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of islet transplantation ( Mohseni Salehi Monfared et al . 2009 ). For example, vitamins D3 and E, which are known to have antioxidant properties, were used to improve the morphology and function of neonatal porcine islets (NPI) ( Luca et al . 2000
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ABSTRACT
Brain natriuretic peptide (BNP) is a novel peptide that has actions similar to atrial natriuretic peptide (ANP). The present study investigated BNP localization in the heart, ANP and BNP contents in several organs, and ANP and BNP clearance through these organs. In the morphological study, it was shown that porcine BNP-like immunoreactivity was mainly distributed in the granules of the atrium. The content of porcine BNP-like immunoreactivity in the atrium was extremely high, about 100-fold greater than in the ventricle. From the determination of porcine BNP and ANP contents of such organs as the heart, kidney and liver and also plasma, it was shown that porcine BNP concentration was approximately one order of magnitude lower than that of ANP, and clearance rates of ANP and porcine BNP from these organs were similar and not significantly different between the organs. These results suggest that the modes of secretion and degradation of porcine BNP are not the same as those of ANP.
Journal of Endocrinology (1992) 132, 101–106
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associated with proliferation (PCNA), apoptosis (Bax), TK (phosphotyrosine), Cdc2/p34, PKA and PKA-activated transcription factor (CREB-1) in cultured porcine ovarian cells. We also investigated how TPO influences the secretion of progesterone
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ABSTRACT
The follicular fluid is an important milieu for the growing and maturing oocyte and granulosa cells. In this study we investigated: (1) the properties of gonadotrophin-binding sites in the supernatant fraction of porcine follicular fluid (pFF) and compared them with those of membrane-bound receptors, and (2) the relative changes that occur in pFF and granulosa cell receptor-binding activity following hormone priming of gilts. 125I-Labelled human chorionic gonadotrophin (hCG) and 125I-labelled ovine FSH (oFSH) binding to particulate and supernatant fractions of pFF were hormone-specific and saturable. The concentration of 125I-labelled hCG-binding sites was roughly 50-fold higher in particulate than in supernatant fractions of pFF. However, 30–40% of the total 125I-labelled hCG-binding activity in pFF was present in the supernatant fraction of commercial batches of pFF. 125I-Labelled oFSH binding to pFF membranes was markedly higher than to supernatant fractions. Binding of 125I-labelled hCG and 125I-labelled oFSH to granulosa cells and supernatants of pFF showed a time-dependent variation in response to hormone priming. The results suggest that gonadotrophin-binding sites in the supernatant fraction of pFF have properties similar to those of their membrane-bound counterparts. 125I-Labelled hCG-binding activity in the supernatant fraction of pFF was shown to be more stable than detergent-solubilized LH/hCG receptors, even in glycerol-preserved preparations. Based on a number of criteria, we have speculated that pFF may have components which may be similar in structure to the extracellular domain of the LH/hCG receptor.
Journal of Endocrinology (1990) 124, 485–494
Department of Animal Production and Agriculture, Research Area: Ecodesarrollo de la Producción Animal, School of Veterinary Medicine, Universidad Autónoma Metropolitana-Xochimilco, México
Departamento de Investigación Experimental y Bioterio, Instituto Nacional de Ciencias Médicas y Nutrición Salvador Zubirán, México
Division of Clinical Pharmacology and Toxicology, The Hospital for Sick Children, 555 University Ave., Toronto, Ontario M5G 1X8, Canada
EIAH-Benemérita Universidad Autónoma de Puebla, San Juan Acateno, Teziutlan, Puebla, México
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Department of Animal Production and Agriculture, Research Area: Ecodesarrollo de la Producción Animal, School of Veterinary Medicine, Universidad Autónoma Metropolitana-Xochimilco, México
Departamento de Investigación Experimental y Bioterio, Instituto Nacional de Ciencias Médicas y Nutrición Salvador Zubirán, México
Division of Clinical Pharmacology and Toxicology, The Hospital for Sick Children, 555 University Ave., Toronto, Ontario M5G 1X8, Canada
EIAH-Benemérita Universidad Autónoma de Puebla, San Juan Acateno, Teziutlan, Puebla, México
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Department of Animal Production and Agriculture, Research Area: Ecodesarrollo de la Producción Animal, School of Veterinary Medicine, Universidad Autónoma Metropolitana-Xochimilco, México
