Latrunculin

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Latrunculin
Latrunculin A structure.svg
Latrunculin A
Latrunculin B.svg
Latrunculin B
Identifiers
3D model (JSmol)
ChEBI
ChEMBL
DrugBank
PubChem CID
UNII
  • A:InChI=1S/C22H31NO5S/c1-15-7-5-3-4-6-8-16(2)11-20(24)27-18-12-17(10-9-15)28-22(26,13-18)19-14-29-21(25)23-19/h3-5,7,11,15,17-19,26H,6,8-10,12-14H2,1-2H3,(H,23,25)/b4-3+,7-5-,16-11-/t15-,17-,18-,19+,22-/m1/s1
    Key: DDVBPZROPPMBLW-IZGXTMSKSA-N
  • B:InChI=1S/C20H29NO5S/c1-13-5-3-4-6-14(2)9-18(22)25-16-10-15(8-7-13)26-20(24,11-16)17-12-27-19(23)21-17/h3,5,9,13,15-17,24H,4,6-8,10-12H2,1-2H3,(H,21,23)/b5-3-,14-9-/t13-,15-,16-,17+,20-/m1/s1
    Key: NSHPHXHGRHSMIK-JRIKCGFMSA-N
  • A:C[C@H]/1CC[C@@H]2C[C@H](C[C@@](O2)([C@@H]3CSC(=O)N3)O)OC(=O)/C=C(\CC/C=C/C=C1)/C
  • B:C[C@H]/1CC[C@@H]2C[C@H](C[C@@](O2)([C@@H]3CSC(=O)N3)O)OC(=O)/C=C(\CC/C=C1)/C
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa).

The latrunculins are a family of natural products and toxins produced by certain sponges, including genus Latrunculia and Negombata , whence the name is derived. It binds actin monomers near the nucleotide binding cleft with 1:1 stoichiometry and prevents them from polymerizing. Administered in vivo, this effect results in disruption of the actin filaments of the cytoskeleton, and allows visualization of the corresponding changes made to the cellular processes. This property is similar to that of cytochalasin, but has a narrow effective concentration range. [1] Latrunculin has been used to great effect in the discovery of cadherin distribution regulation and has potential medical applications. [2] Latrunculin A, a type of the toxin, was found to be able to make reversible morphological changes to mammalian cells by disrupting the actin network. [3]

Contents

Latrunculin A:

Molecular Formula:C22H31NO5S [4]
Molecular Weight:421.552 g/mol [4]

Target and functions

Gelsolin - Latrunculin A causes end- blocking; this protein binds to the barbed sides of the actin filaments which accelerates nucleation. This calcium-regulated protein also plays a role in assembly and disassembly of cilia [4] which plays a crucial role in handedness.

Latrunculin B:

Molecular Formula:C20H29NO5S[4]
Molecular Weight:395.514 g/mol

Target and Function

Actin- Latrunculin B makes up the structure of the actin fibers.

Protein spire homolog 2- needed for cell division, vesicle transport within the actin filament and is essential for the formation of the cleavage formation during cell division[4].

History

Latrunculin is a toxin that is produced by sponges. The red-coloured Latrunculia Magnifica Keller is an abundant sponge in the gulf of Eilat and the gulf of Suez [5] in the red sea, where it lives at a depth of 6–30 meters. [6] The toxin was discovered around 1970. Researchers observed that the red-coloured sponges, Latrunculia Magnifica Keller, were never damaged or eaten by fishes, while others were. Furthermore, when researchers squeezed the sponges in the sea, they observed that a red fluid came out. Fishes nearby immediately fled the surrounding area when the sponge secreted the fluid. These were the first indications that these sponges produced a toxin. Later this hypothesis was confirmed by squeezing the sponge in an aquarium with fish, whereupon the fish showed a loss of balance and severe bleeding, dying within only 4–6 minutes. [6] Similar effects were observed when the toxin was injected in mice.

