Serotonin binds specifically and saturably to an actin-like protein isolated from rat brain synaptosomes.

Small, David H.; Wurtman, Richard J.

doi:10.1073/pnas.81.3.959

Cited by 15 publications

(18 citation statements)

References 33 publications

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“…At 37"C, dissociation of 3H from the protein was biphasic, with apparent half-lives for each phase of about 1.5 and 32 min. This biphasic dissociation was consistent with the previous finding (Small and Wurtman, 1984) that actin contains both high-affinity and low-affinity binding sites for 5-HT; the biphasic dissociation of 5-HT observed in the present study may reflect different dissociation rates from the two sites. At 4"C, the 5-HT-G-actin complex was relatively stable over the incubation period ( Fig.…”

Section: Kinetic Studiessupporting

confidence: 93%

“…T h e 5 -H T binding a s s a y and liquid scintillation counting procedures have been de5cribed previously (Small and Wurtman, 1984). For equilibrium binding studies on G-actin, all incubations were performed in buffer A at 37°C for 1 h. Actin concentrations were determined spectrophotometrically by the method of Houk and Ue (1974).…”

Section: Other Proceduresmentioning

confidence: 99%

“…MATERIALS AND METHODS mine (5-HT, serotonin) binds to an actin-like protein that we partially purified from rat brain synapto-SomeS (Small and Wurtman, 1984 Purification of actin C r u d e G-actin w a s prepared from rabbit skeletal muscle by the method of Spudich and Watt (1971). As this preparation was not sufficiently pure for binding studies, further purification was achieved by a second cycle of polymerization-depolymerization (Pardee and Spudich.…”

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confidence: 99%

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Binding of [³H]Serotonin to Skeletal Muscle Actin

Small

Wurtman

1985

Journal of Neurochemistry

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We previously observed that the neurotransmitter 5-hydroxytryptamine (5-HT, serotonin) binds with high- and low-affinity interactions to an actin-like protein prepared from rat brain synaptosomes. In this study, we examined its binding to highly purified actin obtained from rabbit skeletal muscle. Monomeric G-actin bound serotonin with high and low affinities, exhibiting equilibrium dissociation constants (KD values) of 5 X 10(-5) M and 4 X 10(-3) M, respectively. The serotonin binding site on actin was distinct from those sites previously characterized for divalent cations, nucleotides, and cytochalasin alkaloids. The binding of serotonin (1 microM) to G-actin was increased as much as 26-fold by divalent cations. Potassium iodine (KI) increased the affinity of G-actin for serotonin, KD values for this binding being 3 X 10(-7) M and X 10(-5) M. Serotonin bound with even higher affinity to polymerized F-actin, with KD values of 2 X 10(-8) M and 2 X 10(-5) M. However, the total number of binding sites on F-actin was only about 4% of the number of G-actin. The binding of serotonin (0.1 microM) to G-actin could be inhibited by phenothiazines (1 microM) or reserpine (10 microM), but not by classical antagonists of serotonin receptors or by drugs that release serotonin or inhibit its uptake. The binding of serotonin to actin in vivo may participate in a contractile process related to neurotransmitter release.

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Section: Kinetic Studiessupporting

confidence: 93%

Section: Other Proceduresmentioning

confidence: 99%

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confidence: 99%

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Binding of [³H]Serotonin to Skeletal Muscle Actin

Small

Wurtman

1985

Journal of Neurochemistry

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“…These results agree with those of Benitez-King et al [ 19901 and Benitez-King and Anton-Tay [1993], who proposed that melatonin may play a role in cytoskeletal rearrangements through its calmodulin antagonism. These data and the fact that serotonin binds directly to actin [Small and Wurtman, 1984;Alexander, et al, 19871, suggest that melatonin could promote cytoskeletal modifications either by binding to actin, or actin-associated cytoskeletal proteins.…”