Departamento de Investigación Experimental y Bioterio, Instituto Nacional de Ciencias Médicas y Nutrición Salvador Zubirán, México
Division of Clinical Pharmacology and Toxicology, The Hospital for Sick Children, 555 University Ave., Toronto, Ontario M5G 1X8, Canada
EIAH-Benemérita Universidad Autónoma de Puebla, San Juan Acateno, Teziutlan, Puebla, México
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Department of Animal Production and Agriculture, Research Area: Ecodesarrollo de la Producción Animal, School of Veterinary Medicine, Universidad Autónoma Metropolitana-Xochimilco, México
Departamento de Investigación Experimental y Bioterio, Instituto Nacional de Ciencias Médicas y Nutrición Salvador Zubirán, México
Division of Clinical Pharmacology and Toxicology, The Hospital for Sick Children, 555 University Ave., Toronto, Ontario M5G 1X8, Canada
EIAH-Benemérita Universidad Autónoma de Puebla, San Juan Acateno, Teziutlan, Puebla, México
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Department of Animal Production and Agriculture, Research Area: Ecodesarrollo de la Producción Animal, School of Veterinary Medicine, Universidad Autónoma Metropolitana-Xochimilco, México
Departamento de Investigación Experimental y Bioterio, Instituto Nacional de Ciencias Médicas y Nutrición Salvador Zubirán, México
Division of Clinical Pharmacology and Toxicology, The Hospital for Sick Children, 555 University Ave., Toronto, Ontario M5G 1X8, Canada
EIAH-Benemérita Universidad Autónoma de Puebla, San Juan Acateno, Teziutlan, Puebla, México
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Department of Animal Production and Agriculture, Research Area: Ecodesarrollo de la Producción Animal, School of Veterinary Medicine, Universidad Autónoma Metropolitana-Xochimilco, México
Departamento de Investigación Experimental y Bioterio, Instituto Nacional de Ciencias Médicas y Nutrición Salvador Zubirán, México
Division of Clinical Pharmacology and Toxicology, The Hospital for Sick Children, 555 University Ave., Toronto, Ontario M5G 1X8, Canada
EIAH-Benemérita Universidad Autónoma de Puebla, San Juan Acateno, Teziutlan, Puebla, México
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Department of Animal Production and Agriculture, Research Area: Ecodesarrollo de la Producción Animal, School of Veterinary Medicine, Universidad Autónoma Metropolitana-Xochimilco, México
Departamento de Investigación Experimental y Bioterio, Instituto Nacional de Ciencias Médicas y Nutrición Salvador Zubirán, México
Division of Clinical Pharmacology and Toxicology, The Hospital for Sick Children, 555 University Ave., Toronto, Ontario M5G 1X8, Canada
EIAH-Benemérita Universidad Autónoma de Puebla, San Juan Acateno, Teziutlan, Puebla, México
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Department of Animal Production and Agriculture, Research Area: Ecodesarrollo de la Producción Animal, School of Veterinary Medicine, Universidad Autónoma Metropolitana-Xochimilco, México
Departamento de Investigación Experimental y Bioterio, Instituto Nacional de Ciencias Médicas y Nutrición Salvador Zubirán, México
Division of Clinical Pharmacology and Toxicology, The Hospital for Sick Children, 555 University Ave., Toronto, Ontario M5G 1X8, Canada
EIAH-Benemérita Universidad Autónoma de Puebla, San Juan Acateno, Teziutlan, Puebla, México
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region of either 1 ml saline ( n =10 sows) or 6 mg/day recombinant porcine ST (rpST) (Reporcin, Alpharma Animal Health Pty. Ltd, Victoria, Australia) in 1 ml saline ( n =10 sows) from days 80 to 114 of gestation. The dose of rpST had previously been
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Thyrotrophin (TSH) receptors have been extracted from human and porcine thyroid membranes by treatment with Triton X-100.125I-Labelled bovine TSH was used to monitor receptor activity. Analysis by gel filtration and electrophoresis on acrylamide gels containing sodium dodecyl sulphate suggested that Triton extracts of human thyroid membranes contained TSH receptors with a molecular weight in the region of 50 000 closely associated with Triton micelles of approximate molecular weight 300 000. Isoelectric focusing studies indicated that the Triton-solubilized TSH binding activity had an isoelectric point of pH 4–4·5. The soluble TSH receptors were heat-labile, showed optimum TSH binding at pH 7·4 and reduced hormone binding at high ionic strength. The TSH binding characteristics of membrane-bound and solubilized human TSH receptors were similar and both preparations gave curved Scatchard plots.
