Molecular cloning and characterization of gene for Golgi-localized syntaphilin-related protein on human chromosome 8q23

Funakoshi, Eishi; Nakagawa, Kin-ya; Hamano, Ayako; Hori, Takamitsu; Shimizu, Atsushi; Asakawa, Shuichi; Shimizu, Nobuyoshi; Ito, F.

doi:10.1016/j.gene.2004.10.024

Cited by 6 publications

(10 citation statements)

References 36 publications

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“…The Rabbit anti-GOLSYN antibody was prepared as DNA fragments obtained by internal amplification described previously (6). The following antibodies and 5′ and 3′ RACE reaction were subcloned into a were purchased from the sources indicated: mouse pCR2.…”

Section: Reagentsmentioning

confidence: 99%

“…The RACE reaction was performed to determine the sequences of m-Golsyn gene at 5′ and 3′ ends with First-strand cDNA was synthesized from 5 µg of total RNA by using Ready to Go You-Prime First-Strand Marathon-Ready mouse brain cDNA library used as template. PCR reactions were carried out by using Beads (Amersham Biosciences Corp.) and pd (N) 6 random hexanucleotides as primer according to man-Advantage 2 DNA polymerase mix for the 5′ and 3′ RACE and the internal fragments. For internal ampli-ufacturer's instructions.…”

Section: Reagentsmentioning

confidence: 99%

“…Sucrose gradient centrifugation was performed as primers: 5′-atctggcaccacacct-3′ and 5′-cgtcatactcctgc ttg-3′. DNA fragments amplified by PCR were re-described previously (6). Briefly, pellet P or SV was resuspended in 1.5 M sucrose solution, applied to a solved by electrophoresis on a 1.5% agarose gel, stained with 10 µg/ml of ethidium bromide, and visu-gradient containing 0.32 and 1.25 M sucrose solution, and centrifuged at 100,000 × g for 60 min.…”

Section: Reagentsmentioning

confidence: 99%

“…Immunoblot Analysis Mice were killed, and then their brain, spinal cord, heart, liver, lung, pancreas, stomach, small intestine, Immunoblot analysis was performed as described previously (6). Briefly, proteins separated by SDS-kidney, spleen, testis, and skeletal muscle were quickly removed and immersed in the homogenizing PAGE were transferred electrophoretically onto a polyvinylidene difluoride membrane (Immobilon, buffer described below.…”

Section: Reagentsmentioning

confidence: 99%

“…In this report, we describe the genomic structure of to the human chromosome 8q23 region (6). Because one of genes involved in adult-onset primary open-m-Golsyn, the mouse ortholog of the h-GOLSYN gene and its expression in various cell lines and tis-angle glaucoma (POAG) has been mapped to this chromosomal region (20,22,23,(26)(27)(28)(29)(30)(31), h-GOLSYN sues.…”

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confidence: 99%

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Molecular Cloning of the m-<I>Golsyn</I> Gene and its Expression in the Mouse Brain

Funakoshi

Hamano²,

Fukui³

et al. 2006

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The mouse ortholog of the human GOLSYN gene, termed the m-Golsyn gene, was isolated and mapped to the region on mouse chromosome 15B3.2 syntenic with human chromosome 8q23. Three mRNA species (type la, 1b, and type 2) were produced by use of alternative transcription initiation points and alternative splicing events. The type 1 mRNAs were expressed only in the brain, whereas the type 2 was detected in various tissues. m-Golsyn protein was expressed in various tissues including the brain. Immunohistochemical study of m-Golsyn protein showed its prominent expression in the neuronal cells in various regions of the brain and strong expression in the choroid plexus ependymal cells lining the ventricles. m-Golsyn protein was found to be homologous to syntaphilin, a regulator of synaptic vesicle exocytosis. These results indicate that the m-Golsyn protein may play an important role in intracellular protein transport in neuronal cells of the brain.

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Section: Reagentsmentioning

confidence: 99%

Section: Reagentsmentioning

confidence: 99%

Section: Reagentsmentioning

confidence: 99%

Section: Reagentsmentioning

confidence: 99%

mentioning

confidence: 99%

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Molecular Cloning of the m-<I>Golsyn</I> Gene and its Expression in the Mouse Brain

Funakoshi

Hamano²,

Fukui³

et al. 2006

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Mitochondrial dynamics during cell cycling

2016

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Mitochondria are the cell's power plant that must be in a proper functional state in order to produce the energy necessary for basic cellular functions, such as proliferation. Mitochondria are 'dynamic' in that they are constantly undergoing fission and fusion to remain in a functional state throughout the cell cycle, as well as during other vital processes such as energy supply, cellular respiration and programmed cell death. The mitochondrial fission/fusion machinery is involved in generating young mitochondria, while eliminating old, damaged and non-repairable ones. As a result, the organelles change in shape, size and number throughout the cell cycle. Such precise and accurate balance is maintained by the cytoskeletal transporting system via microtubules, which deliver the mitochondrion from one location to another. During the gap phases G and G, mitochondria form an interconnected network, whereas in mitosis and S-phase fragmentation of the mitochondrial network will take place. However, such balance is lost during neoplastic transformation and autoimmune disorders. Several proteins, such as Drp1, Fis1, Kif-family proteins, Opa1, Bax and mitofusins change in activity and might link the mitochondrial fission/fusion events with processes such as alteration of mitochondrial membrane potential, apoptosis, necrosis, cell cycle arrest, and malignant growth. All this indicates how vital proper functioning of mitochondria is in maintaining cell integrity and preventing carcinogenesis.

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