A novel chemotaxis regulating enzyme that splits folic acid into 6‐hydroxymethylpterin and <i>P</i>‐aminobenzoylglutamic acid

Kakebeeke, P I; Wit, René J.W. de; Konijn, Theo M.

doi:10.1016/0014-5793(80)81172-0

Cited by 14 publications

(13 citation statements)

References 24 publications

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“…These results contrast with those in [4] report that cytoplasmic extracts of D. discoidal inactivated the chemoattractant activity of folic acid. However, cellular slime molds may have other ways of inactivating folic acid as a chemoattractant besides deamination [6].…”

Section: Cell Fractionationmentioning

confidence: 99%

Control of folate deaminase activity of Dictyostelium discoideum by cyclic AMP

Bernstein

Driel

1980

FEBS Letters

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Section: Cell Fractionationmentioning

confidence: 99%

Control of folate deaminase activity of Dictyostelium discoideum by cyclic AMP

Bernstein

Driel

1980

FEBS Letters

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“…As noted above, stimulation of vegetative cells with folate causes the transient rise of intracellular cGMP [39,43]. There is a degradative enzyme associated with the folate chemotactic system, a folate (or pterin) deaminase (8) that has a similar cellular distribution [44,45] and other properties to those of the PDE [Frazier et al, unpublished]. As expected, a receptor for folate and its analogs is present on the surface of vegetative cells [46,47].…”

Section: Vegetative Chemotaxis Of D Discoideiummentioning

confidence: 74%

“…Like the cAMP chemotactic system, the components of this folate chemotactic system include a degradative enzyme, in this case a folate deaminase [8,44,45]. We have undertaken studies of this enzyme with the aim of controlling its activity so that radioligand binding assays of the chemotactic receptor can be performed in the absence of ligand degradation.…”

Section: The Folate Chemotactic System Folate Deaminasementioning

confidence: 99%

Chemotactic Receptors of Dictyostelium discoideum

Frazier

Nandini-Kishore

Meyers

1982

J of Cellular Biochemistry

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For over 30 years, the cellular slime molds, and in particular the species Dictyostelium discoideum, have been viewed as a eukaryotic model system for the study of a variety of regulatory and developmental processes [l]. In particular, the transition from the free-living amoeboid stage to the multicellular slug stage has been the focus of a great deal of attention by those investigators studying the regulation of development [ 1-31. The first morphological evidence that differentiation of a starved population of cells is proceeding on schedule is the appearance of ripples or streams in a lawn of cells resting on a moist surface [l-31. This prelude to the readily identified tight aggregate stage indicates the functioning of the cells' endogenous chemosensory system. In 1969, Bonner and coworkers [4] identified the endogenously produced chemoattractant or acrasin of these cells as cyclic AMP (CAMP). While cAMP is widely encountered as an intracellular regulatory agent or second messenger, the Dictyostelia provide one of the few well documented examples of cAMP as an extracellular messenger molecule.The Polysphondylia such as P violaceum and P pallidum appear to employ a nonnucleotide molecule as their acrasin during starvation induced chemotaxis. This compound has been studied by Bonner and coworkers [S] and has been tentatively identified as a peptide with a blocked amino terminus, although further characterization is required for unambiguous identification. Bonner's group has also been responsible for the identification of folic acid and pterin compounds as chemoattractants of vegetative Dictyostelium amoebae [6-81. This identification of a nonacrasin chemoattractant raises the possibility of studying the transition from a vegetative to a developmental mode of chemotaxis. DEVELOPMENTAL CHEMOTAXIS IN D discoideumThe phenomenology of the CAMP chemotactic system in D discoideum has been well established [9,10]. It is convenient for descriptive purposes to imagine

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“…Two enzymes acting on folic acid [ 1 ] were evi. denced in the extracellular medium of Dictyostelium cells, a 2-folate deaminase [12] and a C9-N10 splitting enzyme [13], supposed to inactivate folic acid as chernio-attractant. However, the 2-folate deaminase activity and location have been followed during development: it mimics cAMP phosphodiesterase in its regulatory function [ 14,15].…”

Section: Discussionmentioning

confidence: 99%