Intravenous but not intragastric urogastrone-EGF is trophic to the intestine of parenterally fed rats

Goodlad, R A; Wilson, Thomas J.; Lenton, W; Gregory, H.; McCullagh, K.G.; Wright, Nicholas

doi:10.1016/0167-0115(84)90110-1

Cited by 38 publications

(66 citation statements)

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“…41,42 Altered glycosylation may directly affect the synthesis and stability of the core protein, syndecan-1, or it may be indirect because many of the HS biosynthetic enzymes in the Golgi are most likely N-linked glycosylated. Intracellular accumulation of the small amount of residual HS-immunoreactive material in the nuclear region, perhaps the Golgi, suggests that the sulfated chains do not reach the surface.…”

Section: Discussionmentioning

confidence: 99%

Reduced Heparan Sulfate Accumulation in Enterocytes Contributes to Protein-Losing Enteropathy in a Congenital Disorder of Glycosylation

Westphal

Murch

Kim

et al. 2000

The American Journal of Pathology

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Intestinal biopsy in a boy with gastroenteritis-induced protein-losing enteropathy (PLE) showed loss of heparan sulfate (HS) and syndecan-1 core protein from the basolateral surface of the enterocytes, which improved after PLE subsided. Isoelectric focusing analysis of serum transferrin indicated a congenital disorder of glycosylation (CDG) and subsequent analysis showed three point mutations in the ALG6 gene encoding an ␣1,3-glucosyltransferase needed for the addition of the first glucose to the dolichol-linked oligosaccharide. The maternal mutation, C998T, causing an A333V substitution, has been shown to cause CDG-Ic, whereas the two paternal mutations, T391C (Y131H) and C924A (S308R) have not previously been reported. The mutations were tested for their ability to rescue faulty N-linked glycosylation of carboxypeptidase Y in an ALG6-deficient Saccharomyces cerevisiae strain. Normal human ALG6 rescues glycosylation and A333V partially rescues, whereas the combined paternal mutations (Y131H and S308R) are ineffective. Underglycosylation resulting from each of these mutations is much more severe in rapidly dividing yeast. Similarly, incomplete protein glycosylation in the patient is most severe in rapidly dividing enterocytes during gastroenteritis-induced stress. 1-4 These defects reduce the amount or change the structure of the lipid-linked oligosaccharide (LLO) precursor for N-linked glycosylation, leading to underglycosylation of many proteins, 3 including antithrombin-III, factor XI, or protein C. This reduces their levels, leaving patients at risk for coagulopathy. Mutations in phosphomannose isomerase (MPI, causing CDG-Ib) and phosphomannomutase (PMM2, causing CDG-Ia) reduce the amount of GDP-Man, the immediate precursor of LLO,5 thus reducing the amount of N-linked glycosylation. Mutations in ALG6, which encodes an ␣1,3-glucosyltransferase, cause CDG-Ic. 6 -8 This enzyme is required for the addition of the first of three glucose residues to LLO, and without the first glucose, further glucosylation is prevented. The nonglucosylated precursor oligosaccharide is a poor substrate for the oligosaccharyltransferase complex and is inefficiently transferred to proteins. 9,10

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Section: Discussionmentioning

confidence: 99%

Reduced Heparan Sulfate Accumulation in Enterocytes Contributes to Protein-Losing Enteropathy in a Congenital Disorder of Glycosylation

Westphal

Murch

Kim

et al. 2000

The American Journal of Pathology

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“…Therefore, in a second set of experiments, rats were given total parenteral nutrition (TPN) with or without supplements of TGF-x or EGF for 3 days, as described previously (Goodlad et al, 1987(Goodlad et al, , 1992. In brief, male Wistar rats (approximately 200 g) were anaesthetised with 0.7 ml of Hypnorm and 0.07 ml of diazepam (intraperitoneal route), and a silastic cannula was tied into the right external jugular vein.…”

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confidence: 99%

“…The PC1O antibody recognises a highly conserved epitope on both human and rodent PCNA. Autoradiography was performed using standard methods (Goodlad et al, 1987(Goodlad et al, , 1992. In brief, sections were dehydrated in alcohols containing 300 mM ammonium acetate, dried, dipped in Ilford K5 emulsion and exposed for 6-10 days at 4C before development in Kodak D19.…”

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confidence: 99%

“…The rats were housed individually in wire-bottomed cages. The TPN diet was pumped into the rats, from a refrigerator, by a multichannel peristaltic pump, at a rate of 60 ml per rat per day, giving 1.8 g of nitrogen, 6.0 g of lipid, 8.5 g of glucose and 1,047 kJ kg-' day-' (Goodlad et al, 1987). There were three groups of 11 rats in the second study, the first being the (TPN alone) controls; the second were given 275 jg kg-' TGF-a (J. Fritton, ICI Macclesfield, Cheshire, UK) and the third were given 300 ILg kg-' EGF (M. Edwards, British Biotechnology, Cowley, Oxford, UK).…”

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Proliferating cell nuclear antigen expression in non-cycling cells may be induced by growth factors in vivo

