Pigment granule translocation in red ovarian chromatophores from the palaemonid shrimp Macrobrachium olfersi (Weigmann, 1836): Functional roles for the cytoskeleton and its molecular motors

Milograna, Sarah Ribeiro; Ribeiro, Márcia Regina; Baqui, Munira Muhammad Abdel; McNamara, John Campbell

doi:10.1016/j.cbpa.2014.08.010

Cited by 5 publications

(4 citation statements)

References 58 publications

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“…Proteins were then furtherly grouped into 29 subcategories (Figure ). In particular, we identified several cytoskeleton proteins that are crucial for cell division and migration, aggregation and dispersion of granules within the cytoplasm as well as for phagocytosis, an essential process against pathogens and for tissue remodeling …”

Section: Proteins Identified From Circulating Hemocytes Of Pc By Lc‐mmentioning

confidence: 99%

Toward the Molecular Deciphering of Pomacea canaliculata Immunity: First Proteomic Analysis of Circulating Hemocytes

et al. 2019

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Pomacea canaliculata is a freshwater snail with interesting biological features that include invasiveness, human parasite hosting, and adult regeneration. Its immune system may represent the target for strategies aimed at controlling the spread of the snail population and its hosting of the human parasite Angiostrongylus cantonensis. Moreover, immune functions likely have a role in the snail's ability to wound heal and regenerate. Despite its importance in multiple processes, very little is known about the molecular basis of P. canaliculata immunity. Aiming to contribute to filling this gap, the ultrastructure of circulating hemocytes in healthy snails is studied and the first proteomic analysis of these cells is performed, evidencing 83 unique proteins, 96% of which have identifiable homologs in other species. Fifteen proteins are retrieved as potentially involved in immune‐related signaling pathways, such as hemocyanin, C1q‐like protein, and HSP90 together with cytoskeleton and cytoskeleton‐related proteins involved in cell motility and membrane dynamics. This first proteome study on non‐stimulated hemocytes provides a valid reference for future investigations on the molecular changes under stressful circumstances, like pathogen exposure, wounding, or environmental changes.

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Section: Proteins Identified From Circulating Hemocytes Of Pc By Lc‐mmentioning

confidence: 99%

Toward the Molecular Deciphering of Pomacea canaliculata Immunity: First Proteomic Analysis of Circulating Hemocytes

et al. 2019

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“…In M. olfersi ovarian chromatophores, inhibition of PKA accelerated the rapid phase of pigment aggregation, suggesting that this kinase may restrain the molecular motors of aggregation (nonmuscle myosin II and dynein; Milograna et al., ), alter the turnover of actin microfilaments (Milograna et al., ) or activate dispersion motors (kinesin; Boyle and McNamara, ). Decreased cAMP titers may enable dephosphorylation of PKA targets (Tuma and Gelfand, ), including the SER Ca 2+ channels, by native phosphoprotein phosphatase, since PKA phosphorylates human cardiac L‐type Ca 2+ channels (Kamp and Hell, ) and Ca 2+ channel receptors in rabbit skeletal muscle (Rohrkastens et al., ).…”

Section: Discussionmentioning

confidence: 99%

“…This Ca 2+ ‐binding effector stimulates nitric oxide synthase (NOS) ⑧ to synthesize nitric oxide (NO) that activates cytosolic guanylyl cyclase ⑨ to convert GTP into cGMP. This second messenger stimulates protein kinase G ⑩ that coordinates activity of the molecular motors dynein and nonmuscle myosin II ⑪ by regulating other downstream kinases and phosphatases (i.e., Rho‐associated protein kinase and myosin light chain phosphatase [Milograna et al., , ]), ultimately culminating in pigment aggregation ⑫.…”

Section: Discussionmentioning

confidence: 99%

“…However, homologues of the AKH and AKH/corazonin‐related peptide (ACP) receptors, which together are characterized as GnRH‐like receptors, share a common ancestor with vertebrate GnRH receptors, and are known from several invertebrate group, particularly mollusks and insects (Roch et al., ; Caers et al., ; Hauser and Grimmelikhuijzen, ). Some of the ultimate downstream targets activated during the RPCH signaling cascade are known in the chromatophores of the freshwater shrimp Macrobrachium olfersi , and include kinesin (Boyle and McNamara, ) and type II myosins (Milograna et al., ). However, knowledge of the intermediate intracellular events culminating in the generation of, and cross talk among the various second messengers that participate in the RPCH‐signaling cascade is still scanty.…”

Section: Introductionmentioning

confidence: 99%

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Pigment Translocation in Caridean Shrimp Chromatophores: Receptor Type, Signal Transduction, Second Messengers, and Cross Talk Among Multiple Signaling Cascades

et al. 2016

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Pigment aggregation in shrimp chromatophores is triggered by red pigment concentrating hormone (RPCH), a neurosecretory peptide whose plasma membrane receptor may be a G-protein coupled receptor (GPCR). While RPCH binding activates the Ca /cGMP signaling cascades, a role for cyclic AMP (cAMP) in pigment aggregation is obscure, as are the steps governing Ca release from the smooth endoplasmic reticulum (SER). A role for the antagonistic neuropeptide, pigment dispersing homone (α-PDH) is also unclear. In red, ovarian chromatophores from the freshwater shrimp Macrobrachium olfersi, we show that a G-protein antagonist (AntPG) strongly inhibits RPCH-triggered pigment aggregation, suggesting that RPCH binds to a GPCR, activating an inhibitory G-protein. Decreasing cAMP levels may cue pigment aggregation, since cytosolic cAMP titers, when augmented by cholera toxin, forskolin or vinpocentine, completely or partially impair pigment aggregation. Triggering opposing Ca /cGMP and cAMP cascades by simultaneous perfusion with lipid-soluble cyclic nucleotide analogs induces a "tug-of-war" response, pigments aggregating in some chromatosomes with unpredictable, oscillatory movements in others. Inhibition of cAMP-dependent protein kinase accelerates aggregation and reduces dispersion velocities, suggesting a role in phosphorylation events, possibly regulating SER Ca release and pigment aggregation. The second messengers IP and cADPR do not stimulate SER Ca release. α-PDH does not sustain pigment dispersion, suggesting that pigment translocation in caridean chromatophores may be regulated solely by RPCH, since PDH is not required. We propose a working hypothesis to further unravel key steps in the mechanisms of pigment translocation within crustacean chromatophores that have remained obscure for nearly a century.

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Identification of Functional SSR Markers in Freshwater Ornamental Shrimps Neocaridina denticulata Using Transcriptome Sequencing

Huang

Chu

et al. 2020

Mar Biotechnol

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Pigment granule translocation in red ovarian chromatophores from the palaemonid shrimp Macrobrachium olfersi (Weigmann, 1836): Functional roles for the cytoskeleton and its molecular motors

Cited by 5 publications

References 58 publications

Toward the Molecular Deciphering of Pomacea canaliculata Immunity: First Proteomic Analysis of Circulating Hemocytes

Toward the Molecular Deciphering of Pomacea canaliculata Immunity: First Proteomic Analysis of Circulating Hemocytes

Pigment Translocation in Caridean Shrimp Chromatophores: Receptor Type, Signal Transduction, Second Messengers, and Cross Talk Among Multiple Signaling Cascades

Identification of Functional SSR Markers in Freshwater Ornamental Shrimps Neocaridina denticulata Using Transcriptome Sequencing

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