Heterologous expression and topography of the main intrinsic protein (MIP) from rat lens

Drake, K.Dawn; Schuette, Diana; Chepelinsky, Ana B.; Crabbe, M. James C.

doi:10.1016/s0014-5793(02)02256-1

Cited by 9 publications

(4 citation statements)

References 29 publications

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“…1B. Chick MIP(AQP0), like its bovine counterpart, is a plasma-membrane protein with a high probability of having six transmembrane domains (Gorin et al, 1984;Drake et al, 2002).…”

Section: Molecular Cloning Of Chick Lens Mip(aqp0) and Sequence Analysismentioning

confidence: 99%

Interaction of major intrinsic protein (aquaporin-0) with fiber connexins in lens development

Jiang

2004

Journal of Cell Science

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We observed that chick lens-fiber gap-junction-forming proteins, connexin (Cx) 45.6 and Cx56, were associated with an unknown protein, which was then identified as major intrinsic protein (MIP), also known as aquaporin-0 (AQP0), the most abundant membrane protein in lens fibers. A 1063 bp cDNA of chick MIP(AQP0) was identified that encodes a 262 amino acid protein with a predicted molecular weight of 28.1 kDa. Dual immunofluorescence and confocal microscopy of sagittal and coronal sections of the lens tissues showed that MIP(AQP0) consistently localized with gap junction plaques formed by Cx45.6 and Cx56 during the early stages of embryonic chick lens development. Immunoprecipitation combined with immunoblotting analyses revealed that MIP(AQP0) was associated with Cx45.6 and Cx56 at these developmental stages. The specificity of this interaction was further confirmed with the silver staining of the protein components of immunoprecipitates. The pull-down analysis of lens lysates revealed that C-terminus of MIP(AQP0) probably interacted with these two fiber connexins. In late embryonic and adult lenses, however, uniform co-distribution of MIP(AQP0) and fiber connexins was largely disrupted, except for the area surrounding the actively differentiating bow regions, as was revealed by immunofluorescence and immunoprecipitation experiments. The interaction of MIP(AQP0) with lens fiber connexins in differentiating lens cells but not in mature lens fibers suggests a potential role for MIP(AQP0) in the facilitation of fiber connexins for the formation of gap junctions during lens development.

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“…1B. Chick MIP(AQP0), like its bovine counterpart, is a plasma-membrane protein with a high probability of having six transmembrane domains (Gorin et al, 1984;Drake et al, 2002).…”

Section: Molecular Cloning Of Chick Lens Mip(aqp0) and Sequence Analysismentioning

confidence: 99%

Interaction of major intrinsic protein (aquaporin-0) with fiber connexins in lens development

Jiang

2004

Journal of Cell Science

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“…The potentially produced selection includes all 13 human aquaporins [40] and a wide range of active plant aquaporins [41][42][43][44][45][46][47]. Large-scale expressions of various functional recombinant aquaporins have been obtained with the aid of a baculovirus/insect cell system [48][49][50][51][52][53][54][55].…”

Section: Production Of Aquaporinsmentioning

confidence: 99%

Aquaporin Biomimetic Membranes

Abdelrasoul¹,

Doan²,

Lohi³

2017

Biomimetic and Bioinspired Membranes for New Frontiers in Sustainable Water Treatment Technology

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Recent research looked at an array of aquaporin protein structures, their unique functions, and potential applications in the research and industrial sectors. This chapter focuses on the specific functional features of aquaporin biomimetic membranes to interrogate their permeability properties in relation to various biomimetic water-transporting membranes. This chapter discusses in detail functional characteristics of aquaporin, how to produce it, and the status of aquaporin development.

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“…Human lung carcinoma cell lines [Princen et al, 1999], as well as a rat colon tumor line [Imaizumi et al, 1998], exhibit a bystander effect that is not altered by gap junction inhibitors [Princen et al, 1999;Imaizumi et al, 1998] or an enhancer [Imaizumi 1998]. GCV metabolites have been suggested to be effluxed from cells and that some type of cellular uptake mechanism independent of GJIC exists for nucleotide entry into neighboring cells [Drake et al, 2002]. Recently, Cx-forming hemichannels are reported, which facilitate the transport of charged small molecules, such as ATP and NAD+ [Guyot andHanrahan, 2002, Jorgensen et al, 2002;Stout et al, 2002].…”

Section: Advantages Of Cxs As a Cancer Therapeu-tic Targetmentioning

confidence: 99%

Connexin Genes as Promising Therapeutic Targets in Cancers

Yano¹,

Sato²,

Hagiwara³

et al. 2007

CPG

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Cellular homeostasis in many organs is maintained via gap junctions composed of connexin (Cx), a large protein family with a number of subtypes. In fact, gap junctional intercellular communication (GJIC) is actively involved in all aspects of the cellular life cycle, ranging from cell growth to cell death. It has been well known that Cx genes act as tumor suppressor genes in GJIC-dependent and GJIC-independent manners. Actually, cancers have two different phenotypes on Cx expression and localization in cells; one shows complete silencing of Cx gene, other shows normal expression of Cx gene but disruption of localization of Cx protein. The former has the down-regulation of Cx functions as GJICdependent transformation, and the latter has disruption of Cx localization as GJIC-independent transformation. Thus, in order to restore Cx-dependent functions in cancers and establish the new cancer therapy based on tumor-suppressive effects of Cx gene, we should develop different procedures on each cancer which has the two different phenotypes. In this mini-review, we summarize the tumor-suppressive effects of Cx genes and refer to a possibility of development of a new cancer therapy based on the restoration of the tumor-suppressive effects.

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Heterologous expression and topography of the main intrinsic protein (MIP) from rat lens

Cited by 9 publications

References 29 publications

Interaction of major intrinsic protein (aquaporin-0) with fiber connexins in lens development

Interaction of major intrinsic protein (aquaporin-0) with fiber connexins in lens development

Aquaporin Biomimetic Membranes

Connexin Genes as Promising Therapeutic Targets in Cancers

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