Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.4.11.18 (MAP)
 7,412 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

With a rabbit antiserum specific for high molecular weight microtubule-associated proteins (HMW/MAPs: MAP1 and MAP2), centrosomes in interphase and mitotic HeLa cells were visualized by indirect immunofluorescence. Pre-immune serum did not stain a similar organelle. Microtubules were observed to originate from the centrosomes, demonstrating their microtubule organizing (MTOC) function. The MTOC antigen(s) to which the anti-HMW/MAP antiserum reacted was resistant to Colcemid, Triton-X-100, Nonidet P-40 and Brij 35. Immunofluorescence localization of the MTOCs was blocked by pre-incubation of the antiserum with a MAP1--MAP2 preparation but not with tubulin, actin, or a 58 K intermediate filament protein.
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PMID:Localization of high molecular weight microtubule-associated proteins (MAP1 and MAP2) in a HeLa microtubule-organizing centre. 676 Oct 77

By whole-cell transmission electron microscopy (WCTEM), we recently demonstrated that carotenoid droplets are transported by elongating or retracting endoplasmic reticular cisternae in goldfish xanthophores. Here we report that permeabilized xanthophores demonstrate immunogold reactivity against several proteins involved in organelle translocation. The gold labeling against beta-tubulin and the intermediate filament protein p45a were found on microtubules and intermediate filaments. Labeling with anti-actin was found on nonidentifiable structures, on vesicles of unknown origin, occasional labeling on carotenoid droplets, and on occasional microfilaments. Immunoreactivity was demonstrated with anti-p57 on the carotenoid droplet surface, confirming previous results (Lynch et al., 1986a,b). Labeling with anti-PCD6 subunit (of the inositol trisphosphate/ryanodine receptor) was demonstrated on carotenoid droplets suggesting they possess calcium channels. Anti-MAP 1C (dynein) immunolabeling was generally seen on club-shaped structures in the cytomatrix and on carotenoid droplets. Finally, immunogold labeling with anti-MAP 2a + 2b was seen on a meshwork of microfilaments and intermediate filaments. Finally, this is the first report of a WCTEM technique for permeabilized cells that reveals immunoreactive elements, organelles, and cytomatrix components without the additional requirements of extraction or fracturing.
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PMID:Ultrastructural immunogold localization of some organelle-transport relevant proteins in wholemounted permeabilized nonextracted goldfish xanthophores. 765 80

Nestin is one kind of intermediate filament protein, which is considered as a typical marker of neural precursor cells. Considerable evidence supports nestin may have actively functions in neurogenesis and gliosis. Our aim was to investigate nestin expression in the temporal neocortex of patients with intractable epilepsy (IE), and then to discuss the possible role of nestin in IE. Tissue samples from the temporal neocortex of 32 patients who had surgery for IE were used to detect nestin expression by immunohistochemistry, immunofluorescence. We compared these tissues with 12 histologically normal temporal neocortex from intracranial hypertension patients who had decompression procedures. In this study, we found some nestin positive cells in the normal temporal neocortex, but in the intractable epilepsy, they were upregulated, increasing with length of course and seizure frequency. Optical density (OD) value in epileptic tissue was determined 0.246 +/- 0.030, and 0.134 +/- 0.040 in the control (P < 0.05). Double lables of immunofluorescence showed some nestin positive cells coexpression with glial fibrillary acidic protein (GFAP), while some coexpression with microtubule-associated protein-2 (MAP(2)). These findings provided some evidence for increased neurogenesis and gliosis in epilepsy, which could be associated with intractable epilepsy.
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PMID:Nestin in the temporal neocortex of the intractable epilepsy patients. 1871 94

The Arabidopsis thaliana genome encodes about 386 proteins with coiled-coil domains of at least 50 amino acids in length. In mammalian systems, many coiled-coil proteins are part of various cytoskeletal networks including intermediate filament protein, actin-binding proteins and MAP (microtubule-associated proteins). Immunological evidence suggests that some of these cytoskeletal proteins, such as lamins, keratins and tropomyosins, may be conserved in Arabidopsis. However, coiled-coil proteins are of low complexity, and thus, traditional sequence comparison algorithms, such as BLAST may not detect homologies. Here, we use the PROPSEARCH algorithm to detect putative coiled-coil cytoskeletal protein homologues in Arabidopsis. This approach reveals putative intermediate filament protein homologues of filensin, lamin and keratin; putative actin-binding homologues of ERM (ezrin/radixin/moesin), periplakin, utrophin, tropomyosin and paramyosin, and putative MAP homologues of restin/CLIP-170 (cytoplasmic linker protein-170). We suggest that the AtFPP (Arabiopsis thaliana filament-like plant protein) and AtMAP70 (Arabidopsis microtubule-associated protein 70) families of coiled-coil proteins may, in fact, be related to lamins and function as intermediate filament proteins.
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PMID:Putative Arabidopsis homologues of metazoan coiled-coil cytoskeletal proteins. 2128 6