Latrunculin makes up to 0.35% of the dry weight of the sponge. [5] There are two main forms of the toxin, A and B. Latrunculin A is only present in sponges which live in the gulf of Suez while latrunculin B only exist in sponges in the gulf of Eilat. Why this is the case is still under investigation. [5]

Structure

Figure 2 relative activity of Latrunculin analogues The micro filament disrupting activity (at 10 mM effective concentration). Abbreviations: +- weak effect, + significant effect, ++ strong effect, +++ very strong effect (less than 20% viable cells). Activity of latrunculin analogues.gif
Figure 2 relative activity of Latrunculin analogues The micro filament disrupting activity (at 10 μM effective concentration). Abbreviations: ± weak effect, + significant effect, ++ strong effect, +++ very strong effect (less than 20% viable cells).

There are several isomers of latrunculin, A, B, C, D, G, H, M, S and T. The most common structures are latrunculin A and B. Their formulas are respectively C22H31NO5S and C20H29NO5S. The macrolactone ring on top that contains double bonds is a structural feature of the latrunculin molecules. The side chain contains an acylthiazolidinone substitute. Besides these natural occurring forms, scientist have made synthetic forms with different toxic strengths. Figure 2 shows some of these forms with their relative ability to disrupt microfilament activity. Semisynthetic forms that contained N-alkylated derivates were inactive. [7]

Mechanism of action

Latrunculin A and latrunculin B affect polymerization of actin. Latrunculin binds actin monomers near the nucleotide binding cleft with 1:1 stoichiometry and prevents them from polymerizing. [1] The nucleotide monomers are prevented from dissociation from the nucleotide binding cleft, thus preventing polymerizing. [8]

Experimental evidence shows that latruculin-A is biologically active in the solvent DMSO, but not in aqueous solutions, as demonstrated in cell culture and in brain tissue [9] probably due to cellular permeation.

When actin is impaired due to latrunculin, Shiga toxins have a better chance of infiltrating the intestinal epithelial monolayer in E. coli, which may cause a higher chance of generating gastrointestinal illnesses. [10]

It seems that actin monomers are more sensitive to bind latrunculin A than to bind Latrunculin B. [11] In other words, latrunculin A is a more potent toxin. Latrunculin B is inactivated faster than latrunculin A. [12]

The prevention of polymerizing of the actin filaments causes reversible changes in the morphology of mammalian cells. [13] Lantranculin interferes with the structure of the cytoskeleton in rats. [14]

After latrunculin B exposure, mouse fibroblasts grow bigger and PtK2 kidney cells from a potoroo stem produced long, branched extensions. [15] The extensions seem to be an accumulation of actin monomers.

Metabolism

Yeast cells in absence of the proteins osh3 or osh5 demonstrated hypersensitivity to latrunculin B. [16] The osh proteins are homologous to OSBP generated enzymes that appear in mammals, indicating that these might play a role in the toxicokinetics of latrunculins.

Yeast mutants that are resistant to latrunculin show a mutation, D157E, that initiates a hydrogen bond with latrunculin. [8] Other yeast mutants adjust the binding site, thus making it resistant to latrunculin.

No research has been done to figure out how the biotransformation of latrunculin works in eukaryotic cells. However, research suggests that it is the unaltered form of latrunculin that causes toxic effects. [3]

Toxicity

As latrunculin inhibits actin polymerization and actomyosin contractile ability, exposure to latrunculin may result in cellular relaxation, expansion of drainage tissues and decreased outflow resistance in e.g. the trabecular meshwork.

Plant

Latrunculin B causes marked and dose-dependent reductions in pollen germination frequency and pollen tube growth rate. [17]

Adding latrunculin B to solutions of pollen F-actin produced a rapid decrease in the total amount of polymer, the extent of depolymerization increasing with the concentrations of the toxic. The concentration of latrunculin B required for half-maximal inhibition of pollen germination is 40 to 50 nM, whereas pollen tube extension is much more sensitive, requiring only 5 to 7 nM LATB for half-maximal inhibition. The disruption of germination and pollen tube growth by latrunculin B is partially reversible at low concentrations. (<30 nM). [17]

Animal

Squeezing Latrunculia magnifica into aquarium with fishes causes their almost immediate agitation, followed by hemorrhage, loss of balance and death in 4–6 minutes. [18]