Section: Effects Of Melatonin On Dna Synthesismentioning

confidence: 97%

Intracellular melatonin distribution in cultured cell lines

Finocchiaro

Glikin

1998

Journal of Pineal Research

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A specific antibody combined with a fluorescein-labeled immunoglobulin was used to investigate the topographic distribution of melatonin in a variety of cells of different origins. Positive identification of both nuclear and cytosolic melatonin was confirmed in all the tested cells: Swiss 3T3 mouse fibroblasts, BCG1 bovine granulosa, NB41A3 mouse neuroblastoma, F9 mouse teratocarcinoma, MDCK normal canine kidney derived and human HeLa cell lines, as well as in human peripheral blood mononuclear leukocytes and rat splenic cells. In 3T3 mouse fibroblasts melatonin immunofluorescence partially colocalized with actin and serotonin immunostaining, but not with tubulin or actin stress fibers. Several distinct patterns of subcellular melatonin distribution, different from the bromodeoxyuridine-labeled replication profiles, have been discerned throughout the cell cycle of synchronized 3T3 cells. In addition, synchronized 3T3 mouse fibroblasts cultured in the presence of 10(-3) M melatonin progressed more slowly through the cell cycle than control cells. These results suggest that melatonin may interact directly with nuclear and cytoskeletal structures probably affecting different cell functions such as cell cycle control, subcellular organization, and genome stability.

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“…Alteration of intracellular 5-HT during morphogenesis causes the formation of aberrant microvilli and deficiencies in cellular morphogenesis, resulting in neural tube defects [131]. 5-HT also promotes in vitro contractile activity of oligodendrocytes [132] and binds specifically and saturably to an actin-like protein extracted from rat brain synaptosomes [133]. These various observations suggest a 5-HT effect on the cytoskeletal system.…”

Section: Serotonin As An Early Regulatory Factor In Cns Development Amentioning

confidence: 99%

Embryonal central neuroepithelial tumors: Current concepts and future challenges

Herman

Rubinstein

1987

Cancer Metast Rev

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While the embryonal central neuroepithelial tumors present complex conceptual and clinical problems, advances in cell type identification by special neurohistological, immunohisto- and immunocytochemical techniques have permitted discrimination of distinct cytomorphogenetic entities. These are based in part on their resemblance to the normal phases of neurocytogenesis. Four of these tumors, medulloepithelioma, desmoplastic infantile ganglioglioma, pineoblastoma and medulloblastoma, are designated as multipotential in light of their capacity to undergo divergent differentiation. Cytomorphogenetic, clinical and experimental data implicate fetal neural cell targets for transformation and raise the possibility that aberrant developmental regulatory mechanisms may contribute to the biologic behavior of these tumors. Growth factors and some neuroregulatory neurotransmitters (such as serotonin) are known to act as modulators of normal neuromorphogenesis. They could play a regulatory role in central neuroepithelial tumors on the hypothesis that the aberrant behavior of the embryonal neoplasms could either be modified by functional receptor responses or result from abnormal receptor responses to these substances. Future challenges include the definition of new cytomorphogenetic entities and subgroups of the currently defined forms of embryonal CNS tumors based on the presence of specific growth factors and neuroregulatory neurotransmitters, or their receptors, the characterization of neoplastic receptor responses mediating any modulatory role of the presently known growth factors or neuroregulatory neurotransmitters on the growth and maturation potential of the embryonal central neuroepithelial tumors and the further definition of developmental, stage-specific modulators that might be operative in these tumors.

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Serotonin binds specifically and saturably to an actin-like protein isolated from rat brain synaptosomes.

Cited by 15 publications

References 33 publications

Binding of [³H]Serotonin to Skeletal Muscle Actin

Binding of [³H]Serotonin to Skeletal Muscle Actin

Intracellular melatonin distribution in cultured cell lines

Embryonal central neuroepithelial tumors: Current concepts and future challenges

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Serotonin binds specifically and saturably to an actin-like protein isolated from rat brain synaptosomes.

Cited by 15 publications

References 33 publications

Binding of [3H]Serotonin to Skeletal Muscle Actin

Binding of [3H]Serotonin to Skeletal Muscle Actin

Intracellular melatonin distribution in cultured cell lines

Embryonal central neuroepithelial tumors: Current concepts and future challenges

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Product

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Binding of [³H]Serotonin to Skeletal Muscle Actin

Binding of [³H]Serotonin to Skeletal Muscle Actin