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Animal Growth

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Marco Saroglia – One of the best experts on this subject based on the ideXlab platform.

  • Peptide transport and Animal Growth: The fish paradigm
    Biology Letters, 2011
    Co-Authors: Tiziano Verri, Genciana Terova, Konrad Dabrowski, Marco Saroglia


    Protein digestion products are transported from the intestinal lumen into the enterocyte both in the form of free amino acids (AAs), by a large variety of brush border membrane AA transporters, and in the form of di/tripeptides, by a single brush border membrane transporter known as PEPtide Transporter 1 (PEPT1). Recent data indicate that, at least in teleost fish, PEPT1 plays a significant role in Animal Growth by operating, at the gastrointestinal level, as part of an integrated response network to food availability that directly supports body weight. Notably, PEPT1 responds to both fasting and refeeding and is involved in a phenomenon known as compensatory Growth (a phase of accelerated Growth when food levels are restored after a period of Growth depression). In particular, PEPT1 expression decreases during fasting and increases during refeeding, which is the opposite of what observed so far in mammals and birds. These findings in teleost fish document, to our knowledge, for the first time in a vertebrate model, a direct correlation between the expression of an intestinal transporter, such as PEPT1, primarily involved in the uptake of dietary protein degradation products and Animal Growth.

Joseph L Ravet – One of the best experts on this subject based on the ideXlab platform.

  • food quantity and quality regulation of trophic transfer between primary producers and a keystone grazer daphnia in pelagic freshwater food webs
    Oikos, 2007
    Co-Authors: Jonas Persson, Michael T Brett, Tobias Vrede, Joseph L Ravet


    The transfer of energy and nutrients from plants to Animals is a key process in all ecosystems. In lakes, inefficient transfer of primary producer derived energy can result in low Animal Growth rat …

Thomas M Moran – One of the best experts on this subject based on the ideXlab platform.

  • Promotion of Animal Growth with a monoclonal antibody specific to Growth hormone receptor.
    Molecular and cellular endocrinology, 1996
    Co-Authors: Bosco Shang Wang, Constantin A. Bona, Araceli A. Lumanglas, Thomas M Moran


    A monoclonal antibody (mAb), designated 2C3, was raised against the Growth hormone receptor (GHR) of rats. In a radioimmunoassay, 2C3 was found to compete with iodinated porcine GH (pGH) tracer for the binding to GHR, suggesting that GHR binding sites for pGH and 2C3 were identical or closely adjacent. The competition curve generated by 2C3 was identical to that generated by cold pGH, suggesting that the binding affinities of 2C3 and pGH to GHR were very similar. Administration of hypophysectomized rats with 2C3 resulted in the Growth of these GH-deficient Animals for a long period of time, mimicking the somatogenic effect of GH. However, this effect was abolished when 2C3 was injected into Animals in the presence of exogenous GHR. A control mAb recognizing a GHR epitope distal from its binding site for GH failed to produce the Growth in rats. Taken together, findings from the present study indicate that 2C3 is fully capable of engaging with GHR and subsequently triggering the Growth response in rats. This mAb may also prove useful as a biologically active agonist for better understanding the initiation of the physiological process of GHR.

  • Promotion of Animal Growth with a monoclonal anti-idiotype specific to anti-porcine Growth hormone antibody.
    Molecular Immunology, 1994
    Co-Authors: Bosco Shang Wang, Ren-jie Zhang, Constantin A. Bona, Thomas M Moran


    Abstract A monoclonal antibody (mAb), designated PS-7.6, was previously shown to enhance the Growth-promoting activity of porcine Growth hormone (pGH) in an experimental hypophysec tomized (hypox) rat model. The long lasting effect of PS-7.6 was postulated to be a result of the induction of anti-idiotypic antibody (anti-id) in these treated Animals. An attempt was made in this report to further explore this issue. It was demonstrated that mice following immunization with PS-7.6 were capable of producing anti-id in serum. The antibody titers of mice immunized with a mixture of PS-7.6 and pGH were much higher than that of those being immunized with PS-7.6 alone. A monoclonal anti-id, designated 2A6, was generated and found to recognize the intact PS-7.6 and its F(ab’) 2 fragment under non-reducing condition in Western analysis. However, it did not interact with reduced PS-7.6, suggesting the necessity of both H and L chains for the expression of a conformational idiotype. In radioimmunoassay, 2A6 competed with pGH for the binding to PS-7.6, but failed to do so with a control anti-pGH mAb recognizing a distinct pGH epitope from that of PS-7.6. Results from a biospecific interaction analysis which monitored the molecular interactions in a real-time fashion confirmed the facts that 2A6 specifically recognized the variable region of PS-7.6 and that the recognition was inhibited by the presence of pGH. Enzyme-linked immunosorbent assay provided further evidence to indicate that 2A6 bound to GH binding protein, i.e. the soluble GH receptor, and pGH prevented this interaction in a dose-dependent manner. The biological effect of 2A6 was evaluated in hypox rats and shown to promote the Growth of these GH-deficient Animals. Taken together, the present findings clearly demonstrate that 2A6 raised against a Growth-enhancing anti-pGH mAb mimics pGH both conformationally and functionally.