Hall

Coates²,

Goodlad³

et al. 1994

Br J Cancer

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Proliferating cell nuclear antigen (PCNA) is an evolutionarily conserved 36 kDa nuclear protein that by functioning as a co-factor for DNA polymerase 6 is an absolute requirement for semiconservative DNA synthesis (Bravo & MacDonaldBravo, 1987; Suzuka et al., 1989;Baserga, 1991 Levison, 1990;McCormick & Hall, 1992). The rationale for this approach is the ability of several anti-PCNA antibodies to recognise fixation-and processingresistant epitopes (Hall et al., 1990;McCormick & Hall, 1992), thus allowing the possibility of objectively quantifying the number of cycling cells in tissue sections. One particular commercially available antibody, clone PCIO , has been widely employed in pathology in this context.In the original description of the application of this reagent to pathological material, Hall et al. (1990) reported that, in addition to important technical caveats on its use, the number of PCIO-immunoreactive cells appeared to exceed that expected in certain situations, most notably in neoplasia. Part of the explanation for the expression of PCNA in non-cycling cells lies in the long half-life of the PCNA protein . Support for this interpretation was provided by detailed kinetic studies of tumour xenografts (Scott et al., 1991). It has also been shown that PCNA participates in DNA repair processes. Tightly bound PCNA can be found associated with chromatin at all phases of the cell cycle after UV irradiation in vitro (Celis & Madsen, 1986;Toschi & Bravo, 1988), and PCNA has been shown to an obligate requirement for DNA nucleotide excision repair (Shivji et al., 1992). PCNA may be expressed by non-cycling cells in vivo which are undergoing DNA repair (Hall et al., 1993). However, this cannot explain all the situations in which 'aberrant' PCNA expression has been observed.In several organs, notably breast, liver and pancreas, normal tissues adjacent to tumours show high levels of PCNA expression that appears not to be associated with proliferation (Hall et al., 1990;Pelosi et al., 1992;Harrison et al., 1993 25 Ci mmol ', Amersham International, Amersham, UK). One hour later the animals (n = 6) were killed and xenografts growing in the liver were removed, fixed in formalin and processed to paraffin for both immunostaining and autoradiography.It is known from previous studies that LoVo and HT-29 express growth factors similar to transforming growth factor (TGF-x) and epidermal growth factor (EGF) (Anano et al., 1989; Imanishi et al., 1989). Therefore, in a second set of experiments, rats were given total parenteral nutrition (TPN) with or without supplements of TGF-x or EGF for 3 days, as described previously (Goodlad et al., 1987(Goodlad et al., , 1992. In brief, male Wistar rats (approximately 200 g) were anaesthetised with 0.7 ml of Hypnorm and 0.07 ml of diazepam (intraperitoneal route), and a silastic cannula was tied into the right external jugular vein. The cannula was connected through a stainless-steel skin button and tethered to a fluid swivel joint (SMA, Barnet, UK). The rats were housed individu...

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“…It is signi¢cant that EGF should be produced locally around ulcers in the intestine, for several reasons. EGF is a very potent stimulator of cell proliferation in the rodent and human gastrointestinal mucosa (Walker-Smith et al 1985;Goodlad et al 1987), and also modulates intestinal epithelial cell di¡erentiation (Goodlad et al 1991). In normal conditions, EGF is produced by gut-associated salivary and Brunner's glands (Heitz et al 1978).…”

Section: Gene Expression In the Uacl (A) Genes Related To Di¡erentiationmentioning

confidence: 99%

Aspects of the biology of regeneration and repair in the human gastrointestinal tract

Wright

1998

Phil. Trans. R. Soc. Lond. B

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The main pathways of epithelial di¡erentiation in the intestine, Paneth, mucous, endocrine and columnar cell lineages are well recognized. However, in abnormal circumstances, for example in mucosal ulceration, a cell lineage with features distinct from these emerges, which has often been dismissed in the past as pyloric' metaplasia, because of its morphological resemblance to the pyloric mucosa in the stomach. However, we can conclude that this cell lineage has a de¢ned phenotype unique in gastrointestinal epithelia, has a histogenesis that resembles that of Brunner's glands, but acquires a proliferative organization similar to that of the gastric gland. It expresses several peptides of particular interest, including epidermal growth factor, the trefoil peptides TFF1, TFF2, TFF3, lysozyme and PSTI. The presence of this lineage also appears to cause altered gene expression in adjacent indigenous cell lineages. We propose that this cell lineage is induced in gastrointestinal stem cells as a result of chronic mucosal ulceration, and plays an important part in ulcer healing; it should therefore be added to the repertoire of gastrointestinal stem cells.

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Intravenous but not intragastric urogastrone-EGF is trophic to the intestine of parenterally fed rats

Cited by 38 publications

References 2 publications

Reduced Heparan Sulfate Accumulation in Enterocytes Contributes to Protein-Losing Enteropathy in a Congenital Disorder of Glycosylation

Reduced Heparan Sulfate Accumulation in Enterocytes Contributes to Protein-Losing Enteropathy in a Congenital Disorder of Glycosylation

Proliferating cell nuclear antigen expression in non-cycling cells may be induced by growth factors in vivo

Aspects of the biology of regeneration and repair in the human gastrointestinal tract

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