Angiotensin receptors and angiotensin I-converting enzyme in rat intestine
Autor: | Frederick A. O. Mendelsohn, N R Levens, K A Duggan |
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Rok vydání: | 1989 |
Předmět: |
Male
Angiotensin receptor medicine.medical_specialty Colon Duodenum Physiology Ileum Peptidyl-Dipeptidase A Binding Competitive Iodine Radioisotopes Jejunum Physiology (medical) Internal medicine medicine Animals Intestinal Mucosa Receptors Angiotensin Hepatology biology Angiotensin II Gastroenterology Lisinopril Muscle Smooth Rats Inbred Strains Angiotensin-converting enzyme Small intestine Rats Kinetics medicine.anatomical_structure Endocrinology biology.protein Autoradiography hormones hormone substitutes and hormone antagonists medicine.drug |
Zdroj: | American Journal of Physiology-Gastrointestinal and Liver Physiology. 257:G504-G510 |
ISSN: | 1522-1547 0193-1857 |
Popis: | The purpose of this study was to map the distribution of angiotensin II (ANG II) receptors and ANG I-converting enzyme (ACE) in rat intestine. ANG II binding sites were visualized by in vitro autoradiography using iodinated [Sar1, Ile8]ANG II. The distribution of ACE was mapped using an iodinated derivative of lisinopril. Male Sprague-Dawley rats were killed and the interior of the whole intestine washed with ice-cold saline. Segments of duodenum, jejunum, ileum, and colon were quickly frozen in a mixture of isopentane and dry ice. Twenty-micron frozen sections were thaw-mounted onto gelatin-coated slides, incubated with either ligand, and exposed to X-ray film. After exposure and subsequent development, the films were quantitated by computerized densitometry. ANG II receptors were most dense in the colon, followed by the ileum, duodenum, and jejunum. Within each segment of intestine, specific ANG II binding sites were localized exclusively to the muscularis. In contrast, ACE was present in both the mucosa and the muscularis. The colocalization of ANG II receptors and ACE may suggest a role for locally generated ANG II in the control of intestinal function. The luminal orientation of ACE in the mucosa of the small intestine may suggest that at this site ACE serves primarily to hydrolyze dietary peptides. |
Databáze: | OpenAIRE |
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