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MIP  -  major intrinsic protein of lens fiber

Homo sapiens

Synonyms: AQP0, Aquaporin-0, CTRCT15, LIM1, Lens fiber major intrinsic protein, ...
 
 
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Disease relevance of MIP

  • Dominantly inherited cataracts with differing clinical features were found in two families carrying different point mutations in the gene encoding lens water channel protein AQP0 (major intrinsic protein, MIP) [1].
  • Osmotically shocked yeast cells were affected only slightly by expression of the Escherichia coli glycerol channel GlpF, which belongs to the MIP family but is a weak water channel [2].
  • An invasion assay shows that the MIP protein from Legionella pneumophila (LpMIP), which has an equivalent N-terminal alpha-helix, can substitute for TcMIP [3].
  • After 8 weeks, there were fewer activated macrophages in livers of gp91(phox-/-) mice than controls, despite similar mRNA levels for MCP and MIP chemokines, but fibrosis was similar [4].
  • The severity of dyspnea expressed as the slope of the relationship between BS and VE/MVV (DBS/D[VE/MVV]) showed in COPD a significant inverse correlation with VC, FEV1, MIP, and a positive correlation with PaCO2 and VE/MVV at rest [5].
 

Psychiatry related information on MIP

  • Although both groups scored high on the Mania Rating Scale, MIP patients had significantly more often been diagnosed as schizophrenic, or anxiety disorders, with long delays to first diagnosis as bipolar disorder [6].
  • We tested the hypotheses that those users who develop MAMP-induced psychosis (MIP) have greater familial loading for psychotic disorders than users with no psychosis [7].
 

High impact information on MIP

 

Biological context of MIP

 

Anatomical context of MIP

  • When expressed in Xenopus oocytes, the osmotic water permeability (P(f)) of MIP and AQP2 was 48 and 245 x 10(-)(4) cm/s, respectively [14].
  • These allelic cataract mutations provide the first direct evidence that MIP plays a crucial role in the development of a transparent eye lens [9].
  • In this paper we demonstrate that this P25 polypeptide is a member of the MIP family of membrane channel proteins, and that P25 forms homotetramers in the native membranes [15].
  • Structural analysis of a MIP family protein from the digestive tract of Cicadella viridis [15].
  • We show now that MP70 can be solubilized separately from MIP in mild detergent solutions, and that this treatment results in the dissociation of the fibre gap junctions [16].
 

Associations of MIP with chemical compounds

  • Glycerol transporters identified to date belong to the Major Intrinsic Protein (MIP) family of integral membrane proteins, and one of them, aquaporin-3 (AQP3), has been characterized in mammals [17].
  • Replacement of the glycine at this site in AQP0, AQP1, and AQP2 blocked expression of the mutants at the oocyte plasma membrane [18].
  • CONCLUSIONS: Specific sites of MIP N- and C-terminal cleavage in selenite-induced cataractous lenses were identified [19].
  • METHODS: MIP was isolated from single human lenses of various ages (7- 86 years) by homogenization of the lenses, followed by centrifugation and urea washes of the membranes [20].
  • Diisopropylphosphorofluoridate (DFP), the phosphate analogue of the phosphoroamidate MIP, was used for comparison [21].
 

Physical interactions of MIP

 

Regulatory relationships of MIP

  • Similarly, the analogous mass shift for aged MIP-inhibited BChE was 122.4 +/- 0.7 Da, corresponding to a monoisopropylphosphoroamido adduct [21].
 

Other interactions of MIP

 

Analytical, diagnostic and therapeutic context of MIP

  • Northern blot analysis of MT RNA showed a single transcript of about 1-1.3 kb for Rp-MIP [26].
  • The simulations demonstrate that AQP0, in single or double lipid bilayers, is not closed to water transport and that thermal motions of critical side-chains are sufficient to facilitate the movement of water past any of its constriction regions [27].
  • For comparison, CD of MIP26 in OG gave 49 +/- 7% alpha-helix and 32 +/- 12% beta-sheet and -turn; FTIR gave 32 +/- 8% alpha-helix and 45 +/- 6% beta-sheet and -turn [28].
  • Membrane proteins still embedded in the membranes were digested with trypsin, and the resulting C-terminal peptides of AQP0 were analyzed by HPLC tandem mass spectrometry, permitting the identification of modifications and estimation of their abundance [29].
  • CHIP28 (glycosylated and nonglycosylated) and MIP26 were purified further by high-performance size-exclusion chromatography, eluting in OG as apparent dimers and tetramers, respectively [28].