Latrunculin A has been used as acrosome reaction inhibitor of guinea pig in laboratory conditions. [19]

Human

Lat-A-induces reduction of actomyosin contractility. This is associated with trabecular meshwork porous expansion without evidence of reduced structural extracellular matrix protein expression or cellular viability. [20] In high doses, latrunculin can induce acute cell injury and programmed cell death through activating the caspase-3/7 pathway. [18]

Lethal doses

TDLO - Lowest Published Toxic Dose

LD50 – median Lethal Dose [21]

IndicatorSpeciesDose
Oral TDLOMan1,14 ml/kg, 650 mg/kg
Oral LD50Rat7,06 mg/kg
Oral LD50Mouse3,45 g/kg, 10,5 ml/kg
Oral LD50Rabbit6,30 mg/kg
Inhalation LC50Rat6h: 5,900 mg/m3

10h: 20,000 ppm

Inhalation LCLOMouse7h: 29,300 ppm
Inhalation TCLOHuman20m: 2,500 mg/m3

30m: 1,800 ppm

Irritation eyesRabbit24h: 500 mg
Irritation skinRabbit24h: 20 mg

Applications

In nature, latrunculins are used by the sponges themselves as a defense mechanism, and for the same purpose are also sequestered by certain nudibranchs. [22]

Latrunculins are produced for fundamental research and have potential medical applications as latrunculins and their derivatives show antiangionic, antiproliferative, antimicrobial and antimetastatic activities. [2]

Defense mechanism

Like many other sessile organisms, sponges are rich of secondary metabolites with toxic properties and most of them, including Latrunculin, have a defense role against predators, competitors and epibionts. [23]

The sponges themselves are not damaged by latrunculin. As a measure against self-toxination, they keep the latrunculin in membrane-bound vacuoles, that also function as secretory and storage vesicles. These vacuoles are free of actin and prevent the latrunculin from entering the cytosol where it would damage actin. [23] After production in the choanocytes, the latrunculin is transferred via the archeocytes to the vulnerable areas of the sponges where defense is needed, such as injured or regenerating sites. [23]

Sequestering by nudibranchs

Sea slugs of the genus Chromodoris sequester different toxics from the sponges that they eat as defensive metabolites, including latrunculin. They selectively transfer and store latrunculin in the sites of the mantle that are most exposed to potential predators. [22] It is thought that the digestive system of the nudibranchs plays an important role in the detoxification. [22]

In 2015, the discovery that five closely related sea slugs of the genus Chromodoris all use latrunculin as defense, indicates that the toxic might be used via Müllerian mimicry. [22]

Related Research Articles

<span class="mw-page-title-main">Microfilament</span> Filament in the cytoplasm of eukaryotic cells

Microfilaments, also called actin filaments, are protein filaments in the cytoplasm of eukaryotic cells that form part of the cytoskeleton. They are primarily composed of polymers of actin, but are modified by and interact with numerous other proteins in the cell. Microfilaments are usually about 7 nm in diameter and made up of two strands of actin. Microfilament functions include cytokinesis, amoeboid movement, cell motility, changes in cell shape, endocytosis and exocytosis, cell contractility, and mechanical stability. Microfilaments are flexible and relatively strong, resisting buckling by multi-piconewton compressive forces and filament fracture by nanonewton tensile forces. In inducing cell motility, one end of the actin filament elongates while the other end contracts, presumably by myosin II molecular motors. Additionally, they function as part of actomyosin-driven contractile molecular motors, wherein the thin filaments serve as tensile platforms for myosin's ATP-dependent pulling action in muscle contraction and pseudopod advancement. Microfilaments have a tough, flexible framework which helps the cell in movement.

<span class="mw-page-title-main">Actin</span> Family of proteins

Actin is a family of globular multi-functional proteins that form microfilaments in the cytoskeleton, and the thin filaments in muscle fibrils. It is found in essentially all eukaryotic cells, where it may be present at a concentration of over 100 μM; its mass is roughly 42 kDa, with a diameter of 4 to 7 nm.

