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Author |
Pere, M.C. |
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Title |
Maternal and fetal blood levels of glucose, lactate, fructose, and insulin in the conscious pig |
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Journal Article |
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Year |
1995 |
Publication |
Journal of Animal Science |
Abbreviated Journal |
J. Anim Sci. |
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Volume |
73 |
Issue |
10 |
Pages |
2994-2999 |
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Keywords |
Animals; Blood Glucose/*analysis; Catheterization/methods/veterinary; Consciousness/physiology; Female; Fetal Blood/*chemistry; Fructose/analysis/*blood; Insulin/analysis/*blood; Lactates/analysis/*blood; Pregnancy; Swine/*blood/physiology |
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Abstract  |
To study nutrition and metabolism in the fetal pig, a chronic catheterization method was developed that allows blood sampling in arteries and veins, at both the umbilical and uterine sources, in the conscious, unstressed animal. A catheter was inserted in the fetal aorta through a femoral artery, and another one was introduced in the umbilical vein. A catheter was put in a femoral artery of the sow so that its end was in the abdominal aorta. A fourth catheter was placed in a uterine vein draining the fetoplacental unit studied. This procedure was applied to 18 Large White primiparous sows at 99 d of gestation. Blood samples were drawn simultaneously using the four catheters before a meal at 103 d of pregnancy, and glucose, insulin, lactate, and fructose were determinated. Glycemia was 2.5 times higher in the sow than in the fetus. The extraction coefficient of glucose by the fetus amounted to 14% of the umbilical supply. The insulin level in the fetal pig was very low ( < 5 microU/mL). Lactate and fructose seemed to originate from the placenta. Blood lactate was 2.6 times lower in the sow than in the fetus, and its extraction coefficient by the fetus amounted to 8%. Fructose in the fetal blood was 2.3 times higher than that of glucose. Fructose was not utilized by the pig fetus. The present results obtained in the fetal pig are comparable to the conclusions drawn from studies with other species. |
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Station de Recherches Porcines, Institut National de la Recherche Agronomique, Saint-Gilles, France |
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0021-8812 |
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PMID:8617670 |
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Call Number |
Equine Behaviour @ team @ |
Serial |
2751 |
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Author |
Hostikka, S.L.; Eddy, R.L.; Byers, M.G.; Hoyhtya, M.; Shows, T.B.; Tryggvason, K. |
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Title |
Identification of a distinct type IV collagen alpha chain with restricted kidney distribution and assignment of its gene to the locus of X chromosome-linked Alport syndrome |
Type |
Journal Article |
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Year |
1990 |
Publication |
Proceedings of the National Academy of Sciences of the United States of America |
Abbreviated Journal |
Proc. Natl. Acad. Sci. U.S.A. |
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Volume |
87 |
Issue |
4 |
Pages |
1606-1610 |
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Keywords |
Amino Acid Sequence; Base Sequence; Chromosome Mapping; Cloning, Molecular; Collagen/*genetics; Epitopes/analysis; Female; Fluorescent Antibody Technique; Gene Library; *Genes; Humans; Immunoblotting; Kidney/cytology/*metabolism; Macromolecular Substances; Molecular Sequence Data; Nephritis, Hereditary/*genetics; Oligopeptides/chemical synthesis/immunology; Placenta/metabolism; Pregnancy; Restriction Mapping; Sequence Homology, Nucleic Acid; *X Chromosome |
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Abstract |
We have identified and extensively characterized a type IV collagen alpha chain, referred to as alpha 5(IV). Four overlapping cDNA clones isolated contain an open reading frame for 543 amino acid residues of the carboxyl-terminal end of a collagenous domain, a 229-residue carboxyl-terminal noncollagenous domain, and 1201 base pairs coding for a 3' untranslated region. The collagenous Gly-Xaa-Yaa repeat sequence has five imperfections that coincide with those in the corresponding region of the alpha 1(IV) chain. The noncollagenous domain has 12 conserved cysteine residues and 83% and 63% sequence identity with the noncollagenous domains of the alpha 1(IV) and alpha 2(IV) chains, respectively. The alpha 5(IV) chain has less sequence identity with the putative bovine alpha 3(IV) and alpha 4(IV) chains. Antiserum against an alpha 5(IV) synthetic peptide stained a polypeptide chain of about 185 kDa by immunoblot analysis and immunolocalization of the chain in human kidney was almost completely restricted to the glomerulus. The gene was assigned to the Xq22 locus by somatic cell hybrids and in situ hybridization. This may be identical or close to the locus of the X chromosome-linked Alport syndrome that is believed to be a type IV collagen disease. |
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Biocenter, University of Oulu, Finland |
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0027-8424 |
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PMID:1689491 |
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Call Number |
Equine Behaviour @ team @ |
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5291 |
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