scholarly journals A conserved strategy for inducing appendage regeneration in moon jellyfish, Drosophila, and mice

eLife ◽  
2021 ◽  
Vol 10 ◽  
Author(s):  
Michael J Abrams ◽  
Fayth Hui Tan ◽  
Yutian Li ◽  
Ty Basinger ◽  
Martin L Heithe ◽  
...  
Keyword(s):  
Growth Hormone ◽  
Amino Acid ◽  
Limb Regeneration ◽  
Testable Hypothesis ◽  
The Moon ◽  
Moon Jellyfish ◽  
Nutrient Supplementation ◽  
Adult Mice ◽  
Evolutionarily Conserved ◽  
Animal Phylogeny

Can limb regeneration be induced? Few have pursued this question, and an evolutionarily conserved strategy has yet to emerge. This study reports a strategy for inducing regenerative response in appendages, which works across three species that span the animal phylogeny. In Cnidaria, the frequency of appendage regeneration in the moon jellyfish Aurelia was increased by feeding with the amino acid L-leucine and the growth hormone insulin. In insects, the same strategy induced tibia regeneration in adult Drosophila. Finally, in mammals, L-leucine and sucrose administration induced digit regeneration in adult mice, including dramatically from mid-phalangeal amputation. The conserved effect of L-leucine and insulin/sugar suggests a key role for energetic parameters in regeneration induction. The simplicity by which nutrient supplementation can induce appendage regeneration provides a testable hypothesis across animals.

scholarly journals A conserved strategy for inducing appendage regeneration

2020 ◽  
Author(s):  
Michael J. Abrams ◽  
Fayth Tan ◽  
Ty Basinger ◽  
Martin Heithe ◽  
Yutian Li ◽  
...  
Keyword(s):  
Growth Hormone ◽  
Amino Acid ◽  
Limb Regeneration ◽  
Testable Hypothesis ◽  
The Moon ◽  
Moon Jellyfish ◽  
Nutrient Supplementation ◽  
Adult Mice ◽  
Evolutionarily Conserved ◽  
Animal Phylogeny

AbstractCan limb regeneration be induced? Few have pursued this question, and an evolutionarily conserved strategy has yet to emerge. This study reports a strategy for inducing regenerative response in appendages, which works across three species that span the animal phylogeny. In Cnidaria, the frequency of appendage regeneration in the moon jellyfish Aurelia was increased by feeding with the amino acid L-leucine and the growth hormone insulin. In insects, the same strategy induced tibia regeneration in adult Drosophila. Finally, in mammals, L-leucine and sucrose administration induced digit regeneration in adult mice, including dramatically from mid-phalangeal amputation. The conserved effect of L-leucine and insulin/sugar suggests a key role for energetic parameters in regeneration induction. The simplicity by which nutrient supplementation can induce appendage regeneration provides a testable hypothesis across animals.

The minimal amino acid sequence of the insulin-potentiating fragments of human growth hormone: its mechanism of action

Diabetes ◽  
1980 ◽  
Vol 29 (10) ◽  
pp. 782-787 ◽  
Author(s):  
F. M. Ng ◽  
J. Bornstein ◽  
C. E. Pullin ◽  
J. O. Bromley ◽  
S. L. Macaulay
Keyword(s):  
Growth Hormone ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Human Growth Hormone ◽  
Mechanism Of Action ◽  
Human Growth

scholarly journals Shorter, warmer winters may inhibit production of ephyrae in a population of the moon jellyfish Aurelia aurita

Hydrobiologia ◽  
2020 ◽  
Author(s):  
Alexandra Loveridge ◽  
Cathy H. Lucas ◽  
Kylie A. Pitt
Keyword(s):  
Incubation Time ◽  
Life Stage ◽  
Aurelia Aurita ◽  
The Moon ◽  
Minimum Period ◽  
Moon Jellyfish ◽  
Winter Conditions ◽  
Scyphozoan Jellyfish ◽  
Significant Production ◽  
Planula Larvae

AbstractScyphozoan jellyfish blooms display high interannual variability in terms of timing of appearance and size of the bloom. To understand the causes of this variability, the conditions experienced by the polyps prior to the production of ephyrae in the spring were examined. Polyps reared from planula larvae of Aurelia aurita medusae collected from southern England (50°49′58.8; − 1°05′36.9) were incubated under orthogonal combinations of temperature (4, 7, 10 °C) and duration (2, 4, 6, 8 weeks), representing the range of winter conditions in that region, before experiencing an increase to 13 °C. Timing and success of strobilation were recorded. No significant production of ephyrae was observed in any of the 2- and 4-week incubations, or in any 10 °C incubation. Time to first ephyra release decreased with longer winter incubations, and more ephyrae were produced following longer and colder winter simulations. This experiment indicates that A. aurita requires a minimum period of cooler temperatures to strobilate, and contradicts claims that jellyfish populations will be more prevalent in warming oceans, specifically in the context of warmer winter conditions. Such investigations on population-specific ontogeny highlights the need to examine each life stage separately as well as in the context of its environment.

scholarly journals Humanizing the yeast origin recognition complex

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Clare S. K. Lee ◽  
Ming Fung Cheung ◽  
Jinsen Li ◽  
Yongqian Zhao ◽  
Wai Hei Lam ◽  
...  
Keyword(s):  
Amino Acid ◽  
Protein Complex ◽  
Origin Recognition Complex ◽  
Specific Binding ◽  
Life Cycles ◽  
Amino Acid Insertion ◽  
Evolutionarily Conserved ◽  
Transcriptional Start Sites ◽  
Eukaryote Genome ◽  
Origin Recognition