<span class="mw-page-title-main">Phalloidin</span> Chemical compound

Phalloidin belongs to a class of toxins called phallotoxins, which are found in the death cap mushroom (Amanita phalloides). It is a rigid bicyclic heptapeptide that is lethal after a few days when injected into the bloodstream. The major symptom of phalloidin poisoning is acute hunger due to the destruction of liver cells. It functions by binding and stabilizing filamentous actin (F-actin) and effectively prevents the depolymerization of actin fibers. Due to its tight and selective binding to F-actin, derivatives of phalloidin containing fluorescent tags are used widely in microscopy to visualize F-actin in biomedical research.

<span class="mw-page-title-main">Cytochalasin B</span> Chemical compound

Cytochalasin B, the name of which comes from the Greek cytos (cell) and chalasis (relaxation), is a cell-permeable mycotoxin. It was found that substoichiometric concentrations of cytochalasin B (CB) strongly inhibit network formation by actin filaments. Due to this, it is often used in cytological research. It inhibits cytoplasmic division by blocking the formation of contractile microfilaments. It inhibits cell movement and induces nuclear extrusion. Cytochalasin B shortens actin filaments by blocking monomer addition at the fast-growing end of polymers. Cytochalasin B inhibits glucose transport and platelet aggregation. It blocks adenosine-induced apoptotic body formation without affecting activation of endogenous ADP-ribosylation in leukemia HL-60 cells. It is also used in cloning through nuclear transfer. Here enucleated recipient cells are treated with cytochalasin B. Cytochalasin B makes the cytoplasm of the oocytes more fluid and makes it possible to aspirate the nuclear genome of the oocyte within a small vesicle of plasma membrane into a micro-needle. Thereby, the oocyte genome is removed from the oocyte, while preventing rupture of the plasma membrane.

<span class="mw-page-title-main">Tropomyosin</span> Protein

Tropomyosin is a two-stranded alpha-helical, coiled coil protein found in many animal and fungal cells. In animals, it is an important component of the muscular system which works in conjunction with troponin to regulate muscle contraction. It is present in smooth and striated muscle tissues, which can be found in various organs and body systems, including the heart, blood vessels, respiratory system, and digestive system. In fungi, tropomyosin is found in cell walls and helps maintain the structural integrity of cells.

<span class="mw-page-title-main">Profilin</span> Actin-binding protein

Profilin is an actin-binding protein involved in the dynamic turnover and reconstruction of the actin cytoskeleton. It is found in most eukaryotic organisms. Profilin is important for spatially and temporally controlled growth of actin microfilaments, which is an essential process in cellular locomotion and cell shape changes. This restructuring of the actin cytoskeleton is essential for processes such as organ development, wound healing, and the hunting down of infectious intruders by cells of the immune system.

<span class="mw-page-title-main">ADF/Cofilin family</span> Family of actin-binding proteins

ADF/cofilin is a family of actin-binding proteins associated with the rapid depolymerization of actin microfilaments that give actin its characteristic dynamic instability. This dynamic instability is central to actin's role in muscle contraction, cell motility and transcription regulation.

Cytochalasins are fungal metabolites that have the ability to bind to actin filaments and block polymerization and the elongation of actin. As a result of the inhibition of actin polymerization, cytochalasins can change cellular morphology, inhibit cellular processes such as cell division, and even cause cells to undergo apoptosis. Cytochalasins have the ability to permeate cell membranes, prevent cellular translocation and cause cells to enucleate. Cytochalasins can also have an effect on other aspects of biological processes unrelated to actin polymerization. For example, cytochalasin A and cytochalasin B can also inhibit the transport of monosaccharides across the cell membrane, cytochalasin H has been found to regulate plant growth, cytochalasin D inhibits protein synthesis and cytochalasin E prevents angiogenesis.

<span class="mw-page-title-main">Protein filament</span> Long chain of protein monomers

In biology, a protein filament is a long chain of protein monomers, such as those found in hair, muscle, or in flagella. Protein filaments form together to make the cytoskeleton of the cell. They are often bundled together to provide support, strength, and rigidity to the cell. When the filaments are packed up together, they are able to form three different cellular parts. The three major classes of protein filaments that make up the cytoskeleton include: actin filaments, microtubules and intermediate filaments.

