Characterization of central neurons in bivalves using antibodies raised against neuropeptides involved in gastropod egg-laying behavior

The gastrointestinal microbiota plays a pivotal role in maintaining animal health, immunity and reproductive performances. However, literature about the relationship between microbiota and reproductive performance is limited. The aim of the present study was to determine differences in the intestinal microbiota of broiler breeders with different egg laying rate. A total of 200 AA+ parent broiler breeders (41-week-old) were separated into two groups according to their different egg laying rate [average egg laying rate group (AR: 78.57 ± 0.20%) and high egg laying rate group (HR: 90.79 ± 0.43%). Feed conversion ratio (FCR), ovary cell apoptosis rate (ApoCR) and relative abdominal fat weight were lower (p = 0.01), while the hatchability rate of qualified egg was higher (p = 0.04) in HR group than that in AR group. Phascolarctobacterium abundance were lower (p = 0.012) in ileum of HR birds. Romboutsia (genus) in ileum was negatively related to the feed efficiency (r = −0.58, p < 0.05), Firmicutes (phylum) and Lactobacillus (genus) abundances in cecum were positively related to the egg laying rate (ELR) (r = 0.35 and 0.48, p < 0.05), feed efficiency (r = 0.42 and 0.43, p < 0.05), while Spirochaetes (phylum) and Sphaerochaeta (genus) abundances in cecum were negatively related to the ELR (r = −0.43 and −0.70, p < 0.05), feed efficiency (r = 0.54 and 0.48, p < 0.05), and positively related to ApoCR (r = 0.46 and 0.47, p < 0.05). Our results suggested that microbiota, such as Firmicutes (phylum) and Lactobacillus (genus) have positive relationship, while Spirochaetes (phylum) and Romboutsia (genus) abundances exert negative relationship with broiler breeders' reproductive performances.

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Egg-laying behavior and morphological and chemical characterization of egg surface and egg attachment glue of the digger wasp Ampulex compressa (Hymenoptera, Ampulicidae)

Arthropod Structure & Development ◽

10.1016/j.asd.2017.11.010 ◽

2018 ◽

Vol 47 (1) ◽

pp. 74-81 ◽

Cited By ~ 2

Author(s):

Werner Gnatzy ◽

Walter Volknandt ◽

Anja Dzwoneck

Keyword(s):

Chemical Characterization ◽

Egg Laying ◽

Digger Wasp ◽

Ampulex Compressa

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Functional characterization of the rod visual pigment of the echidna (Tachyglossus aculeatus), a basal mammal

Visual Neuroscience ◽

10.1017/s0952523812000223 ◽

2012 ◽

Vol 29 (4-5) ◽

pp. 211-217 ◽

Cited By ~ 18

Author(s):

CONSTANZE BICKELMANN ◽

JAMES M. MORROW ◽

JOHANNES MÜLLER ◽

BELINDA S.W. CHANG

Keyword(s):

Half Life ◽

Functional Characterization ◽

Egg Laying ◽

Sensory Transduction ◽

Wild Type ◽

Functional Variation ◽

Bovine Rhodopsin ◽

Tachyglossus Aculeatus

AbstractMonotremes are the most basal egg-laying mammals comprised of two extant genera, which are largely nocturnal. Visual pigments, the first step in the sensory transduction cascade in photoreceptors of the eye, have been examined in a variety of vertebrates, but little work has been done to study the rhodopsin of monotremes. We isolated the rhodopsin gene of the nocturnal short-beaked echidna (Tachyglossus aculeatus) and expressed and functionally characterized the protein in vitro. Three mutants were also expressed and characterized: N83D, an important site for spectral tuning and metarhodopsin kinetics, and two sites with amino acids unique to the echidna (T158A and F169A). The λmax of echidna rhodopsin (497.9 ± 1.1 nm) did not vary significantly in either T158A (498.0 ± 1.3 nm) or F169A (499.4 ± 0.1 nm) but was redshifted in N83D (503.8 ± 1.5 nm). Unlike other mammalian rhodopsins, echidna rhodopsin did react when exposed to hydroxylamine, although not as fast as cone opsins. The retinal release rate of light-activated echidna rhodopsin, as measured by fluorescence spectroscopy, had a half-life of 9.5 ± 2.6 min−1, which is significantly shorter than that of bovine rhodopsin. The half-life of the N83D mutant was 5.1 ± 0.1 min−1, even shorter than wild type. Our results show that with respect to hydroxylamine sensitivity and retinal release, the wild-type echidna rhodopsin displays major differences to all previously characterized mammalian rhodopsins and appears more similar to other nonmammalian vertebrate rhodopsins such as chicken and anole. However, our N83D mutagenesis results suggest that this site may mediate adaptation in the echidna to dim light environments, possibly via increased stability of light-activated intermediates. This study is the first characterization of a rhodopsin from a most basal mammal and indicates that there might be more functional variation in mammalian rhodopsins than previously assumed.

