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MAP 0, a 400-kDa mi...
MAP 0, a 400-kDa microtubule-associated protein unique to teleost fish.
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- Modig, C (author)
- Gothenburg University,Göteborgs universitet,Zoologiska institutionen,Department of Zoology
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- Rutberg, M (author)
- Gothenburg University,Göteborgs universitet,Zoologiska institutionen,Department of Zoology
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Detrich, H W (author)
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- Billger, Martin (author)
- Gothenburg University,Göteborgs universitet,Zoologiska institutionen,Department of Zoology
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- Strömberg, E (author)
- Gothenburg University,Göteborgs universitet,Zoologiska institutionen,Department of Zoology
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- Wallin, Margareta, 1952 (author)
- Gothenburg University,Göteborgs universitet,Zoologiska institutionen,Department of Zoology
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(creator_code:org_t)
- 1997
- 1997
- English.
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In: Cell motility and the cytoskeleton. - 0886-1544. ; 38:3, s. 258-69
- Related links:
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https://gup.ub.gu.se...
Abstract
Subject headings
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- Microtubules from neural tissues of the Atlantic cod, Gadus morhua, and of several species of Antarctic teleosts are composed of tubulin and several microtubule-associated proteins (MAPs), one of which has an apparent molecular weight of approximately 400-430 kDa. Because its apparent molecular weight exceeds those of the MAP 1 proteins, we designate this high molecular weight teleost protein MAP 0. Cod MAP 0 failed to cross-react with antibodies specific for MAPs 1A, 1B and 2 of mammalian brain, for MAP H1 of squid optic lobe, and for chicken erythrocyte syncolin, which suggests that it has a novel structure. Similarly, MAP 0 from the Antarctic fish was not recognized by an antibody specific for bovine MAP 2. Together, these observations suggest that MAP 0 is a novel MAP that may be unique to fish. To determine the tissue specificity and phylogenetic distribution of this protein, we generated a rabbit polyclonal antibody against cod MAP 0. Using this antibody, we found that MAP 0 was present in microtubule proteins isolated from cod brain tissues and spinal cord but was absent in microtubules from heart, liver, and spleen. At the subcellular level, MAP 0 was distributed in cod brain cells in a punctate pattern coincident with microtubules but was absent in skin cells. MAP 0 was also detected in cells of the peripheral nervous system. A survey of microtubule proteins from chordates and invertebrates showed that anti-MAP 0-reactive homologs were present in five teleost species but not in more primitive fish and invertebrates or in higher vertebrates. MAP 0 bound to cod microtubules by ionic interaction at a site recognized competitively by bovine MAP 2. Although its function is unknown, MAP 0 does not share the microtubule-binding properties of the motor proteins kinesin and dynein. We propose that MAP 0 is a unique, teleost-specific MAP.
Subject headings
- NATURVETENSKAP -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)
Keyword
- Amphibians
- metabolism
- Animals
- Antibody Specificity
- Cells
- Cultured
- Central Nervous System
- chemistry
- Fishes
- metabolism
- Invertebrates
- metabolism
- Microtubule-Associated Proteins
- isolation & purification
- Molecular Weight
- Organ Specificity
- Peripheral Nervous System
- chemistry
- Phylogeny
- Reptiles
- metabolism
- Species Specificity
- Subcellular Fractions
- chemistry
Publication and Content Type
- ref (subject category)
- art (subject category)
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