The influence of lactation products on the temporal expression of histo-blood group antigens in the intestines of suckling pigs: lectin histochemical and immunohistochemical analysis

Abstract

Lectins and carbohydrate-specific monoclonal antibodies were used as cytochemical probes to investigate the possible influence of lactation products on the expression of intestinal membrane and secretory glycoconjugates in suckling piglets. Two different lactational regimes were compared; the first involved normal rearing of piglets for 8 weeks on a single dam and the second involved repeated cross-fostering of littermates onto recently farrowed sows, thereby restricting them to early milk. Five histo-blood group phenotypes were recognized within the piglet population: two immature phenotypes, 'O immature' or 'Oi' and 'A immature' or 'Ai', and three mature forms, 'O', 'A' and '-'. Under the normal suckling regime the transition from immature to mature OA phenotypes was evident at the fifth week post partum. However, in the repeatedly cross-fostered piglets this transition was evident much earlier at 3 weeks post partum. It is suggested that qualitative or quantitative variations in milk composition during the sow's lactation may significantly influence the expression of intestinal histo-blood group antigens in her suckling young.

Effect of Preclosure Colostrum Intake on the Development of the Intestinal Epithelium of Artificially Reared Piglets

“…Evidently, the ingestion of colostral pro teins in the first 24 h promoted an initial and rapid decline in lactase but did not induce longer term precocious changes in this en zyme or in membrane glycosylation. This sug gests that sustained exposure to colostrum/ early milk is necessary to fully entrain the more marked effect on lactase and glycosyla tion we previously reported [10,28], This contrasts with the effect on sucrase where fol lowing postnatal colostrum ingestion, en hanced activity of the enzyme was sustained throughout the experimental period.…”

“…In our pre vious investigations we observed that both the normal postnatal decline in lactase activity, and the fucosylation of microvillar glycoconjugates were precociously enhanced when piglets ingested early lactation milk [ 10,20,28]. In the present study the marked decrease in lactase activity in CF pigs occurred at week 1 post parturn, well before membrane fucosylation was detected in the cytochemical assays.…”

“…Although a highly significant drop in lac tase activity was detected in the CF group at week 1 post partum, the enzyme levels and the glycosylation patterns in both CF and CD groups at weeks 3 and 5 were similar to the values from normally suckled individuals [20,28]. Evidently, the ingestion of colostral pro teins in the first 24 h promoted an initial and rapid decline in lactase but did not induce longer term precocious changes in this en zyme or in membrane glycosylation.…”

Effect of Fermented Feed on the Microbial Population of the Gastrointestinal Tracts of Pigs

“…This indicates that other lactobacilli than L. plantarum were present. The presence of these lactobacilli can be due to changes in the available substrates or products (14,18) or alterations in the intestine, e.g., diet-induced intestinal glycosylation (12) or epithelial proliferation by VFA (27). The influence of L. plantarum on Enterobacteriaceae in the GIT is difficult to explain from the results of this experiment.…”

Effect of nonpathogenic Escherichia coli monoassociation on small intestinal brush-border glycoconjugate moieties and cytokine production after colonization in ex-germ-free rats and pigs

“…Both FUT1 and FUT2 contribute to formation of α1,2-fucosylated antigenic structures 40 as determinants of pig erythrocyte blood groups, whose full expression was evident at 5-8 weeks of life. [42][43][44] Binding specificity of AAL with AAL-Sepharose column 45 and crystal structure of the complex between AAL and fucose 46 showed that this lectin recognizes not only α1,6-core fucosylated N-linked glycoproteins but also α1,2-, α1,3-, and α1,4-fucosylated residues. The broader range of fucose potential binding sites of AAL indicates that also some mucin O-glycans, important for adhesion, cell signaling, and defining various blood group epitopes, react with AAL.…”