Scandinavian journal of gastroenterology · 1996
In vitro hydrolysis of gliadin and casein peptides: secondary defect in coeliac disease shown by organ culture.
СтатьяПоддержка исследования: вне правительства СШАНазвание и аннотация: Перевод пока не подготовлен
Обработка статьи · этапы, ошибки и управление
Загрузка состояния…
Ошибки и ограничения
История · было → стало
Состояние обновляется каждые 5 секунд, пока блок открыт. Процент показывается только там, где известен объём работы. Пауза останавливает продолжение этапа; текущий запрос к источнику может завершиться.
Walz F, Wieser H, Stern M
Аннотация
BACKGROUND: Small-intestinal organ culture was used as an in vitro model of coeliac disease, studying biopsy specimens from patients with coeliac disease, cow's milk allergy, and controls.
METHODS: Organ culture incubations were done using the pure gliadin peptide B3144 (amino acid sequences 3-56 of alpha-type gliadins) and a control peptide from casein (amino acid sequences 152-193 of alpha s1-casein). The importance of using negative controls was stressed by non-specific tissue damage. By reversed-phase high-performance liquid chromatography of organ culture supernatants, 27 specimens were further investigated.
RESULTS: There was good retrieval of peptide calibration peaks after culture. Qualitative and quantitative evaluation of chromatography runs showed degradation of at least 29% of B3144 and 37% of Cas-P. Normal mucosa (controls and coeliac patients on a gluten-free diet) was able to hydrolyse peptide fractions completely, whereas incubation with damaged mucosa (coeliac disease, cow's milk allergy) left initial peptides.
CONCLUSION: It is concluded, using a pure single gliadin peptide, that deficient peptide hydrolysis in coeliac disease was a secondary event.
METHODS: Organ culture incubations were done using the pure gliadin peptide B3144 (amino acid sequences 3-56 of alpha-type gliadins) and a control peptide from casein (amino acid sequences 152-193 of alpha s1-casein). The importance of using negative controls was stressed by non-specific tissue damage. By reversed-phase high-performance liquid chromatography of organ culture supernatants, 27 specimens were further investigated.
RESULTS: There was good retrieval of peptide calibration peaks after culture. Qualitative and quantitative evaluation of chromatography runs showed degradation of at least 29% of B3144 and 37% of Cas-P. Normal mucosa (controls and coeliac patients on a gluten-free diet) was able to hydrolyse peptide fractions completely, whereas incubation with damaged mucosa (coeliac disease, cow's milk allergy) left initial peptides.
CONCLUSION: It is concluded, using a pure single gliadin peptide, that deficient peptide hydrolysis in coeliac disease was a secondary event.