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1.
J Biol Chem ; 275(41): 32106-13, 2000 Oct 13.
Article in English | MEDLINE | ID: mdl-10851241

ABSTRACT

A novel mammalian galectin cDNA (ovgal11) was isolated by representational difference analysis from sheep stomach (abomasal) tissue infected with the nematode parasite, Haemonchus contortus. The mRNA is greatly up-regulated in helminth larval infected gastrointestinal tissue subject to inflammation and eosinophil infiltration. Immunohistological analysis indicates that the protein is localized in the cytoplasm and nucleus of upper epithelial cells of the gastrointestinal tract. The protein is also detected in mucus samples collected from infected abomasum but not from uninfected tissue. The restricted and inducible expression of ovgal11 mRNA and limited secretion of the protein support the hypothesis that OVGAL11 may be involved in gastrointestinal immune/inflammatory responses and possibly protection against infection.


Subject(s)
Haemonchiasis/genetics , Hemagglutinins/genetics , Hemagglutinins/isolation & purification , Sheep/genetics , Up-Regulation , Abomasum/immunology , Abomasum/metabolism , Abomasum/parasitology , Abomasum/pathology , Amino Acid Sequence , Animals , Base Sequence , Blotting, Western , Cell Nucleus/chemistry , Cloning, Molecular , Cytoplasm/chemistry , Galectins , Gene Expression Profiling , Haemonchiasis/immunology , Haemonchiasis/metabolism , Haemonchiasis/veterinary , Haemonchus/immunology , Haemonchus/physiology , Hemagglutinins/chemistry , Hemagglutinins/immunology , Immunohistochemistry , Inflammation/immunology , Inflammation/metabolism , Inflammation/parasitology , Inflammation/pathology , Intestinal Mucosa/immunology , Intestinal Mucosa/metabolism , Intestinal Mucosa/parasitology , Intestinal Mucosa/pathology , Molecular Sequence Data , RNA, Messenger/genetics , RNA, Messenger/metabolism , Sequence Alignment , Sheep/immunology , Sheep/parasitology
2.
J Surg Res ; 87(1): 130-3, 1999 Nov.
Article in English | MEDLINE | ID: mdl-10527714

ABSTRACT

BACKGROUND: Glucagon-like peptide 2 (GLP-2) has recently been shown to be a potent enterotrophic factor that may mediate mucosal hyperplasia during intestinal adaptation. The intestinal brush-border protease dipeptidyl peptidase IV (DPP IV) cleaves GLP-2 to an inactive form. It has been postulated that DPP IV activity limits the enterotrophic activity of GLP-2 in rats and humans. Massive small bowel resection (MSBR) in rats is an animal model of intestinal adaptation that has been used successfully to characterize factors involved in the modulation of adaptation. METHODS: Total RNA was extracted from normal terminal ileum or terminal ileum post-MSBR from Sprague-Dawley rats which were sacrificed 2, 4, and 7 days postresection. A partial rat DPP IV clone was isolated by reverse transcription polymerase chain reaction, and Northern blot analysis of rat DPP IV mRNA levels in normal small bowel and small bowel post-MSBR was performed. RESULTS: Within normal small bowel, DPP IV mRNA levels were greatest in the terminal ileum; levels in the duodenum and jejunum were approximately 50% of those in the terminal ileum. DPP IV mRNA levels decreased in terminal ileum post-MSBR 2, 4, and 7 days after resection. CONCLUSION: The decreased DPPIV gene expression suggests a novel mechanism by which the effects on mucosal growth of GLP-2 may be further enhanced, and further that GLP-2 may be a more useful therapeutic agent in humans than currently anticipated.


Subject(s)
Adaptation, Physiological , Dipeptidyl Peptidase 4/genetics , Intestines/physiology , Intestines/surgery , RNA, Messenger/analysis , Animals , Glucagon/metabolism , Glucagon-Like Peptide 1 , Glucagon-Like Peptide 2 , Glucagon-Like Peptides , Intestines/enzymology , Peptide Fragments/metabolism , Peptides/metabolism , Protein Precursors/metabolism , Rats , Rats, Sprague-Dawley
3.
Mol Cell Endocrinol ; 141(1-2): 179-86, 1998 Jun 25.
Article in English | MEDLINE | ID: mdl-9723898

ABSTRACT

The regulation of glucose metabolism by glucagon and GLP-1 is well established, but novel functions for these and other proglucagon-derived peptides are less well defined. This paper highlights the diversity of both GLP-1 and glucagon activity by studying the tissue distribution of glucagon and GLP-1 receptor gene expression by both Southern blot analysis of RT-PCR products and nuclease protection assays. By Southern blot analysis of RT-PCR products, GLP-1 receptor mRNA was detected in lung, hypothalamus, hippocampus, cerebral cortex, kidney, pancreas, and throughout the gastrointestinal tract. Glucagon receptor expression was detected in liver, kidney, spleen, thymus, adrenal glands, pancreas, cerebral cortex, lung, and throughout the gastrointestinal tract. Nuclease protection assay revealed glucagon receptor expression to be highest in liver and kidney, whereas GLP-1 receptor expression was only detected by protection assay in lung, stomach, and large bowel. Despite previous evidence that other receptors for proglucagon-derived peptides may exist, no evidence of novel receptors or multiple isoforms of the glucagon and GLP-1 receptors was found, indicating that the two cloned receptors may mediate all the effects of proglucagon-derived peptides, or that novel receptors may share less homology with the glucagon and GLP-1 receptors than previously anticipated.


Subject(s)
Receptors, Glucagon/genetics , Animals , Base Sequence , Blotting, Southern , DNA Primers , DNA Probes , Glucagon-Like Peptide-1 Receptor , Nucleic Acid Hybridization , Organ Specificity , RNA, Messenger/analysis , Rats , Rats, Sprague-Dawley , Reverse Transcriptase Polymerase Chain Reaction , Sequence Homology, Nucleic Acid , Single-Strand Specific DNA and RNA Endonucleases
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