Cells injected with guanosine 5'-[alpha, beta-methylene]triphosphate, an alpha, beta-nonhydrolyzable analog of GTP, show anomalous patterns of tubulin polymerization affecting cell translocation, intracellular movement, and the organization of Golgi elements. 1983

J Wehland, and I V Sandoval

Injection of the alpha, beta-nonhydrolyzable GTP analog, guanosine 5'-[alpha, beta-methylene]triphosphate (pp[CH2]pG) into PtK2, A549, and Swiss 3T3 cells produced dramatic changes in the normal pattern of long radiating microtubules displayed by the cells before injection. Injection of pp[CH2]pG into cells growing in normal medium resulted in the formation of microtubule bundles resistant to depolymerization by Colcemid and calcium. Cells injected with pp[CH2]pG after incubation with Colcemid for 2 hr showed polymerization of tubulin into long wavy ribbons within 2 hr after injection. Removal of Colcemid 1 hr after the injection of pp[CH2]pG resulted in assembly of tubulin into short single randomly oriented microtubules. All cells injected with pp[CH2]pG showed impeded translocation and restriction or absence of intracellular movement. pp[CH2]pG also prevented the fragmentation of Golgi elements in A549 cells treated with Colcemid. Cells first treated with Colcemid and then injected with pp[CH2]pG failed to reassemble the Golgi elements after the removal of Colcemid. Cells in intimate membrane contact with cells injected with pp[CH2]pG showed similar changes in microtubule polymerization, cell movement, and organization of Golgi elements.

UI MeSH Term Description Entries
D008870 Microtubules Slender, cylindrical filaments found in the cytoskeleton of plant and animal cells. They are composed of the protein TUBULIN and are influenced by TUBULIN MODULATORS. Microtubule
D011485 Protein Binding The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments. Plasma Protein Binding Capacity,Binding, Protein
D002465 Cell Movement The movement of cells from one location to another. Distinguish from CYTOKINESIS which is the process of dividing the CYTOPLASM of a cell. Cell Migration,Locomotion, Cell,Migration, Cell,Motility, Cell,Movement, Cell,Cell Locomotion,Cell Motility,Cell Movements,Movements, Cell
D002478 Cells, Cultured Cells propagated in vitro in special media conducive to their growth. Cultured cells are used to study developmental, morphologic, metabolic, physiologic, and genetic processes, among others. Cultured Cells,Cell, Cultured,Cultured Cell
D006056 Golgi Apparatus A stack of flattened vesicles that functions in posttranslational processing and sorting of proteins, receiving them from the rough ENDOPLASMIC RETICULUM and directing them to secretory vesicles, LYSOSOMES, or the CELL MEMBRANE. The movement of proteins takes place by transfer vesicles that bud off from the rough endoplasmic reticulum or Golgi apparatus and fuse with the Golgi, lysosomes or cell membrane. (From Glick, Glossary of Biochemistry and Molecular Biology, 1990) Golgi Complex,Apparatus, Golgi,Complex, Golgi
D006160 Guanosine Triphosphate Guanosine 5'-(tetrahydrogen triphosphate). A guanine nucleotide containing three phosphate groups esterified to the sugar moiety. GTP,Triphosphate, Guanosine
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D014404 Tubulin A microtubule subunit protein found in large quantities in mammalian brain. It has also been isolated from SPERM FLAGELLUM; CILIA; and other sources. Structurally, the protein is a dimer with a molecular weight of approximately 120,000 and a sedimentation coefficient of 5.8S. It binds to COLCHICINE; VINCRISTINE; and VINBLASTINE. alpha-Tubulin,beta-Tubulin,delta-Tubulin,epsilon-Tubulin,gamma-Tubulin,alpha Tubulin,beta Tubulin,delta Tubulin,epsilon Tubulin,gamma Tubulin

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J Wehland, and I V Sandoval
October 1977, Life sciences,
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