Coexistence of renin and cathepsin B in epithelioid cell secretory granules

Taugner, R.; Bührle, Ch. Ph.; Nobiling, R.; Kirschke, Heidrun

doi:10.1007/bf00495138

Cited by 79 publications

(20 citation statements)

References 31 publications

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“…Tissue processing, anti-renin staining using the PAP meth od, and light microscopical evaluation was done according to Taugner et al [21], The degree o f kidney renin expression was quantified with the immunohistochemical JG index of Taugner et al [21], i.e. the fraction of glomeruli with clearly labelled afferent arterioles from the total number of visible glomeruli in the section.…”

Section: Preparation O F Tissues Fo R Microscopy and Histomorpliologimentioning

confidence: 99%

Magnesium Metabolism: Basic Aspects and Implications of Ciclosporine Toxicity in Rats

Rob

Lebeau

Nobiling

et al. 1996

Nephron

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In rapidly growing male Sprague-Dawley rats with an initial body weight of 100 ± 10 g, we investigated how alimentary magnesium (Mg) supply, Mg metabolism and ciclosporine (Ci)-associated nephrotoxicity are interrelated. Food with 100 ppm Mg (lMg) or 1,000 ppm Mg (stMg) or 10,000 ppm Mg (rMg), Ci 20 mg/kg body weight daily or olive oil were applied for 3 months (n = 10/group). Mg concentrations in various compartments were measured by atomic absorption spectrophotometry. Creatinine clearance (Jaffé), urinary N-acetyl-β-D-glucosaminidase (NAG) activity (fiuorometrically), urinary sodium excretion (flame photometry) and osmolality were measured. Histomorphological examination was done and renal renin expression was studied by monoclonal antibodies. Ci reduced the Mg concentration of the femur under lMg(72.6 ± 9.7 vs. 112.6 ± 14.3 mmol/kg dry substance, p < 0.05) and under stMg (150.6 ± 16.6 vs. 194.1 ± 10.2 mmol/kg dry substance, p < 0.05), thus indicating Ci-related Mg deficiency. This was due to a significant increase in Mg excretion in Ci treatment compared to dietary controls. Under rMg, there was no difference between Ci-treated and control animals. Ci treatment lowered creatinine clearance in lMg (1.42 ± 0.05 vs. 3.02 ± 0.58 ml/min) and in stMg (1.04 ± 0.45 vs. 2.18 ± 0.51 ml/min), NAG/creatinine and urinary sodium excretion were negatively affected by Ci under lMg and stMg. Histomorphology showed macrocalcifications due to Mg deficiency and Ci-specifïc findings, which were markedly enhanced in lMg and stMg. Animals with plentiful Mg supply had no functional alterations due to Ci and no or weakly expressed histomorphological lesions. Renin-positive stained cells were higher in Ci-treated animals. This seems to be functionally relevant under lMg and stMg, since it was associated with sodium retention and elevated relative heart weight, indicating hypertension. Alimentary or drug-induced Mg deficiency plays a relevant role in the pathophysiology of chronic Ci nephrotoxicity. Our data suggest that Mg supplementation is helpful to reduce Ci toxicity, even if there is ‘normal’ alimentary Mg intake.

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Section: Preparation O F Tissues Fo R Microscopy and Histomorpliologimentioning

confidence: 99%

Magnesium Metabolism: Basic Aspects and Implications of Ciclosporine Toxicity in Rats

Rob

Lebeau

Nobiling

et al. 1996

Nephron

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“…White (London Resin, U.K.). Procedures used were modified from Taugner et al (1985) and Graber & Kreutzberg (1985) in order to decrease polymerization damage. Briefly, dehydrated pellets were treated with mixtures of L.R.…”

Section: Cell Lines and Virus Growth Spodoptera Frugiperdamentioning

confidence: 99%

A Cytopathological Investigation of Autographa californica Nuclear Polyhedrosis Virus p10 Gene Function Using Insertion/Deletion Mutants

Williams

Rohel²,

Kuzio

et al. 1989

Journal of General Virology

143

100

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SUMMARYThe role of the Autographa cali]brniea nuclear polyhedrosis virus pl0 gene in viral cytopathology and morphogenesis was examined using classes of pl 0 deletion mutants with and without lacZ (fl-galactosidase) gene fusion. Mutant-infected cells did not form the fibrillar cytoplasmic and nuclear structures normally observed late in infection with wild-type (wt) virus, and the cells failed to lyse even at 2 weeks post-infection. Based on wt and mutant cytopathology, we suggest lysis may be facilitated by stepwise exhaustion of the host nuclear membrane, and may require a function resident in the carboxy region of p 10; this portion of the molecule is also essential for formation of the p 10-rich fibrillar bodies. Additional changes in cytopathology were correlated with the level of p 10/LacZ fusion protein expression. The insertional mutant designated Ac229, which encodes 51 N-terminal amino acids of pl0 fused to LacZ, caused intranuclear accumulation of granular structures at sites corresponding to the fibrillar bodies of wt viral infections. Occlusion body membranes, which associate with the fibrillar bodies in wt infections, were also formed in mutant virus-infected cells. However, membranes did not associate with occlusion bodies in Ac229 infections, and were aberrantly attached to occlusion bodies in cells infected with mutants having simple p 10 deletions (represented by Ac231). Loss of the outer membrane increased sensitivity of the occlusion bodies to disruption by physical stress; a partially attached membrane afforded some protection from disruption.

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“…Cysteine exoproteinases include cathepsin C (dipeptidyl peptidase I), which is also found in lysosomes. In general, cysteine proteinases are involved in the intracellular catabolism of peptides and proteins (Barrett and Kirschke, 1981), processing of proenzymes and prohormones (Taugner^a/., 1985;Marks et al, 1986), breakdown of collagen (Etherington, 1980), and bone resorption (Delaisse etal., 1984). They may play a role in modulating the penetration and destruction of tissues by malignant cells during tumor invasion and metastasis (Sloane and Honn, 1984) and by microorganisms during infection .…”

Section: Introduction a Cysteine Proteinasesmentioning

confidence: 99%

Cystatins — Inhibitors of Cysteine Proteinases

Bobek

Levine

1992

Critical Reviews in Oral Biology & Medicine

146

100

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ABSTRACT:The cystatin superfamily of proteins, derived from a common ancestor, is comprised of a diverse group of potent cysteine proteinase inhibitors and antibacterial/viral agents grouped into several families. This review concentrates on family 2 cystatins, namely, the human salivary cystatins and cystatin C. Emphasis is given to their physicochemical and functional properties at both the protein and the molecular level. The role of cystatins in disease processes, including those in the oral cavity, is also discussed. Finally, future directions for cystatin research in oral biology are presented.

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Coexistence of renin and cathepsin B in epithelioid cell secretory granules

Cited by 79 publications

References 31 publications

Magnesium Metabolism: Basic Aspects and Implications of Ciclosporine Toxicity in Rats

Magnesium Metabolism: Basic Aspects and Implications of Ciclosporine Toxicity in Rats

A Cytopathological Investigation of Autographa californica Nuclear Polyhedrosis Virus p10 Gene Function Using Insertion/Deletion Mutants

Cystatins — Inhibitors of Cysteine Proteinases

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