Solubilized porcine TSH receptors appeared to have a similar molecular weight to the human receptors and were also closely associated with Triton micelles of approximate molecular weight 300 000. Scatchard analysis of TSH binding to membrane-bound or solubilized porcine TSH receptors gave approximately linear plots with association constants of 2·8 ± 0·95 (s.e.m.) × 109 and 1·7 ± 0·27 × 1091/mol respectively. Comparison of the binding capacities of the solubilized and membrane-bound porcine receptors indicated that the 0·5% Triton extracts contained 40% of the original TSH binding activity and that this was present at a concentration of 25 ng/ml.
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SUMMARY
A method is described for the isolation of a purified luteinizing hormone (LH) from the anterior lobes of porcine pituitary glands. This includes fractional precipitation, gel filtration and isoelectric focusing. The preparation, which can be recovered in a fairly short time, is of high potency (equivalent to 3·4 mg standard NIH-LH-B7/mg and 6800 i.u. LH/mg).
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Antisera were raised against highly purified preparations of porcine luteinizing hormone (pLH) and follicle-stimulating hormone (pFSH). Highly specific and sensitive radioimmunoassay systems were developed.
The antisera to LH and FSH were used at working dilutions of 1: 500 000 and 1: 200 000 respectively and the sensitivities of the assays were 0·1 ng LH/ml serum (3 × 10−12 mol/l) and 0·5 ng FSH/ml serum (1·5 × 10−11 mol/l). The LH and FSH preparations used as standards were 1·2 and 81 times as potent as NIH-LH-S15 and NIH-FSH-P1 respectively. Both assays were validated and adapted for the measurement of the gonadotrophin content of porcine serum.
The concentrations of LH and FSH in blood were measured simultaneously in prepubertal sows throughout a 24 h period, in adult sows during the oestrous cycle and in both prepubertal and adult animals after treatment with LH releasing hormone.
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SUMMARY
Whereas the liver is the major site of accumulation of 125I-labelled porcine calcitonin soon after injection in the rat, both human and salmon calcitonin were rapidly taken up in rat kidney, with relatively insignificant amounts found in the liver.
In-vitro studies of degradation of 125I-labelled calcitonins showed that human calcitonin was readily degraded by most rat tissues but the major activity was found in a kidney microsomal fraction, whereas the liver supernatant was most active towards pig calcitonin. Salmon calcitonin was resistant to breakdown by all tissues and fractions except the kidney microsomal fraction, which rapidly degraded it to trichloroacetic acid-soluble fragments. Liver homogenates from a number of mammalian and non-mammalian species degraded pig calcitonin but had little effect on salmon calcitonin.
The results show that the kidney is the most important organ in the metabolism of human and salmon calcitonin in the rat, while confirming that the liver is mainly responsible for the metabolism of porcine calcitonin.
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IGF-binding protein (IGFBP)-3 is produced by cultured porcine embryonic myogenic cell (PEMC) cultures and is secreted into the medium. Levels of secreted IGFBP-3 and IGFBP-3 mRNA are significantly reduced during differentiation and increase after differentiation is complete, suggesting that IGFBP-3 may play some role in myogenesis and/or in changes in myogenic cell proliferation that accompany differentiation. IGFBP-3 reportedly may either suppress or stimulate proliferation of cultured cells depending on cell type. Additionally, IGFBP-3 has been shown to affect proliferation via both IGF-dependent and IGF-independent mechanisms in some cell types but not all. Currently, the effect, if any, of IGFBP-3 on myogenic cell proliferation is not known. Consequently, the goal of this study was to assess the IGF-I-dependent and IGF-I-independent actions of recombinant porcine IGFBP-3 on proliferation of cultured porcine myogenic cells. To facilitate these investigations, we have expressed porcine IGFBP-3 in the baculovirus system, purified and characterized the expressed recombinant porcine IGFBP-3 (rpIGFBP-3), and produced and characterized an anti-porcine IGFBP-3 antibody that neutralizes the biological activity of porcine IGFBP-3. rpIGFBP-3 suppressed IGF-I-stimulated proliferation of PEMCs in a concentration-dependent manner with equimolar concentrations of IGF-I and rpIGFBP-3, resulting in complete suppression of IGF-I-stimulated proliferation. rpIGFBP-3 also suppressed Long-R3-IGF-I-stimulated proliferation of PEMC, indicating that rpIGFBP-3 possesses IGF-independent activity in this cell system. These data have established that IGFBP-3 has the potential to affect proliferation of PEMCs during critical periods of muscle development that may impact ultimate muscle mass achievable postnatally.
