Immunohistochemical localization of intestinal phospholipase A2 in rat paneth cells

Senegas-Balas, F.; Balas, D; Verger, Robert; De, Alain; Figarella, Catherine; Ferrato, Francine; Lechêne, Patrick; Bertrand, C.; Ribet, A

doi:10.1007/bf00489538

Cited by 55 publications

(26 citation statements)

References 21 publications

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“…Earlier, the distribution of PLA2 was studied in the gastrointestinal tract of humans (Kiyohara et al 1992;Nevalainen et al 1995) and rats (Senegas-Balas et al 1984). The results have been divergent, probably due to the use of different antibodies.…”

Section: Discussionmentioning

confidence: 99%

Distribution of Group II Phospholipase A2 Protein and mRNA in Rat Tissues

Nyman

Ojala

Laine

et al. 2000

J Histochem Cytochem.

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S U M M A R Y Group II phospholipase A2 (PLA2) is an acute-phase protein and an important component of the host defense against bacteria. In this study we investigated the distribution of PLA2 protein by immunohistochemistry and the distribution of mRNA of PLA2 by Northern blotting and in situ hybridization in rat tissues. PLA2 protein was localized in the Paneth cells of the intestinal mucosa, chondrocytes and the matrix of cartilage, and megakaryocytes in the spleen. By Northern blotting, mRNA of PLA2 was found in the gastrointestinal tract, lung, heart, and spleen. By in situ hybridization, PLA2 mRNA was localized in the Paneth cells of the small intestinal mucosa but in no other cell types. Our results show specific distribution of PLA2 in a limited number of cell types in rat tissues. The reagents developed in this study (the anti-rat PLA2 antibody and probes for Northern blotting and in situ hybridization of mRNA of rat PLA2) will provide useful tools for future studies concerning the role of PLA2 in various experimental disease models.

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Section: Discussionmentioning

confidence: 99%

Distribution of Group II Phospholipase A2 Protein and mRNA in Rat Tissues

Nyman

Ojala

Laine

et al. 2000

J Histochem Cytochem.

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“…Type II PLA2, which is present in the granules of rat and human intestinal Paneth cells (13,14), hydrolyses phosphatidylglycerol, a major bacterial phospholipid, several hundred times more rapidly than phosphatidylcholine, the principal phospholipid of egg yolk (20)(21)(22). In a recent report characterizing human ileal PLA2, Minami et al stated that the physiological role of iPLA2 was unknown, but noted its production by Paneth cells which contained other molecules (lysozyme, IgA, and defensin) that might control the local bacterial milieu (22).…”

Section: Discussionmentioning

confidence: 99%

“…1 b in reference 6). We now describe the purification of one of these molecules, and its identification as a Type 2 phospholipase A2, a known Paneth cell constituent in rats (13) and humans (14).…”

Section: Introductionmentioning

confidence: 99%

Bactericidal properties of murine intestinal phospholipase A2.

Harwig¹,

Tan²,

Qu³

et al. 1995

J. Clin. Invest.

237

149

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We purified a molecule from the murine small intestine that killed both Escherichia coli and Listeria monocytogenes, and identified it as intestinal phospholipase A2 (iPLA2) by NH2-terminal sequencing and enzymatic measurements. The ability of iPLA2 to kill. L monocytogenes was greatly enhanced by 5 mM calcium, inhibited by EGTA and abolished after reduction and alkylation, suggesting that enzymatic activity was required for iPLA2-mediated bactericidal activity. A mouse-avirulent phoP mutant, S. typhimunium 7953S, was 3.5-fold more susceptible to iPLA2 than its isogenic virulent parent, S. typhimurium 14028S (estimated minimal bactericidal concentrations 12.7±0.5 jig/ml vs. 43.9±4.5 jig/ml,

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“…However, it has been demonstrated that Paneth cells produce and secrete antibacterial agents (lysozyme, cryptidin, and immunoglobulin A), hydrolases, lipases, and growth factors and modulators (Desai et al 1991;Quellette and Lualdi 1990;Saito et al 1988;Lechene de la Porte et al 1986;Poulsen et al 1986;Senegas-Balas et al 1984;Erlandsen et al 1974 Erlandsen et al , 1976Erlandsen and Parsons, 1973). The granules also contain a zinc-binding protein (Sawada et al 1994).…”

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confidence: 99%

N- andO-linked Oligosaccharides in the Secretory Granules of Rat Paneth Cells: An Ultrastructural Cytochemical Study

Leis

Madrid

Ballesta

et al. 1997

J Histochem Cytochem.

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P aneth cells , originally described by Schwalbe (1872) and later by Paneth (1888), are normally located at the base of the crypts of Lieberkühn in the small intestine of many mammals, except carnivores. They are easily recognized by a large number of eosinophilic granules located in the supranuclear portion of the cell. Electron microscopic studies (Satoh et al. 1990;Staley and Trier 1965;Hally 1958) have revealed the structural complexity of Paneth granules. These granules are characterized in several species, including rat and human, by an electron-lucent peripheral halo of variable thickness surrounding a large electron-dense core (Satoh et al. 1990).The functions of the Paneth cells have not been clearly established. However, it has been demonstrated that Paneth cells produce and secrete antibacterial agents (lysozyme, cryptidin, and immunoglobulin A), hydrolases, lipases, and growth factors and modulators (Desai et al. 1991;Quellette and Lualdi 1990;Saito et al. 1988;Lechene de la Porte et al. 1986;Poulsen et al. 1986;Senegas-Balas et al. 1984;Erlandsen et al. 1974 Erlandsen et al. , 1976Erlandsen and Parsons, 1973). The granules also contain a zinc-binding protein (Sawada et al. 1994). It has been suggested that goblet and Paneth cells share a common pathway of development (Kedinger et al. 1988;Lopez-Lewellyn and Erlandsen 1980;Lopez-Lewellyn 1979).Lectins are proteins or glycoproteins that bind specifically to carbohydrate groups (Goldstein and Hayes, 1978). They have been widely used in combination with enzymes for in situ characterization of the

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Immunohistochemical localization of intestinal phospholipase A2 in rat paneth cells

Cited by 55 publications

References 21 publications

Distribution of Group II Phospholipase A2 Protein and mRNA in Rat Tissues

Distribution of Group II Phospholipase A2 Protein and mRNA in Rat Tissues

Bactericidal properties of murine intestinal phospholipase A2.

N- andO-linked Oligosaccharides in the Secretory Granules of Rat Paneth Cells: An Ultrastructural Cytochemical Study

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