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Calcineurin, a Calcium/Calmodulin-dependent Protein Phosphatase, Is Involved in Movement, Fertility, Egg Laying, and Growth inCaenorhabditis elegans

Molecular Biology of the Cell ◽

10.1091/mbc.e02-01-0005 ◽

2002 ◽

Vol 13 (9) ◽

pp. 3281-3293 ◽

Cited By ~ 79

Author(s):

Jaya Bandyopadhyay ◽

Jiyeon Lee ◽

Jungsoo Lee ◽

Jin Il Lee ◽

Jae-Ran Yu ◽

...

Keyword(s):

Signaling Pathways ◽

Protein Phosphatase ◽

Body Wall ◽

Egg Laying ◽

Α Subunit ◽

C Elegans ◽

Calcium Calmodulin Dependent ◽

Dependent Protein ◽

Identification And Characterization

Calcineurin is a Ca2+-calmodulin–dependent serine/threonine protein phosphatase that has been implicated in various signaling pathways. Here we report the identification and characterization of calcineurin genes in Caenorhabditis elegans (cna-1 and cnb-1), which share high homology with Drosophila and mammalian calcineurin genes. C. elegans calcineurin binds calcium and functions as a heterodimeric protein phosphatase establishing its biochemical conservation in the nematode. Calcineurin is expressed in hypodermal seam cells, body-wall muscle, vulva muscle, neuronal cells, and in sperm and the spermatheca. cnb-1 mutants showed pleiotropic defects including lethargic movement and delayed egg-laying. Interestingly, these characteristic defects resembled phenotypes observed in gain-of-function mutants ofunc-43/Ca2+-calmodulin–dependent protein kinase II (CaMKII) and goa-1/Go-protein α-subunit. Double mutants of cnb-1 andunc-43(gf) displayed an apparent synergistic severity of movement and egg-laying defects, suggesting that calcineurin may have an antagonistic role in CaMKII-regulated phosphorylation signaling pathways in C. elegans.

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Purification and chemical characterization of caudodorsal cell hormone-II from the egg-laying controlling caudodorsal cells of Lymnaea stagnalis

Peptides ◽

10.1016/0196-9781(92)90099-o ◽

1992 ◽

Vol 13 (2) ◽

pp. 215-220 ◽

Cited By ~ 13

Author(s):

K.W. Li ◽

W.P.M. Geraerts ◽

J. Joosse

Keyword(s):

Lymnaea Stagnalis ◽

Chemical Characterization ◽

Egg Laying ◽

Cell Hormone

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Purification and characterization of Aplysia atrial gland secretory granules containing egg-laying prohormone-related peptides

Peptides ◽

10.1016/0196-9781(94)90177-5 ◽

1994 ◽

Vol 15 (1) ◽

pp. 101-108 ◽

Cited By ~ 4

Author(s):

Gregg T. Nagle ◽

Walter R.A. Van Heumen ◽

Mahdy A. El-Hamzawy ◽

Alexander Kurosky

Keyword(s):

Secretory Granules ◽

Egg Laying ◽

Purification And Characterization ◽

Atrial Gland

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Histochemical characterization of neuronal NADPH-diaphorase.

Journal of Histochemistry & Cytochemistry ◽

10.1177/37.5.2703701 ◽

1989 ◽

Vol 37 (5) ◽

pp. 653-661 ◽

Cited By ~ 215

Author(s):

B T Hope ◽

S R Vincent

Keyword(s):

Nadph Diaphorase ◽

Rat Striatum ◽

Tetrazolium Salt ◽

Diaphorase Activity ◽

Central Neurons ◽

Membrane Bound ◽

Pre Treatment ◽

Dt Diaphorase ◽

Discrete Populations

We examined the properties of neuronal NADPH-diaphorase in sections of rat striatum, using histochemical procedures. NADPH-diaphorase histochemistry stained discrete populations of central neurons and provided a Golgi-like image of the neurons exhibiting this activity. The NADPH-diaphorase reaction appeared to be enzyme catalyzed, since it was abolished by pre-treatment with proteases, heat, and acid or alkaline denaturation. Under anaerobic conditions, any tetrazolium salt with a redox potential more positive than NADPH could be reduced by the enzyme. NADPH-diaphorase activity was sensitive to inhibition by sulfhydryl reagents but was unaffected by metal chelators, superoxide dismutase, and catalase. Therefore, the enzyme is unlikely to be a metalloenzyme or to reduce tetrazoliums by producing superoxide anions or hydrogen peroxide. Various analogues of beta-NADPH could be used by the enzyme; however, beta-NADH, which can be used by DT-diaphorase, was ineffective. The enzyme was also resistant to dicumarol, an inhibitor of DT-diaphorase activity. Electron microscopy indicated that the NADPH-diaphorase reaction resulted in staining of various membranous organelles. We conclude that neuronal NADPH-diaphorase is a membrane-bound enzyme distinct from DT-diaphorase and other known enzymes with diaphorase activity. The histochemical characteristics presented here should now enable meaningful biochemical studies of neuronal NADPH-diaphorase to be undertaken.

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