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PubMed1984

Ultrastructural localization of nicotinamide adenine dinucleotide phosphatase (NADPase) activity within columnar, goblet, and Paneth cells of rat small intestine.

The distribution of nicotinamide adenine dinucleotide phosphatase (NADPase) activity was examined in epithelial cells of rat small intestine. Segments of ileum were fixed with glutaraldehyde and tissue chopper sections were incubated for up to 4 hr at pH 5.0 in cytochemical media prepared with NADP as substrate. NADPase activity was found primarily within the Golgi saccules of columnar, goblet, and Paneth cells. Columnar and goblet cells showed most of the NADPase activity within the saccules which were intermediate between the cis and trans faces of the Golgi stack. Paneth cells, however, showed the heaviest staining within saccules between the intermediate and innermost saccule at the trans aspect of the Golgi stack. Both columnar cells and Paneth cells also contained spotty, and sometimes heavy, deposits of reaction product within an occasional focal area of the GERL system and within an occasional lysosome. Control experiments indicated that the Golgi-associated NADPase activity was enhanced if cells were pretreated for about 12 hr with EGTA prior to incubation. No similar enhancement was apparent if the tissues were pretreated with DMSO. Furthermore, NADPase activity within the Golgi saccules could be inhibited completely by incubating intestinal epithelial cells with NADP in the presence of sodium fluoride or L(+)-tartrate.

Animals↗
PubMed2006

PPARbeta/delta regulates paneth cell differentiation via controlling the hedgehog signaling pathway.

BACKGROUND & AIMS: All 4 differentiated epithelial cell types found in the intestinal epithelium derive from the intestinal epithelial stem cells present in the crypt unit, in a process whose molecular clues are intensely scrutinized. Peroxisome proliferator-activated receptor beta (PPARbeta) is a nuclear hormone receptor activated by fatty acids and is highly expressed in the digestive tract. However, its function in intestinal epithelium homeostasis is understood poorly. METHODS: To assess the role of PPARbeta in the small intestinal epithelium, we combined various cellular and molecular approaches in wild-type and PPARbeta-mutant mice. RESULTS: We show that the expression of PPARbeta is particularly remarkable at the bottom of the crypt of the small intestine where Paneth cells reside. These cells, which have an important role in the innate immunity, are strikingly affected in PPARbeta-null mice. We then show that Indian hedgehog (Ihh) is a signal sent by mature Paneth cells to their precursors, negatively regulating their differentiation. Importantly, PPARbeta acts on Paneth cell homeostasis by down-regulating the expression of Ihh, an effect that can be mimicked by cyclopamine, a known inhibitor of the hedgehog signaling pathway. CONCLUSIONS: We unraveled the Ihh-dependent regulatory loop that controls mature Paneth cell homeostasis and its modulation by PPARbeta. PPARbeta currently is being assessed as a drug target for metabolic diseases; these results reveal some important clues with respect to the signals controlling epithelial cell fate in the small intestine.

Animals↗
PubMed1993

Cellular localization of tumor necrosis factor (TNF)-alpha transcripts in normal bowel and in necrotizing enterocolitis. TNF gene expression by Paneth cells, intestinal eosinophils, and macrophages.

Tumor necrosis factor-alpha (TNF) has been shown to induce intestinal necrosis in animals. Moreover, plasma TNF levels are elevated in patients with necrotizing enterocolitis. Thus, it is possible that TNF plays a role in the pathogenesis of NEC. In the present study we used in situ hybridization (with human TNF riboprobes) to localize TNF transcripts in the intestinal tissues from normal biopsies and NEC patients. We found that in normal intestine a small amount of TNF mRNA was present only in Paneth cells. In contrast, in the acute stage of NEC, a high amount of TNF transcripts was detected in Paneth cells as well as in infiltrating eosinophils. In one case that showed infiltrating macrophages, TNF mRNA was also detected in these cells. Resident macrophages in the lamina propria and other inflammatory cells were negative for TNF transcripts. Our results suggest that: 1) Paneth cells are the major source of TNF transcripts in normal intestine, and 2) there is a marked increase in TNF mRNA formation in Paneth cells, as well as in infiltrating eosinophils and macrophages in patients with NEC. TNF-containing cells may play an important role in the pathophysiology of NEC.

Colon↗
PubMed2005

Events at the host-microbial interface of the gastrointestinal tract. V. Paneth cell alpha-defensins in intestinal host defense.