References

  1. Functional impairment of lens aquaporin in two families with dominantly inherited cataracts. Francis, P., Chung, J.J., Yasui, M., Berry, V., Moore, A., Wyatt, M.K., Wistow, G., Bhattacharya, S.S., Agre, P. Hum. Mol. Genet. (2000) [Pubmed]
  2. In vivo functional assay of a recombinant aquaporin in Pichia pastoris. Daniels, M.J., Wood, M.R., Yeager, M. Appl. Environ. Microbiol. (2006) [Pubmed]
  3. Trypanosoma cruzi macrophage infectivity potentiator has a rotamase core and a highly exposed alpha-helix. Pereira, P.J., Vega, M.C., González-Rey, E., Fernández-Carazo, R., Macedo-Ribeiro, S., Gomis-Rüth, F.X., González, A., Coll, M. EMBO Rep. (2002) [Pubmed]
  4. NADPH oxidase is not an essential mediator of oxidative stress or liver injury in murine MCD diet-induced steatohepatitis. Dela Pe??a, A., Leclercq, I.A., Williams, J., Farrell, G.C. J. Hepatol. (2007) [Pubmed]
  5. Dyspnea on exercise. Pathophysiologic mechanisms. Rampulla, C., Baiocchi, S., Dacosto, E., Ambrosino, N. Chest (1992) [Pubmed]
  6. The mood-instability hypothesis in the origin of mood-congruent versus mood-incongruent psychotic distinction in mania: validation in a French National Study of 1090 patients. Azorin, J.M., Akiskal, H., Hantouche, E. Journal of affective disorders (2006) [Pubmed]
  7. Morbid risk for psychiatric disorder among the relatives of methamphetamine users with and without psychosis. Chen, C.K., Lin, S.K., Sham, P.C., Ball, D., Loh, e.l.-.W., Murray, R.M. Am. J. Med. Genet. B Neuropsychiatr. Genet. (2005) [Pubmed]
  8. Missense mutations in MIP underlie autosomal dominant 'polymorphic' and lamellar cataracts linked to 12q. Berry, V., Francis, P., Kaushal, S., Moore, A., Bhattacharya, S. Nat. Genet. (2000) [Pubmed]
  9. Mutations in the founder of the MIP gene family underlie cataract development in the mouse. Shiels, A., Bassnett, S. Nat. Genet. (1996) [Pubmed]
  10. cDNA cloning and gene structure of a novel water channel expressed exclusively in human kidney: evidence for a gene cluster of aquaporins at chromosome locus 12q13. Ma, T., Yang, B., Kuo, W.L., Verkman, A.S. Genomics (1996) [Pubmed]
  11. Human AQP2 and MIP genes, two members of the MIP family, map within chromosome band 12q13 on the basis of two-color FISH. Saito, F., Sasaki, S., Chepelinsky, A.B., Fushimi, K., Marumo, F., Ikeuchi, T. Cytogenet. Cell Genet. (1995) [Pubmed]
  12. Aquaporins (water channels): role in vasopressin-activated water transport. Dibas, A.I., Mia, A.J., Yorio, T. Proc. Soc. Exp. Biol. Med. (1998) [Pubmed]
  13. Closely spaced tandem arrangement of AQP2, AQP5, and AQP6 genes in a 27-kilobase segment at chromosome locus 12q13. Ma, T., Yang, B., Umenishi, F., Verkman, A.S. Genomics (1997) [Pubmed]
  14. Transmembrane helix 5 is critical for the high water permeability of aquaporin. Kuwahara, M., Shinbo, I., Sato, K., Terada, Y., Marumo, F., Sasaki, S. Biochemistry (1999) [Pubmed]
