One of the protein components of lens fiber membranes is glyceraldehyde 3‐phosphate dehydrogenase

Lenstra, Johannes A.; Raaij, A.J.M. van den Eijnden-van; Bloemendal, H.

doi:10.1016/0014-5793(82)80821-1

Cited by 11 publications

(4 citation statements)

References 15 publications

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“…An enrichment in the Na', K+-ATPase and the predominant presence of' a 35-kDa component, identical to a lenticular plasma membrane component (MP35 [29]), confirmed that this procedure, which does not deviate essentially from published procedures, yielded a membrane preparation. However, since no attempt was made to separate plasma membranes from, for example, mitochondria1 membrane fragments or smooth endoplasmatic reticulum, our procedures a s well as those commonly used d o not allow the assignment of the membrane protein spots in Fig.…”

Section: Topography Q F ' Cellular Proteinssupporting

confidence: 56%

“…As reported earlier for HeLa cells [I51 the membrane fraction (Fig.lA, third lane) was dominated by a protein of 35000 M,, which was detected as a streaky spot in the basic part of the two-dimensional gel (Fig.2C), indicated by the letter 'm'. The same protein has been found as main component in plasma membranes from lens fiber cells ('MP35', [29]) and has been observed on gels of plasma membranes from Chinese hamster ovary cells [30].…”

Section: Gel Electrophoretic Analysis Of the Fractionsmentioning

confidence: 83%

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Topography of the total protein population from cultured cells upon fractionation by chemical extractions

Lenstra

Bloemendal

1983

European Journal of Biochemistry

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1. Chemical extractions are proposed a s a major tool for a fractionation of cellular proteins. As a model system, proteins from cultured hamster lens cells have been divided by independent extractions into seven subcellular fractions, corresponding to water-soluble proteins and the proteins from membranes, microfilaments (and, other deoxycholate-soluble proteins), intermediate filaments, microtubules, polysomes and nuclei respectively. The latter two fractions have becn subfractionated yielding ribosomal proteins, the elongation and initiation f, act o r s of the protein-synthesis machinery, chromatin proteins and non-chromatin proteins.2. The protein compositions of the fractions have been analyzed by one-dimensional and two-dimensional gel electrophoresis. This resulted in an almost complete topography of the proteins detected on two-dimensional gels of total-cell lysates.3. Comparison of two-dimensional patterns of proteins from the total-cell lysate and proteins from hamster erythrocytes or from liver, muscle or brain tissue showed that the different cell types have only few proteins in common. Two proteins are common to all of these cell types, namely actin and a 68-kDa protein. The latter protein was, like actin, vimentin and the tubulin subunits, also present in most cell fractions. Evidence is presented that this protein is identical to a 68-kDa heat-shock protein.

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Section: Topography Q F ' Cellular Proteinssupporting

confidence: 56%

Section: Gel Electrophoretic Analysis Of the Fractionsmentioning

confidence: 83%

Topography of the total protein population from cultured cells upon fractionation by chemical extractions

Lenstra

Bloemendal

1983

European Journal of Biochemistry

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“…In addition to band 3, also other proteins from membrane preparations from lens, cardiac and skeletal muscle, synaptosomes, and yeast (Green et al, 1965;Knull, 1978Knull, , 1980Lenstra et al, 1982;Caswell and Corbett, 1985;Pierce and Philipson, 1985) interact with GAPDH. The reported association of GAPDH with synaptosomal proteins and the presumed localization of APP at synaptic sites (Knull, 1978, 1980 are particularly interesting and may provide some evidence for the list of postulated secondary functions attributed to GAPDH.…”

Section: D1 Scu Sslonmentioning

confidence: 99%

Rat Brain Glyceraldehyde‐3‐Phosphate Dehydrogenase Interacts with the Recombinant Cytoplasmic Domain of Alzheimer's β‐Amyloid Precursor Protein

Schulze

Schuler

Stüber

et al. 1993

Journal of Neurochemistry

121

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Abundant senile plaques are a histological hallmark in the brain of Alzheimer's disease patients. Such plaques consist of, among many other constituents, aggregated beta A4 amyloid peptide. This peptide is derived from an amyloid precursor protein (APP) by irregular proteolytic processing and is considered to be involved in the development of Alzheimer's disease. To study possible interactions of brain proteins with beta A4 amyloid or other fragments of APP, beta A4 amyloid and beta A4 amyloid extended to the C-terminus of APP were recombinantly produced as fusion proteins termed "Amy" and "AmyC," respectively. Using Amy and AmyC affinity chromatography, a 35-kDa protein from rat brain was isolated that bound tightly to AmyC but not to Amy, thus indicating an interaction of the protein with the C-terminus of APP. This 35-kDa protein was identified as the glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase (GAPDH). Binding of GAPDH to AmyC but not to Amy was confirmed by gel filtration. Although AmyC slightly reduced the Vmax of GAPDH, the same reduction was observed in the presence of Amy. These findings suggest that the interaction of the cytoplasmic domain of APP with GAPDH is unlikely to influence directly the rate of glycolysis but may serve another function.

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“…The lens proteins of the mammalian eye, for example, consist of a mixture that includes glyceraldehyde-3-P dehydrogenase (Lenstra et al, 1982). In vertebrates, proteins similar or identical to the glycolytic enzymes P-glycerate kinase (Viswanatha et al, 1992), glyceraldehyde-3-P dehydrogenase (Singh and Green, 1993), and aldolase (Ronai et al, 1992) are found in the nucleus.…”

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confidence: 99%

Three Enzymes of Carbon Metabolism or their Antigenic Analogs in Pea Leaf Nuclei

1995

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Antigens closely resembling or identical to the three glycolytic enzyme proteins phosphate-glycerate kinase, glyceraldehyde-3-phosphate dehydrogenase, and aldolase are found in situ in the nucleus of the leaf mesophyll cells of pea (Pisum safivum 1.). These proteins have already been identified in vertebrate nuclei. Apparently, these enzymes are nuclear proteins with "secondary" roles not directly related to their enzymatic function in carbon metabolism in both animals and plants.

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One of the protein components of lens fiber membranes is glyceraldehyde 3‐phosphate dehydrogenase

Cited by 11 publications

References 15 publications

Topography of the total protein population from cultured cells upon fractionation by chemical extractions

Topography of the total protein population from cultured cells upon fractionation by chemical extractions

Rat Brain Glyceraldehyde‐3‐Phosphate Dehydrogenase Interacts with the Recombinant Cytoplasmic Domain of Alzheimer's β‐Amyloid Precursor Protein

Three Enzymes of Carbon Metabolism or their Antigenic Analogs in Pea Leaf Nuclei

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