is mostly the alpha-helical structure of AQP0.
Determined the pseudoatomic structure of full-length aquaporin-0 (AQP0) in complex with calmodulin (show KRIT1 Antibodies), using electron microscopy to elucidate how this signaling protein modulates water-channel (show AQP4 Antibodies) function.
Tyr23 is a dominate factor leading to the low water permeability in AQP0.
AQP-0 and connexins can be segregated in the membrane by protein-lipid interactions as modified by AQP-0 homo-oligomerization
determination of the x-ray structure of bovine aquaporin 0 to a resolution of 2.2 A; structure aids the analysis of the interaction of the extracellular domains and the possibility of a cell-cell adhesion role for AQP0
The crystal packing was determined by molecular replacement and shows that, within the cubic lattice, AQP0 tetramers are associated head-to-head along their 4-fold axes.
Major intrinsic protein is a member of the water-transporting aquaporins as well as the original member of the MIP family of channel proteins. The function of the fiber cell membrane protein encoded by this gene is undetermined, yet this protein is speculated to play a role in intracellular communication. The MIP protein is expressed in the ocular lens and is required for correct lens function. This gene has been mapped among aquaporins AQP2, AQP5, and AQP6, in a potential gene cluster at 12q13.
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