<span class="mw-page-title-main">Cytochalasin D</span> Chemical compound

Cytochalasin D is a member of the class of mycotoxins known as cytochalasins. Cytochalasin D is an alkaloid produced by Helminthosporium and other molds.

<span class="mw-page-title-main">Tropomodulin</span>

Tropomodulin (TMOD) is a protein which binds and caps the minus end of actin, regulating the length of actin filaments in muscle and non-muscle cells.

<span class="mw-page-title-main">Cortactin</span> Protein found in humans

Cortactin is a monomeric protein located in the cytoplasm of cells that can be activated by external stimuli to promote polymerization and rearrangement of the actin cytoskeleton, especially the actin cortex around the cellular periphery. It is present in all cell types. When activated, it will recruit Arp2/3 complex proteins to existing actin microfilaments, facilitating and stabilizing nucleation sites for actin branching. Cortactin is important in promoting lamellipodia formation, invadopodia formation, cell migration, and endocytosis.

CapZ, also known as CAPZ, CAZ1 and CAPPA1, is a capping protein that caps the barbed end of actin filaments in muscle cells.

<span class="mw-page-title-main">Actin, cytoplasmic 2</span> Protein-coding gene in the species Homo sapiens

Actin, cytoplasmic 2, or gamma-actin is a protein that in humans is encoded by the ACTG1 gene. Gamma-actin is widely expressed in cellular cytoskeletons of many tissues; in adult striated muscle cells, gamma-actin is localized to Z-discs and costamere structures, which are responsible for force transduction and transmission in muscle cells. Mutations in ACTG1 have been associated with nonsyndromic hearing loss and Baraitser-Winter syndrome, as well as susceptibility of adolescent patients to vincristine toxicity.

<span class="mw-page-title-main">Vasodilator-stimulated phosphoprotein</span> Mammalian protein found in Homo sapiens

Vasodilator-stimulated phosphoprotein is a protein that in humans is encoded by the VASP gene.

<span class="mw-page-title-main">Actin assembly-inducing protein</span>

The Actin assembly-inducing protein (ActA) is a protein encoded and used by Listeria monocytogenes to propel itself through a mammalian host cell. ActA is a bacterial surface protein comprising a membrane-spanning region. In a mammalian cell, the bacterial ActA interacts with the Arp2/3 complex and actin monomers to induce actin polymerization on the bacterial surface generating an actin comet tail. The gene encoding ActA is named actA or prtB.

Actin remodeling is the biochemical process that allows for the dynamic alterations of cellular organization. The remodeling of actin filaments occurs in a cyclic pattern on cell surfaces and exists as a fundamental aspect to cellular life. During the remodeling process, actin monomers polymerize in response to signaling cascades that stem from environmental cues. The cell's signaling pathways cause actin to affect intracellular organization of the cytoskeleton and often consequently, the cell membrane. Again triggered by environmental conditions, actin filaments break back down into monomers and the cycle is completed. Actin-binding proteins (ABPs) aid in the transformation of actin filaments throughout the actin remodeling process. These proteins account for the diverse structure and changes in shape of Eukaryotic cells. Despite its complexity, actin remodeling may result in complete cytoskeletal reorganization in under a minute.

<span class="mw-page-title-main">Rho-associated protein kinase</span>

Rho-associated protein kinase (ROCK) is a kinase belonging to the AGC family of serine-threonine specific protein kinases. It is involved mainly in regulating the shape and movement of cells by acting on the cytoskeleton.

<span class="mw-page-title-main">MDia1</span> Protein

mDia1 is a member of the protein family called the formins and is a Rho effector. It is the mouse version of the diaphanous homolog 1 of Drosophila. mDia1 localizes to cells' mitotic spindle and midbody, plays a role in stress fiber and filopodia formation, phagocytosis, activation of serum response factor, formation of adherens junctions, and it can act as a transcription factor. mDia1 accelerates actin nucleation and elongation by interacting with barbed ends of actin filaments. The gene encoding mDia1 is located on Chromosome 18 of Mus musculus and named Diap1.