Host defense of the small intestine is mediated, in part, by antimicrobial peptides, including alpha-defensins. In the small intestine, Paneth cells, specialized secretory epithelial cells located at the base of the crypt invaginations lining the intestinal wall, produce alpha-defensins. The alpha-defensins are cysteine-rich cationic peptides with antibiotic activity against a wide range of bacteria and other microbes. Studies of transgenic and knockout mice have supported a pivotal role of Paneth cell alpha-defensins in protection from bacterial pathogens. New data suggest that deficient expression of Paneth cell alpha-defensins may contribute to the pathophysiology of Crohn's disease, a chronic inflammatory bowel disease.

Animals↗
PubMed1968

Neoplastic Paneth cells.

A villous papilloma of the colon showing neoplastic proliferation of Paneth cells is described. The literature is reviewed and only three other tumours are accepted as showing neoplastic proliferation of Paneth cells.

Humans↗
PubMed1994

A Paneth cell analogue in Xenopus small intestine expresses antimicrobial peptide genes: conservation of an intestinal host-defense system.

Antimicrobial peptides are a widespread component of host defense. We characterized the tissue distribution and cellular localization of expression of the magainin family of antimicrobial peptide genes in Xenopus laevis. Two genes from this family, magainin and PGLa, are expressed at high levels in the skin and throughout the gastrointestinal tract. Magainin and PGLa mRNAs are synthesized in the granular multinucleated cell (GMC) of the gastric mucosa, a cell shown previously to contain magainin and PGLa peptides by immunohistochemical methods. In addition, we have localized magainin and PGLa mRNAs to distinct cells of Xenopus small intestine. Further characterization of this large, granule-filled cell by electron microscopy demonstrates features in common with the Paneth cell of mammalian small intestine, previously identified as a site of expression of antimicrobial peptide genes of the defensin family in mouse and human. Our identification of granule-laden, eosinophilic intestinal cells in Xenopus as a site of magainin and PGLa antimicrobial peptide gene expression suggests that these cells are functional analogues of mammalian Paneth cells and further supports a conserved role of antimicrobial peptides in host defense of the vertebrate small intestine.

Animals↗
PubMed1992

[Ultrastructural and morphometric analysis of the Paneth cell reaction to administration of cholera toxin].

Experiments were made on 40 immature guinea--pigs which were divided into two groups. 20 animals received intraduodenal injections of cholera toxin and 20 others were injected normal saline (groups I and II, respectively). Group I animals exhibited a rapid fall in one--cell secretion of XS recorded on hour 6-12 after the injection of cholera toxin. Inhibition of functional activity was associated with defected synthesis of granules in the cells of Paneth.

Age Factors↗
PubMed2006

Matrix metalloproteinase-7 activation of mouse paneth cell pro-alpha-defensins: SER43 down arrow ILE44 proteolysis enables membrane-disruptive activity.

Small intestinal Paneth cells secrete alpha-defensin microbicidal peptides as mediators of innate enteric immunity. In mice, production of mature Paneth cell alpha-defensins, termed cryptdins (Crps), requires proteolytic activation of inactive precursors (pro-Crps) by the convertase matrix metalloproteinase-7. Proteolysis of mouse (pro-Crp4)(20-92) produces the specific cleavage intermediates pro-Crp4(44-92), pro-Crp4(54-92), and pro-Crp4(59-92). To identify which cleavage event enables bactericidal activity, recombinant pro-Crp4-processing intermediates were purified to homogeneity and assayed for bactericidal peptide activity. The in vitro bactericidal activities of pro-Crp4-processing intermediates were very similar to fully processed Crp4, contrasting the lack of bactericidal and membrane-disruptive activity shown by pro-Crp4(20-92). Thus, cleavage of pro-Crp4(20-92) at Ser(43) downward arrowIle(44) is sufficient to activate bactericidal activity, and amino acids in the pro-Crp4(20-43) of the proregion maintain the precursor in an inactive state. Because cationic Arg residues are determinants of Crp4 bactericidal peptide activity, we hypothesized that Asp and Glu residues in pro-Crp4(20-43) neutralize Crp4 Arg side chains in pro-Crp4(20-92). Therefore, a pro-Crp4(20-92) variant with Gly substitutions at all pro-Crp4(20-43) Asp and Glu positions ((DE/G)-pro-Crp4) was prepared, and it was bactericidal and lysed phospholipid vesicles under conditions where native pro-Crp4(20-92) lacks activity. These findings show that MMP-7 proteolysis of pro-Crp4(20-92) at Ser(43) downward arrowIle(44) converts inactive precursors to bactericidal forms by removal of covalently associated, inhibitory acidic amino acids from proximity with the Crp4 component of the molecule.

Amino Acid Sequence↗
PubMed1993

A hydrophilic resin-embedding method for light and electron microscopic detection of tissue anionic sites with cationic colloidal iron: as applied to mouse Paneth cells.

