N-Acetyl-β-Glucosaminidase in the Small Intestine and its Changes during Postnatal Development of the Rat

Koldovský, Otakar; Herbst, John J.

doi:10.1159/000240296

Cited by 22 publications

(18 citation statements)

References 19 publications

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“…Classical biochemical studies identified the key enzymatic and transport pathways responsible for uptake and digestion of maternal milk by newborn mammals (31,35). In mice, the immature enterocyte profile becomes down-regulated beginning at approximately 2 wk after birth and rapidly shifts to the adult program during the third week of life (Fig.…”

Section: Discussionmentioning

confidence: 99%

“…S5A). The ability of the neonatal SI to absorb intact macromolecules via pinocytosis depends on lysosomal enzymes, including N-acetylgalactosaminidase (Naga), β-gal (Glb1), and β-glucuronidase (GusB) (31). These transcripts are strongly expressed during the suckling period, but decrease before weaning (Fig.…”

Section: Down-regulated Blimp1 Expression In Crypt Progenitors Beginnmentioning

confidence: 99%

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The transcriptional repressor Blimp1/Prdm1 regulates postnatal reprogramming of intestinal enterocytes

Harper

Mould

Andrews

et al. 2011

Proc. Natl. Acad. Sci. U.S.A.

127

153

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Female mammals produce milk to feed their newborn offspring before teeth develop and permit the consumption of solid food. Intestinal enterocytes dramatically alter their biochemical signature during the suckling-to-weaning transition. The transcriptional repressor Blimp1 is strongly expressed in immature enterocytes in utero, but these are gradually replaced by Blimp1− crypt-derived adult enterocytes. Here we used a conditional inactivation strategy to eliminate Blimp1 function in the developing intestinal epithelium. There was no noticeable effect on gross morphology or formation of mature cell types before birth. However, survival of mutant neonates was severely compromised. Transcriptional profiling experiments reveal global changes in gene expression patterns. Key components of the adult enterocyte biochemical signature were substantially and prematurely activated. In contrast, those required for processing maternal milk were markedly reduced. Thus, we conclude Blimp1 governs the developmental switch responsible for postnatal intestinal maturation.enterocyte maturation | gut development | nutrition | cell fate

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Section: Discussionmentioning

confidence: 99%

Section: Down-regulated Blimp1 Expression In Crypt Progenitors Beginnmentioning

confidence: 99%

The transcriptional repressor Blimp1/Prdm1 regulates postnatal reprogramming of intestinal enterocytes

Harper

Mould

Andrews

et al. 2011

Proc. Natl. Acad. Sci. U.S.A.

127

153

View full text Add to dashboard Cite

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“…Phenyl p-galactosidase activity was assayed as described by Asp (1971a) except that 0·1 M sodium acetate buffer, pH 4·5 was used instead of citrate. P-N-Acetyl-o-glucosaminidase activity was assayed as described by Koldovsky and Herbst (1971), except that the final concentration of substrate (p-nitrophenyl-Nacetyl-p-o-glucosaminide) was 2·5 mM, the pH was 5·0 and the reaction was stopped with 1 M Tris-HCI, pH 8·3 (Asp 1971b). IX-L-Fucosidase, EC 3.2.1.51, was assayed with p-nitrophenyl-IX-L-fucoside as substrate (Levvy and McAilan 1961).…”

Section: Methodsmentioning

confidence: 99%

Intestinal Glycosidase Activities in one Adult and two Suckling Echidnas: Absence of a Neutral Lactase (b-D-Galactosidase).

Stewart¹,

Messer²,

Walcott³

et al. 1983

Aust. Jnl. Of Bio. Sci.

