Organ Culture in the Study of the Gastrointestinal Tract in Health and Disease

Howdle, P D

doi:10.1042/cs0650105

Cited by 10 publications

(4 citation statements)

References 30 publications

(35 reference statements)

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“…Although organ culture techniques have substantially lenghtened the period in which steady-state conditions could be maintained for the study of gastric digestive functions in comparison with isolated gastric glands (Chew and Hersehy, 1982;Defize et al, 1984;Donaldson and Kapadia, 1980;Finks et al, 1985;Trier, 1976), this technique has not been found very satisfactory because degenerative changes already occur within the first 6 -24 hours (Finks et al, 1985;Howdle, 1983;Kasbekar et al, 1983;Sutton and Donaldson, 1975). We clearly established that human fetal gastric explants can be maintained in serum-free organ culture for at least 15 days (Ménard et al, 1993).…”

Section: Serum-free Organ Culturementioning

confidence: 96%

Establishment of culture systems of human gastric epithelium for the study of pepsinogen and gastric lipase synthesis and secretion

Basque

Ménard

2000

Microsc. Res. Tech.

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A main purpose of gastric secretion pertains to the digestion of dietary proteins and involves the release of pepsinogens by the fundic and antral mucosa. Over the last decade, data on human gastric physiology has expanded to equally include a significant role in fat digestion. Characteristics of human gastric lipase (HGL) such as optimum acid pH, resistance to proteolysis and non requirement of bile salts or cofactors, are advantageous in gastric lipolysis. Furthermore, the importance of HGL increases in the context of perinatal physiology and pathological situations where secretion of HGL could compensate, to some extent the depressed pancreatic activities. It is therefore important to understand the regulatory mechanisms involved in the synthesis and secretion of human gastric digestive enzymes. The establishment of an organ culture technique as well as a novel primary culture system of human gastric epithelium permitted us to demonstrate that Pg5 and HGL are colocalized in human chief cells and both digestive enzymes are efficiently synthesized and secreted in explants and primary cultures. Pepsin activity rises at the cellular level while its secretion remains constant. In contrast, cellular lipase activity drastically diminishes while being preferentially secreted. This nonparallelism supports the concept that Pg5 and HGL are differently regulated in culture. Furthermore, EGF downregulates HGL expression at the mRNA level via the p42/44MAPK pathway without affecting Pg5. Future studies should be designed to fully understand the cellular and molecular mechanisms involved in regulating HGL activity in normal and pathological conditions. Microsc. Res. Tech. 48:293–302, 2000 © 2000 Wiley‐Liss, Inc.

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Section: Serum-free Organ Culturementioning

confidence: 96%

Establishment of culture systems of human gastric epithelium for the study of pepsinogen and gastric lipase synthesis and secretion

Basque

Ménard

2000

Microsc. Res. Tech.

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“…These results have not been reproduced by others (15,16). The assessment of gluten toxicity by immunological tests such as LlF (leu-kocyte migration inhibiting factor) ( 17) has not been generally accepted, as immunological pro perties and pat hoge nic effects of gliadin fractions are not identi cal (12,13).…”

Section: Discussionmentioning

confidence: 94%

Effects of Gliadin Peptides B1‐B4 in Celiac Disease.

Stallmach,

Belitz,

Gellermann

et al. 1987

J. pediatr. gastroenterol. nutr.

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SummarySmall intestinal organ culture was used as an in vitro system to study the enterotoxic effects of gliadin peptides. Measurement of enterocyte height proved to be a reliable and reproducible way of assessing mucosal change during organ culture. Enterocyte height decreases nonspecifically in normal cultured mucosa, whereas the height of enterocytes of celiac mucosa increases in vitro in controls. All the gliadin peptide fractions (B1, B2, B3, B4) that had been prepared by peptic‐tryptic hydrolysis, ultrafiltration, and gel chromatography, equally inhibited the morphological increase of enterocyte height normally observed without gliadin in untreated celiac mucosa. Electrophoretic studies and amino acid analysis of B1‐B4 revealed similarity between gliadin fractions with quantitative differences in molecular weight distribution of the peptide components. Our studies suggest that organ culture assessed by morphometry is a suitable model for the investigation of toxic peptides of gliadin in celiac disease. In the future, pure gliadin peptides will have to be examined.

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“…In the past two decades, in vitro models have been increasingly used in attempt to study gastric mucosal functions in defined conditions. Although organ culture techniques have substantially lenghtened the period in which steady-state conditions could be maintained for the study of gastric digestive functions in comparison with isolated gastric glands (Chew and Hersehy, 1982;Defize et al, 1984;Donaldson and Kapadia, 1980;Finks et al, 1985;Trier, 1976), this technique has not been found very satisfactory because degenerative changes already occur within the first 6 -24 hours (Finks et al, 1985;Howdle, 1983;Kasbekar et al, 1983;Sutton and Donaldson, 1975). We clearly established that human fetal gastric explants can be maintained in serum-free organ culture for at least 15 days (Ménard et al, 1993).…”

Section: Serum-free Organ Culturementioning

confidence: 99%

Establishment of culture systems of human gastric epithelium for the study of pepsinogen and gastric lipase synthesis and secretion

Basque¹,

Ménard²

2000

Microsc. Res. Tech.

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A main purpose of gastric secretion pertains to the digestion of dietary proteins and involves the release of pepsinogens by the fundic and antral mucosa. Over the last decade, data on human gastric physiology has expanded to equally include a significant role in fat digestion. Characteristics of human gastric lipase (HGL) such as optimum acid pH, resistance to proteolysis and non requirement of bile salts or cofactors, are advantageous in gastric lipolysis. Furthermore, the importance of HGL increases in the context of perinatal physiology and pathological situations where secretion of HGL could compensate, to some extent the depressed pancreatic activities. It is therefore important to understand the regulatory mechanisms involved in the synthesis and secretion of human gastric digestive enzymes. The establishment of an organ culture technique as well as a novel primary culture system of human gastric epithelium permitted us to demonstrate that Pg5 and HGL are colocalized in human chief cells and both digestive enzymes are efficiently synthesized and secreted in explants and primary cultures. Pepsin activity rises at the cellular level while its secretion remains constant. In contrast, cellular lipase activity drastically diminishes while being preferentially secreted. This nonparallelism supports the concept that Pg5 and HGL are differently regulated in culture. Furthermore, EGF downregulates HGL expression at the mRNA level via the p42/44(MAPK) pathway without affecting Pg5. Future studies should be designed to fully understand the cellular and molecular mechanisms involved in regulating HGL activity in normal and pathological conditions.

show abstract

Organ Culture in the Study of the Gastrointestinal Tract in Health and Disease

Cited by 10 publications

References 30 publications

Establishment of culture systems of human gastric epithelium for the study of pepsinogen and gastric lipase synthesis and secretion

Establishment of culture systems of human gastric epithelium for the study of pepsinogen and gastric lipase synthesis and secretion

Effects of Gliadin Peptides B1‐B4 in Celiac Disease.

Establishment of culture systems of human gastric epithelium for the study of pepsinogen and gastric lipase synthesis and secretion

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