A cationic colloidal iron method was introduced for electron microscopic detection of anionic sites in hydrophilic resin-embedded specimens, and the method was applied to Paneth cells of the mouse jejunum. Mouse jejunal blocks were embedded in hydrophilic acrylic resin (LR White), cut into ultrathin sections, stained with the diluted cationic colloidal iron, and exposed to osmium vapor. The jejunal tissues, including the Paneth cells, embedded in hydrophilic resin were reactive to the fine cationic colloidal iron. At pH value 1.5, fine electron dense colloidal iron deposited along the rims of the secretory granules and the Golgi apparatus of the Paneth cell. Colloidal particles distributed on the osmiophilic reticular structures in the rim and in dot-like fashion lined the border between the granular core and rim. At pH value 4.0, ribosomes reacted to cationic colloidal iron particles in addition to the granular rims and Golgi apparatus. At pH 7.0, even the cores of the secretory granules were stained. Semi-thin sections prepared from the LR White-embedded specimens and stained at pH 1.5 with the diluted (1:3 in volume) cationic colloidal iron showed sufficient Prussian blue reaction for light microscopy in the rims of Paneth granules and mucus of goblet cells. This method is therefore useful for correlative light and electron microscopic detection of tissue anionic sites, including sulfate, carboxyl and phosphate groups, at various pH values.

Animals↗
PubMed1994

Mouse Paneth cell defensins: primary structures and antibacterial activities of numerous cryptdin isoforms.

Cryptdins are antimicrobial peptides of the defensin family that are produced by intestinal Paneth cells. mRNAs encoding 17 cryptdin isoforms have been characterized from a cDNA library generated from a single jejunal crypt. Six cryptdin cDNAs correspond to known peptides, and the remainder predict 11 novel Paneth cell defensins. Most cryptdin cDNAs have > or = 93% nucleotide sequence identity overall, except for cryptdin 4 and 5 cDNAs, whose respective mature peptide-encoding regions are only 74 and 78% identical to that of cryptdin 1. Cryptdin cDNAs differ at a small number of nucleotide positions: frequent substitutions were found in codons 38 and 52 of the propiece and in codons 68, 73, 76, 87, and 89 of the deduced peptides; cDNA clones with changes in codons 74, 83, and 88 were found, but there were fewer of these. The antimicrobial activities of cryptdins 1 to 6 were tested against Escherichia coli ML35 in two assays. In an agar diffusion assay, the potencies of cryptdins 1 to 3, 5, and 6 were approximately equivalent to that of rabbit neutrophil defensin NP-1 but cryptdin 4 was 30 times more active than NP-1. In a bactericidal assay system, cryptdins 1 and 3 to 6 were equally active at 10 micrograms/ml but cryptdin 2 and rabbit NP-1 were not active at this concentration. Since cryptdins 2 and 3 differ only at residue 10 (Thr and Lys, respectively), this amino acid appears to function in bactericidal interaction with E. coli. The demonstration that Paneth cells express a diverse population of microbicidal defensins further implicates cryptdins in restricting colonization or invasion of small intestinal epithelium by bacteria.

Amino Acid Sequence↗
PubMed1993

Enhancing factor, a Paneth cell specific protein from mouse small intestines: predicted amino acid sequence from RT-PCR amplified cDNA and its expression.

Enhancing factor (EF), a Paneth cell specific growth factor modulator, has been identified in our laboratory from mouse small intestines. In this paper we describe generation of an EF specific cDNA by RT-PCR and its sequence. The predicted amino acid sequence was found to be similar to, and hence confirms, the partial amino acid sequence obtained earlier by protein sequencing. In Northern blot analysis, a 1 kb transcript was observed in intestinal RNA alone. In situ hybridization indicated that the EF gene is expressed exclusively in the Paneth cells. The present study indicates that EF is an isoform of PLA2 type II, with a unique tissue distribution, found predominantly in the Paneth cells of the small intestines. Further, based on the properties of EF, we propose that isoforms of PLA2, belonging to type II, may be involved in regulation of cell proliferation via EGF binding.

Amino Acid Sequence↗
PubMed1988

Immunohistochemical observations of lysozyme in the Paneth cells of specific-pathogen-free and germ-free mice.

The localization of lysozyme, which may function as an antibacterial agent, was immunohistochemically studied on the mouse Paneth cell secretory granules showing bipartite substructures (central core and peripheral halo). The lysozyme immunoreactivity was observed in the core, but not in the halo. Even in germ-free mice, Paneth cells have many secretory granules and their cores show lysozyme immunoreactivity. It seems likely that mice Paneth cells possess the ability to produce secretory granules containing lysozyme in disregard of the intestinal bacterial milieu.

