Dietary regulation of rat intestinal angiotensin-converting enzyme and dipeptidyl peptidase IV

Suzuki, Yasuhiro; Erickson, Roger H.; Sedlmayer, A.; Chang, Sae-Kyung; Ikehara, Yukio; Kim, Y. S.

doi:10.1152/ajpgi.1993.264.6.g1153

Cited by 20 publications

(21 citation statements)

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“…Alkaline phosphatase activity was also lower with lactalbumin, egg albumin, zein, gelatin or wheat gluten than with the phosphoproteins casein and vitellin [36]. Feeding a high-proline-rich diet resulted in an increased expression of intestinal brush border dipeptidyl peptidase IV [32]. Soya protein contains about 40 % less proline than milk protein [8].…”

Section: Histomorphometrymentioning

confidence: 94%

Morphology and enzyme activities of the small intestine are modulated by dietary protein source in the preruminant calf

Montagné¹,

Toullec²,

Savidge³

et al. 1999

Reprod. Nutr. Dev.

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-A study was undertaken to assess the impact of the protein nature and soya antigenicity on the morphology and some enzyme activities of the jejunum in preruminant calves. Twenty Holstein calves fitted with a duodenal cannula were fed a liquid diet based on skimmed milk powder (SMP) for 2 weeks. They were then switched onto diets containing a mixture of SMP and either antigenic heated soybean flour (HSF; n = 12) or hypo-antigenic soya protein concentrate (SPC; n = 8) for 8 weeks, after which they were reverted back to the SMP diet for 2 weeks. The diets contained similar amounts of digestible nitrogen and energy, and were fed at a rate of 55 g DM/kg o . 75/d. Proximal jejunal biopsies were collected just before (week 0), during (weeks 2 and 8) and after (week 10) feeding of the soya-based diets, and were used for morphology measurements and the determination of total alkaline phosphatase, lactase, amino-peptidases A and N, and dipeptidyl peptidase IV activities. Feed intake and growth were similar between the HSF and SPC groups during the experimental period. The effects of antigenicity and the antigenicity x time interaction were never significant (P > 0.05). Villus height decreased (P < 0.01) between weeks 0 and 2, and increased (P < 0.05) between weeks 8 and 10. Villus width increased between weeks 2 and 8 (P < 0.001 Crypt depth also increased between weeks 0 and 2 (P < 0.001 Specific activities of alkaline phosphatase (P < 0.01) and amino-peptidase N (P < 0.05) decreased between weeks 0 and 2. Conversely, those of alkaline phosphatase (P < 0.0001 ), lactase (P < 0.01) and dipeptidyl-peptidase IV (P < 0.0001) increased between weeks 8 and 10. Specific activities for lactase and amino-peptidase N decreased (P < 0.01) between weeks 2 and 8.

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Section: Histomorphometrymentioning

confidence: 94%

Morphology and enzyme activities of the small intestine are modulated by dietary protein source in the preruminant calf

Montagné¹,

Toullec²,

Savidge³

et al. 1999

Reprod. Nutr. Dev.

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“…Using gliadin, a proline-rich protein, in feeding rats that were normal and genetically deficient in dipeptidyl-peptidase IV, the control groups maintained their weights, whereas the deficient group experienced a significant weight loss [98]. The amount of the enzyme in rat small intestine can be increased by feeding a high-proline-containing diet [99]. Dipeptidyl-peptidase IV also extinguishes signals by cleaving exterior peptide mediators, functions as receptor and participates in signal transduction or in adhesion.…”

Section: Biological Relevancementioning

confidence: 99%

The prolyl oligopeptidase family

Polgár¹

2002

CMLS, Cell. Mol. Life Sci.

289

227

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A group of serine peptidases, the prolyl oligopeptidase family, cannot hydrolyze peptides containing more than about 30 residues. This group is unrelated to the classical trypsin and subtilisin families, and includes dipeptidyl peptidase IV, acylaminoacyl peptidase and oligopeptidase B, in addition to the prototype prolyl oligopeptidase. The recent crystal structure determination of prolyl oligopeptidase (80 kDa) has shown that the enzyme contains a peptidase domain with an alpha/beta hydrolase fold, and its catalytic triad is covered by the central tunnel of an unusual seven-bladed beta-propeller. This domain operates as a gating filter, excluding large, structured peptides from the active site. The binding mode of substrates and the catalytic mechanism differ from that of the classical serine peptidases in several features. The members of the family are important targets of drug design. Prolyl oligopeptidase is involved in amnesia, depression and blood pressure control, dipeptidyl peptidase IV in type 2 diabetes and oligopeptidase B in trypanosomiasis.

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“…Thus the dipeptidyl peptidase IV promoter possesses the ability to initiate transcription in a tissue-specific fashion in spite of having the sequence characteristics of a housekeeping gene promoter. [15]. Thus intestinal DPP IV exhibits both inducibility and spatial regulation.…”

Section: Introductionmentioning

confidence: 99%

Human dipeptidyl peptidase IV gene promoter: tissue-specific regulation from a TATA-less GC-rich sequence characteristic of a housekeeping gene promoter

Böhm

Gum

Erickson

et al. 1995

Biochemical Journal

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The dipeptidyl peptidase IV gene encodes a plasma-membrane exopeptidase that is highly expressed in small intestine, lung and kidney. In order to better understand the mechanisms responsible for this tissue-specific expression we cloned, sequenced and functionally characterized the 5′-flanking region of the human dipeptidyl peptidase IV gene. The first 500 bases of the 5′-flanking sequence constituted an unmethylated CpG island, contained several Sp1-binding sites and lacked a consensus TATA box, all characteristics of gene promoters lacking tissue-specific expression. RNase-protection analysis using both small intestinal and Caco2 cell RNA indicated that the dipeptidyl peptidase IV transcript was initiated from no fewer than six major and 12 minor start sites. The 5′-flanking sequence also exhibited functional promoter activity in transient transfection experiments. Here, various lengths of the sequence were cloned upstream of a luciferase gene and introduced into cultured cells using lipofectin. A region located between bases -150 and -109 relative to the start of translation was found to be important for high-level promoter activity in both Caco2 and HepG2 cells. Moreover, Caco2 cells and HepG2 cells, which express high levels of dipeptidyl peptidase IV activity, exhibited much higher normalized luciferase activity after transfection than did 3T3, Jurkat or COS-7 cells, which have low enzyme levels. Sodium butyrate was found to increase both enzyme activity and normalized luciferase in HepG2 cells. Thus the dipeptidyl peptidase IV promoter possesses the ability to initiate transcription in a tissue-specific fashion in spite of having the sequence characteristics of a housekeeping gene promoter.

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Dietary regulation of rat intestinal angiotensin-converting enzyme and dipeptidyl peptidase IV

Cited by 20 publications

References 0 publications

Morphology and enzyme activities of the small intestine are modulated by dietary protein source in the preruminant calf

Morphology and enzyme activities of the small intestine are modulated by dietary protein source in the preruminant calf

The prolyl oligopeptidase family

Human dipeptidyl peptidase IV gene promoter: tissue-specific regulation from a TATA-less GC-rich sequence characteristic of a housekeeping gene promoter

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