AbstractThe Origin Recognition Complex (ORC) is an evolutionarily conserved six-subunit protein complex that binds specific sites at many locations to coordinately replicate the entire eukaryote genome. Though highly conserved in structure, ORC’s selectivity for replication origins has diverged tremendously between yeasts and humans to adapt to vastly different life cycles. In this work, we demonstrate that the selectivity determinant of ORC for DNA binding lies in a 19-amino acid insertion helix in the Orc4 subunit, which is present in yeast but absent in human. Removal of this motif from Orc4 transforms the yeast ORC, which selects origins based on base-specific binding at defined locations, into one whose selectivity is dictated by chromatin landscape and afforded with plasticity, as reported for human. Notably, the altered yeast ORC has acquired an affinity for regions near transcriptional start sites (TSSs), which the human ORC also favors.

scholarly journals The amino acid sequence of equine growth hormone

FEBS Letters ◽  
1973 ◽  
Vol 34 (2) ◽  
pp. 353-355 ◽  
Author(s):  
M.M. Zakin ◽  
E. Poskus ◽  
J.M. Dellacha ◽  
A.C. Paladini ◽  
J.A. Santomé
Keyword(s):  
Growth Hormone ◽  
Amino Acid ◽  
Amino Acid Sequence

Reduced and S-carboxymethylated human growth hormone: a probe for diabetogenic action

1984 ◽  
Vol 247 (5) ◽  
pp. E639-E644
Author(s):  
C. M. Cameron ◽  
J. L. Kostyo ◽  
J. A. Rillema ◽  
S. E. Gennick
Keyword(s):  
Growth Hormone ◽  
Amino Acid ◽  
Human Growth Hormone ◽  
Human Growth ◽  
Mouse Mammary Gland ◽  
Amino Acid Incorporation ◽  
Acid Incorporation ◽  
Hypophysectomized Rats

The biological activity profile of reduced and S-carboxymethylated human growth hormone (RCM-hGH) was determined to establish its suitability for study of the diabetogenic property of hGH. RCM-hGH was found to have greatly attenuated in vivo growth-promoting activity in the 9-day weight-gain test in hypophysectomized rats (approximately 1%) and to have a similar low order of in vitro activity in stimulating amino acid incorporation into the protein of the isolated rat diaphragm. RCM-hGH also only had approximately 1% of the in vitro insulin-like activity of the native hormone on isolated adipose tissue from hypophysectomized rats. In contrast, RCM-hGH retained substantial in vivo diabetogenic activity in the ob/ob mouse, appearing to have approximately 50% of the activity of the native hormone. RCM-hGH was also found to retain significant, although attenuated (25%), in vitro lactogenic activity when tested for the ability to stimulate amino acid incorporation into a casein-rich protein fraction in mouse mammary gland explants. Because RCM-hGH exhibits a high degree of diabetogenic activity, although lacking significant anabolic or insulin-like activities, it will be useful as a "monovalent" probe for the study of the molecular mechanism of the diabetogenic action of GH.

scholarly journals Artificial reefs for sea cucumber aquaculture confirmed as settlement substrates of the moon jellyfish Aurelia coerulea

Hydrobiologia ◽  
2018 ◽  
Vol 818 (1) ◽  
pp. 223-234 ◽  
Author(s):  
Zhijun Dong ◽  
Lei Wang ◽  
Tingting Sun ◽  
Qingqing Liu ◽  
Youfang Sun
Keyword(s):  
Sea Cucumber ◽  
Artificial Reefs ◽  
The Moon ◽  
Moon Jellyfish ◽  
Aurelia Coerulea

Growth hormone decreases muscle glutamine production and stimulates protein synthesis in hypercatabolic patients

2000 ◽  
Vol 279 (2) ◽  
pp. E323-E332 ◽  
Author(s):  
Gianni Biolo ◽  
Fulvio Iscra ◽  
Alessandra Bosutti ◽  
Gabriele Toigo ◽  
Beniamino Ciocchi ◽  
...  
Keyword(s):  
Growth Hormone ◽  
Protein Synthesis ◽  
Amino Acid ◽  
De Novo ◽  
Muscle Protein ◽  
Recombinant Human Growth Hormone ◽  
Glutamine Metabolism ◽  
Trauma Patients ◽  
Mrna Levels ◽  
Glutamine Production

We determined the effects of 24-h recombinant human growth hormone (rhGH) infusion into a femoral artery on leg muscle protein kinetics, amino acid transport, and glutamine metabolism in eight adult hypercatabolic trauma patients. Metabolic pathways were assessed by leg arteriovenous catheterization and muscle biopsies with the use of stable amino acid isotopes. Muscle mRNA levels of selected enzymes were determined by competitive PCR. rhGH infusion significantly accelerated the inward transport rates of phenylalanine and leucine and protein synthesis, whereas the muscle protein degradation rate and cathepsin B and UbB polyubiquitin mRNA levels were not significantly modified by rhGH. rhGH infusion decreased the rate of glutamine de novo synthesis and glutamine precursor availability, total branched-chain amino acid catabolism, and nonprotein glutamate utilization. Thus net glutamine release from muscle into circulation significantly decreased after rhGH administration (∼50%), whereas glutamine synthetase mRNA levels increased after rhGH infusion, possibly to compensate for reduced glutamine precursor availability. We conclude that, after trauma, the anticatabolic action of rhGH is associated with a potentially harmful decrease in muscle glutamine production.

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