Animals↗
PubMedDate not supplied

[Comparative histochemical study of insulinocytes and Paneth cells].

Histochemical reactions of insulocytes and Paneth cells of rabbits and rats were investigated following the injection of the agents selectively affecting the above cells, as well as of glucose, a specific stimulant of insulin secretion. The data obtained suggest a functional relation between the pancreatic islet cells and the intestinal cryptic basal regions, which is mediated by the mechanisms, involved in regulation of the glycemic level.

Animals↗
PubMed2004

The role of Paneth cells and their antimicrobial peptides in innate host defense.

The intestinal epithelium is the largest surface area that is exposed to various pathogens in the environment, however, in contrast to the colon the number of bacteria that colonize the small intestine is extremely low. Paneth cells, one of four major epithelial cell lineages in the small intestine, reside at the base of the crypts and have apically oriented secretory granules. These granules contain high levels of antimicrobial peptides that belong to the alpha-defensin family. Paneth cells secrete these microbicidal granules that contain alpha-defensins when exposed ex vivo to bacteria or their antigens, and recent evidence reveals that antimicrobial peptides, particularly alpha-defensins, that are present in Paneth cells contribute to intestinal innate host defense.

Animals↗
PubMed1991

[The effects of ciprofloxacin on intestinal flora and Paneth cells].

The effects of ciprofloxacin were investigated on colonic microbial flora and Paneth cells in eight healthy albino rabbits following a 10 mg intravenous dose. Two rabbits were used as control group. Aerobic fecal cultures were negative on rabbits of experiment. Vacuolisation and reduction of eosinophilic fields were seen in Paneth cells by light microscopic examination.

Animals↗
PubMed2004

Paneth cell alpha-defensins from rhesus macaque small intestine.

Antimicrobial peptides are secreted by small intestinal Paneth cells as components of innate immunity. To investigate the role of alpha-defensins in enteric host defenses in nonhuman primates, alpha-defensin cDNAs were isolated, alpha-defensin peptides were purified from rhesus macaque small bowel, and the bactericidal activities of the peptides were measured. Six rhesus enteric alpha-defensin (RED) cDNAs, RED-1 to RED-6, were identified in a jejunum cDNA library; the deduced RED peptides exhibited extensive diversity relative to the primary structures of rhesus myeloid alpha-defensins. RED-4 was purified from monkey jejunum, and N-terminal peptide sequencing of putative RED-4 peptides identified two N termini, RTCYCRTGR. and TCYCRTGRC.; these corresponded to alternative N termini for the RED-4 molecules, as deduced from their molecular masses and RED cDNAs. In situ hybridization experiments localized RED mRNAs exclusively to small intestinal Paneth cells. Recombinant RED-1 to RED-4 were purified to homogeneity and shown to be microbicidal in the low micromolar range (</=10 micro g/ml) against gram-positive and gram-negative bacteria, with individual peptides exhibiting variable target cell specificities. Thus, compared to myeloid alpha-defensins from rhesus macaques, enteric alpha-defensin peptides are highly variable in both primary structure and activity. These studies should facilitate further analyses of the role of alpha-defensins in primate enteric immunity.

Amino Acid Sequence↗
PubMed1989

Neoplastic Paneth cells in the stomach. Report of two cases and review of the literature.

We report two cases of gastric lesions characterized on endoscopic biopsy specimens by the extensive proliferation of Paneth cells with neoplastic characteristics. One patient with long-standing pernicious anemia developed a large polypoid carcinoma of the stomach in which the majority of malignant glands were lined by Paneth cells showing varying degrees of differentiation. The second patient developed an irregular white patch just proximal to an old gastrojejunostomy anastomosis, which revealed numerous clusters of adenomatous tubules filled with cytoplasmic Paneth granules. The "Paneth" nature of the granules was supported by the morphological, histochemical, and ultrastructural findings. These cases are unusual since neoplastic Paneth cells occur only rarely in frank adenocarcinomas or in premalignant conditions of the stomach.

Adenocarcinoma↗
PubMed1981

Neoplastic Paneth cells in adenocarcinoma of the urinary bladder: a first case report.

A case of a highly differentiated, primary, nonurachal adenocarcinoma of intestinal type, originating from the urinary bladder mucosa, is reported. The tumor contained Paneth cells as an integrated part, and their identity on the light microscopic level was confirmed by histochemical stains including immunohistochemical stain for muramidase. A gradual change from Paneth cell types to mucous cells was seen. Argentaffin cells and goblet cells appeared in some parts of the tumor but no detectable transitional forms were found. Only a few carcinomas containing malignant Paneth cells have been recorded, and this case is believed to be the first observed in an extraintestinal site.

Adenocarcinoma↗