<span class="mw-page-title-main">Cytoskeletal drugs</span> Substances or medications that interact with actin or tubulin

Cytoskeletal drugs are small molecules that interact with actin or tubulin. These drugs can act on the cytoskeletal components within a cell in three main ways. Some cytoskeletal drugs stabilize a component of the cytoskeleton, such as taxol, which stabilizes microtubules, or Phalloidin, which stabilizes actin filaments. Others, such as Cytochalasin D, bind to actin monomers and prevent them from polymerizing into filaments. Drugs such as demecolcine act by enhancing the depolymerisation of already formed microtubules. Some of these drugs have multiple effects on the cytoskeleton: for example, Latrunculin both prevents actin polymerization as well as enhancing its rate of depolymerization. Typically the microtubule targeting drugs can be found in the clinic where they are used therapeutically in the treatment of some forms of cancer. As a result of the lack of specificity for specific type of actin, the use of these drugs in animals results in unacceptable off-target effects. Despite this, the actin targeting compounds are still useful tools that can be used on a cellular level to help further our understanding of how this complex part of the cells' internal machinery operates. For example, Phalloidin that has been conjugated with a fluorescent probe can be used for visualizing the filamentous actin in fixed samples.

References

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  13. ↑ Pendleton A, Koffer A (January 2001). "Effects of latrunculin reveal requirements for the actin cytoskeleton during secretion from mast cells". Cell Motility and the Cytoskeleton. 48 (1): 37–51. doi:10.1002/1097-0169(200101)48:1<37::aid-cm4>3.0.co;2-0. PMID   11124709.
  14. ↑ Yarmola EG, Somasundaram T, Boring TA, Spector I, Bubb MR (September 2000). "Actin-latrunculin A structure and function. Differential modulation of actin-binding protein function by latrunculin A". The Journal of Biological Chemistry. 275 (36): 28120–7. doi: 10.1074/jbc.m004253200 . PMID   10859320.
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  18. 1 2 Konishi H, Kikuchi S, Ochiai T, Ikoma H, Kubota T, Ichikawa D, Fujiwara H, Okamoto K, Sakakura C, Sonoyama T, Kokuba Y, Sasaki H, Matsui T, Otsuji E (June 2009). "Latrunculin a has a strong anticancer effect in a peritoneal dissemination model of human gastric cancer in mice". Anticancer Research. 29 (6): 2091–7. PMID   19528469.
  19. ↑ Roa-Espitia AL, Hernández-Rendón ER, Baltiérrez-Hoyos R, Muñoz-Gotera RJ, Cote-Vélez A, Jiménez I, González-Márquez H, Hernández-González EO (September 2016). "Focal adhesion kinase is required for actin polymerization and remodeling of the cytoskeleton during sperm capacitation". Biology Open. 5 (9): 1189–99. doi:10.1242/bio.017558. PMC   5051654 . PMID   27402964.
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  21. ↑ Cayman chemical (2017). "SAFETY DATA SHEET Latrunculin A" (PDF).
  22. 1 2 3 4 Cheney KL, White A, Mudianta IW, Winters AE, Quezada M, Capon RJ, Mollo E, Garson MJ (2016-01-20). "Choose Your Weaponry: Selective Storage of a Single Toxic Compound, Latrunculin A, by Closely Related Nudibranch Molluscs". PLOS ONE. 11 (1): e0145134. Bibcode:2016PLoSO..1145134C. doi: 10.1371/journal.pone.0145134 . PMC   4720420 . PMID   26788920.
  23. 1 2 3 Gillor O, Carmeli S, Rahamim Y, Fishelson Z, Ilan M (May 2000). "Immunolocalization of the Toxin Latrunculin B within the Red Sea Sponge Negombata magnifica (Demospongiae, Latrunculiidae)". Marine Biotechnology. 2 (3): 213–23. doi:10.1007/s101260000026. PMID   10852799. S2CID   1759699.
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