lactoferrin and Gastritis--Atrophic

A total of 238 randomly selected gastric biopsies were examined with polyclonal antibodies from rabbits (antihuman-lysozyme and antihuman-lactoferrin) using the Peroxidase-Antiperoxidase-method according to Sternberger. The preparations were evaluated by comparing the intensity of the staining as well as the quantity and distribution of positive cells within the mucosa. The results show that lysozyme can be demonstrated constantly in the glandular neck zone and in the mucoid glandular body within the normal non-inflamed mucosa of the antrum, whereas in the normal corpus mucosa only a small amount of lysozyme appears focally and inconsistently in the neck area of the glands. A substantial increase in the intensity of lysozyme presentation due to inflammatory changes as related to the chronic superficial gastritis of the antrum cannot be discovered. On the contrary, the presentable amount of lysozyme decreases in line with the progressing inflammation and, in case of chronic-atrophic gastritis with intestinal metaplasia is restricted to the Paneth cells. A distinct and constant presentation of lysozyme can be achieved in the glandular neck zone, in the lower gastric pits and partially in the upper glandular body of the corpus mucosa in cases of chronic inflammatory processes. Obviously lysozyme is formed in the epithelial cells and not taken up from other cells. Furthermore it can be concluded from the findings that to a large extent lysozyme formation is linked to the proliferation activity of the epithelial cells. Lactoferrin cannot be found in normal non-inflammatory mucosa neither of the antrum nor of the corpus. But it can be found among most of the biopsy specimens with inflammatory changes.(ABSTRACT TRUNCATED AT 250 WORDS)

Topics: Adolescent; Adult; Aged; Aged, 80 and over; Biopsy; Campylobacter Infections; Female; Gastric Mucosa; Gastritis; Gastritis, Atrophic; Granulocytes; Humans; Immunoenzyme Techniques; Lactoferrin; Lactoglobulins; Male; Metaplasia; Middle Aged; Muramidase