  15. Structural analysis of a MIP family protein from the digestive tract of Cicadella viridis. Beuron, F., Le Cahérec, F., Guillam, M.T., Cavalier, A., Garret, A., Tassan, J.P., Delamarche, C., Schultz, P., Mallouh, V., Rolland, J.P. J. Biol. Chem. (1995) [Pubmed]
  16. Dissociation of lens fibre gap junctions releases MP70. Kistler, J., Bullivant, S. J. Cell. Sci. (1988) [Pubmed]
  17. Evidence for the presence of aquaporin-3 in human red blood cells. Roudier, N., Verbavatz, J.M., Maurel, C., Ripoche, P., Tacnet, F. J. Biol. Chem. (1998) [Pubmed]
  18. Conversion of aquaporin 6 from an anion channel to a water-selective channel by a single amino acid substitution. Liu, K., Kozono, D., Kato, Y., Agre, P., Hazama, A., Yasui, M. Proc. Natl. Acad. Sci. U.S.A. (2005) [Pubmed]
  19. Modifications to rat lens major intrinsic protein in selenite-induced cataract. Schey, K.L., Fowler, J.G., Shearer, T.R., David, L. Invest. Ophthalmol. Vis. Sci. (1999) [Pubmed]
  20. Characterization of human lens major intrinsic protein structure. Schey, K.L., Little, M., Fowler, J.G., Crouch, R.K. Invest. Ophthalmol. Vis. Sci. (2000) [Pubmed]
  21. Mechanism of aging of mipafox-inhibited butyrylcholinesterase. Kropp, T.J., Richardson, R.J. Chem. Res. Toxicol. (2007) [Pubmed]
  22. The C terminus of lens aquaporin 0 interacts with the cytoskeletal proteins filensin and CP49. Lindsey Rose, K.M., Gourdie, R.G., Prescott, A.R., Quinlan, R.A., Crouch, R.K., Schey, K.L. Invest. Ophthalmol. Vis. Sci. (2006) [Pubmed]
  23. Incorporation of proteins into (Xenopus) oocytes by proteoliposome microinjection: functional characterization of a novel aquaporin. Le Cahérec, F., Bron, P., Verbavatz, J.M., Garret, A., Morel, G., Cavalier, A., Bonnec, G., Thomas, D., Gouranton, J., Hubert, J.F. J. Cell. Sci. (1996) [Pubmed]
  24. Aquaporins: water channel proteins of the cell membrane. Takata, K., Matsuzaki, T., Tajika, Y. Progress in histochemistry and cytochemistry. (2004) [Pubmed]
  25. Structural basis of water-specific transport through the AQP1 water channel. Sui, H., Han, B.G., Lee, J.K., Walian, P., Jap, B.K. Nature (2001) [Pubmed]
  26. Identification of a new water channel (Rp-MIP) in the Malpighian tubules of the insect Rhodnius prolixus. Echevarría, M., Ramírez-Lorca, R., Hernández, C.S., Gutiérrez, A., Méndez-Ferrer, S., González, E., Toledo-Aral, J.J., Ilundáin, A.A., Whittembury, G. Pflugers Arch. (2001) [Pubmed]
  27. Water transport in AQP0 aquaporin: molecular dynamics studies. Han, B.G., Guliaev, A.B., Walian, P.J., Jap, B.K. J. Mol. Biol. (2006) [Pubmed]
  28. Secondary structure analysis of purified functional CHIP28 water channels by CD and FTIR spectroscopy. Van Hoek, A.N., Wiener, M., Bicknese, S., Miercke, L., Biwersi, J., Verkman, A.S. Biochemistry (1993) [Pubmed]
  29. Post-translational modifications of aquaporin 0 (AQP0) in the normal human lens: spatial and temporal occurrence. Ball, L.E., Garland, D.L., Crouch, R.K., Schey, K.L. Biochemistry (2004) [Pubmed]
 
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