Distribution of vasoactive intestinal polypeptide and substance P receptors in human colon and small intestine

• Published in: Digestive diseases and sciences Vol. 34; no. 7; p. 1100
• Main Authors: Korman, L Y, Sayadi, H, Bass, B, Moody, T W, Harmon, J W
• Format: Journal Article
• Language: English
• Published: United States 01.07.1989
• Subjects: Autoradiography; Colon - metabolism; Humans; Intestinal Mucosa - metabolism; Intestine, Small - metabolism; Iodine Radioisotopes; Muscle, Smooth - metabolism; Receptors, Gastrointestinal Hormone - metabolism; Receptors, Neurokinin-1; Receptors, Neurotransmitter - metabolism; Receptors, Vasoactive Intestinal Peptide; Substance P - metabolism; Vasoactive Intestinal Peptide - metabolism
• ISSN: 0163-2116
• DOI: 10.1007/BF01536382

Vasoactive intestinal polypeptide (VIP) and substance P are found in neurons in the lamina propria and submucosa and muscularis propria of human small intestine and colon. VIP receptors coupled to adenylate cyclase are present on epithelial, smooth muscle, and mononuclear cells. This study analyzes the distribution of [125I]VIP binding and [125I]substance P in human colon and small intestine using autoradiographic techniques. [125I]VIP binding was present in high density in the mucosal layer of colon and small intestine. [125I]VIP binding was not significantly greater than nonspecific binding in smooth muscle layers or the lymphoid follicles. In contrast, [125I]substance P binding was present in high density over the colonic muscle but was not present over the mucosal layer. In human colon cancer, [125I]VIP grain density over the malignant tissue was only slightly higher than background. These autoradiographic studies of [125I]VIP binding indicate that the highest density of VIP receptors was found in the small intestine and superficial colonic mucosa, whereas the density of substance P receptors was highest over the smooth muscle layers. These findings suggest a mismatch between immunochemical content of the peptide and autoradiographic density of the receptor.