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The activities of various glycosidases in homogenates of the small-intestinal mucosa of one adult and two suckling echidnas, Tachyglossus aculeatus, were investigated. The activities of lactase (!i-D-galactosidase), !i-N-acetylglucosaminidase, neuraminidase and ()(-L-fucosidase were higher in the sucklings than in the adult animal. Maltase and isomaltase activities were lower. Sucrase and cellobiase activities were absent or present in trace amounts only. The lactase activity had a pH optimum of 4· 0--4· 5, was predominantly in the soluble fraction following ultracentrifugation and was inhibited by p-chloromercuribenzene sulfonate, suggesting that it was due to a lysosomal acid !i-galactosidase and not a brush-border neutral lactase. The maltase activity of the sucklings also had the characteristics predominantly of a lysomal acid hydrolase. It is proposed that in suckling echidnas, the oligosaccharides (mainly neuraminyllactose and fucosyllactose) of the mother's milk are digested intracellularly by lysosomal enzymes, rather than at the brush border, of the epithelial cells of the small-intestinal mucosa.

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“…p-N-Acetyl-n-glucosaminidase (BC 3.2.1.30) was determined as described by Koldovsky and Herbst (1971), except that the final concentration of substrate (p-nitrophenyl-N-acetyl-p-n-glucosaminide) was 2·5 mM, the pH was 5·0 (unless otherwise stated) and the reaction was stopped after 5-15 min by the addition of 1 M Tris-HCI, pH 8·3 (Asp 1971).…”

Section: Enzyme Assaysmentioning

confidence: 99%

Intestinal Lactase (ß-Galactosidase) and Other Glycosidase Activities in Suckling and Adult Tammar Wallabies (Macropus Eugenii)

Walcott¹,

Messer²

1980

Aust. Jnl. Of Bio. Sci.

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The activities of various glycosidases in homogenates of the small intestinal mucosa of two adult and 18 suckling tammar wallabies (M. eugenii) aged from 6 to 50 weeks were investigated.Lactase (p-D-galactosidase), p-N-acetylglucosaminidase, IX-L-fucosidase and neuraminidase activities were high during the first 34 weeks post partam and then declined to very low levels. Maltase, isomaltase, sucrase and trehalase activities were very low or absent during the first 34 weeks, and then increased.The lactase activity was unusual in being greater in the distal than the middle or proximal thirds of the intestine, and in its low pH optimum (pH 4·6), inhibition by p-chloromercuribenzene sulfonate but not by Tris, and lack of cellobiase activity. These properties are those of a lysosomal acid p-galactosidase rather than of a brush border neutral lactase. The maltase activity had the characteristics of a lysosomal acid IX-glucosidase early in lactation and of a brush border neutral maltase in adult animals.The significance of these findings is discussed in relation to changes in dietary carbohydrates during weaning and to the mode of digestion of milk carbohydrates by the pouch young. IntroductionStudies on various mammalian species have demonstrated marked changes in the activities of small intestinal glycosidases during the period from birth to weaning (Henning and Kretchmer 1973). In rats, for example, the activities of lactase (,B-D-galactosidase) and of the acid (lysosomal) glycosidases are high during suckling and decline at weaning, whereas those of maltase and other neutral a-D-glucosidases are low at birth and then increase (Rubino et al. 1961;Koldovsky 1972).These studies were all done with eutherians (placental mammals) and there are no comparable data for marsupials, even though the milk carbohydrates of marsupials are qualitatively very different from those of eutherians; instead of lactose, they consist mainly of higher oligosaccharides which are exceptionally rich in galactose (Gross and Bolliger 1958;Jenness et al. 1964;Messer and Mossop 1977). Kerry (1969) investigated intestinal disaccharide activities in eight species of marsupials, but only two of the animals studied were pouch young.In this paper we report on the activities of various intestinal glycosidases of 18 suckling tam mar wallabies (Macropus eugenii) aged between 5 and 50 weeks, and of two adult animals.

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N-Acetyl-β-Glucosaminidase in the Small Intestine and its Changes during Postnatal Development of the Rat

Cited by 22 publications

References 19 publications

The transcriptional repressor Blimp1/Prdm1 regulates postnatal reprogramming of intestinal enterocytes

The transcriptional repressor Blimp1/Prdm1 regulates postnatal reprogramming of intestinal enterocytes

Intestinal Glycosidase Activities in one Adult and two Suckling Echidnas: Absence of a Neutral Lactase (b-D-Galactosidase).

Intestinal Lactase (ß-Galactosidase) and Other Glycosidase Activities in Suckling and Adult Tammar Wallabies (Macropus Eugenii)

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