Simultaneous measurements of calcium oxalate crystal nucleation and aggregation: impact of various modifiers

Hess, Bernhard; Meinhardt, Udo; Zipperle, Ljerka; Giovanoli, R.; Jaeger, P

doi:10.1007/bf00393304

Cited by 70 publications

(61 citation statements)

References 18 publications

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“…Sialic acid residues may be important for this action of THP because neuraminidase treatment abolished the effect (23). In the present study, we used absorbance at 630 nm that represents an exact measure of particle concentration per unit volume (24), and a Coulter Counter to assess nucleation and aggregation of CaOx crystals. The latter tech- Table 2, UM produced fewer particles than THP in all groups and the total volume of crystals produced by UM was larger than that produced by THP.…”

Section: Discussionmentioning

confidence: 99%

Role of Tamm-Horsfall protein and uromodulin in calcium oxalate crystallization

Carvalho

Mulinari

Nakagawa

2002

Braz J Med Biol Res

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One of the defenses against nephrolithiasis is provided by macromolecules that modulate the nucleation, growth, aggregation and retention of crystals in the kidneys. The aim of the present study was to determine the behavior of two of these proteins, Tamm-Horsfall and uromodulin, in calcium oxalate crystallization in vitro. We studied a group of 10 male stone formers who had formed at least one kidney stone composed of calcium oxalate. They were classified as having idiopathic nephrolithiasis and had no well-known metabolic risk factors involved in kidney stone pathogenesis. Ten normal men were used as controls, as was a group consisting of five normal women and another consisting of five pregnant women. Crystallization was induced by a fixed supersaturation of calcium oxalate and measured with a Coulter Counter. All findings were confirmed by light and scanning electron microscopy. The number of particulate material deposited from patients with Tamm-Horsfall protein was higher than that of the controls (P<0.001). However, Tamm-Horsfall protein decreased the particle diameter of the stone formers when analyzed by the mode of the volume distribution curve (P<0.002) (5.64 ± 0.55 µm compared to 11.41 ± 0.48 µm of uromodulin; 15.94 ± 3.93 µm and 12.45 ± 0.97 µm of normal men Tamm-Horsfall protein and uromodulin, respectively; 8.17 ± 1.57 µm and 9.82 ± 0.95 µm of normal women Tamm-Horsfall protein and uromodulin, respectively; 12.17 ± 1.41 µm and 12.99 ± 0.51 µm of pregnant Tamm-Horsfall protein and uromodulin, respectively). Uromodulin produced fewer particles than Tamm-Horsfall protein in all groups. Nonetheless, the total volume of the crystals produced by uromodulin was higher than that produced by Tamm-Horsfall protein. Our results indicate a different effect of Tamm-Horsfall protein and uromodulin. This dual behavior suggests different functions. Tamm-Horsfall protein may act on nucleation and inhibit crystal aggregation, while uromodulin may promote aggregation of calcium oxalate crystals.

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Section: Discussionmentioning

confidence: 99%

Role of Tamm-Horsfall protein and uromodulin in calcium oxalate crystallization

Carvalho

Mulinari

Nakagawa

2002

Braz J Med Biol Res

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“…This assay was carried out by the method of Hess et al [33]. To 1 ml of potassium oxalate solution taken in the quartz cuvette, 1 ml of CaCl 2 solution was added, so that the final concentration of the incubation mixture was 4.25 m M for calcium and 0.75 m M for oxalate.…”

Section: Methodsmentioning

confidence: 99%

Structural and Functional Modification of THP on Nitration: Comparison with Stone Formers THP

Viswanathan

Kalaiselvi²,

Subashini³

et al. 2004

Nephron Physiol

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Objective: The crucial steps involved in the lithogenic process are governed by the macromolecular components of urine, of which proteins play a major role. Structurally abnormal proteins have been reported to be present in the urine of stone formers. Free radical injury has come a long way in explaining some of the pathophysiological events of renal lithiasis. Thus, our present work was designed to study the impact of the potent oxidant peroxynitrite on the biochemical components of the urinary Tamm-Horsfall glycoprotein (THP). Materials and Methods: Nitration on THP was carried out using peroxynitrite (ONOO^–). After nitration, biochemical components like thiols, S-nitrosothiol, hexose, hexosamine and sialic acid were determined and these factors were compared with those of stone formers and normal THP. Crystallization behavior of control, nitrated NS-THP and stone formers THP was studied. Results: There was a significant decrease in thiol, hexose, hexosamine and sialic acid contents in stone formers and nitrated NS-THP, when compared to that of the control THP. In contrast to this, S-nitrosothiol content was significantly increased in stone formers and nitrated NS-THP (p < 0.001) when compared with the control THP. NO_x metabolites were significantly elevated in stone formers THP when compared with that of control THP. When subjected to CaOx crystallization, stone formers THP and nitrated NS-THP promoted both CaOx nucleation and aggregation, while normal THP was found to be an inhibitor of the above processes. Conclusion: From our results we conclude that nitration of THP could represent one of the prime events in modifying kinetic behavior of THP, thus converting THP into a heterogeneous nucleator of renal calculi formation.

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“…urolithiasis, such as inter-a-trypsin inhibitor, prothrombin families, osteopontin, albumin, Tamm-Horsfall protein, nephrocalcin, and a1-microglobulin (3)(4)(5). However, it is unclear which of the matrix proteins found in the stones are promoters or inhibitors of urolithiasis.…”

Section: Introductionmentioning

confidence: 99%

Mass spectroscopic characteristics of low molecular weight proteins extracted from calcium oxalate stones: preliminary study

Chen

Lai

Tsai

et al. 2008

Clinical Laboratory Analysis

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It is believed that boundary compositions of matrix proteins might play a role in stone formation; however, few proteomic studies concerning matrix proteins in urinary stones have been conducted. In this study, we extracted low molecular weight proteins from calcium oxalate stones and measured their characteristic patterns by mass spectroscopy. A total of 10 stones were surgically removed from patients with urolithiasis. Proteins were extracted from the stones and identified by one‐dimensional electrophoresis (sodium dodecyl sulfate buffer [SDS]–polyacrylamide gel electrophoresis [SDS‐PAGE]). After in‐gel digest, samples were analyzed by the surface‐enhanced laser desorption ionization‐time of flight (SELDI‐TOF) technique. The peptide sequences were analyzed from the data of mass spectroscopy. Proteins were identified from Database Search (SwissProt Protein Database; Swiss Institute of Bioinformatics; http://www.expasy.org/sprot) on a MASCOT server (Matrix Science Ltd.; http://www.matrixscience.com). A total of three bands of proteins (27, 18, and 14 kDa) were identified from SDS‐PAGE in each stone sample. A database search (SwissProt) on a MASCOT server revealed that the most frequently seen proteins from band 1 (27 kDa) were leukocyte elastase precursor, cathepsin G precursor, azurocidin precursor, and myeloblastin precursor (EC 3.4.21.76) (leukocyte proteinase 3); band 2 (18 kDa) comprised calgranulin B, eosinophil cationic protein precursor, and lysozyme C precursor; band 3 (14 kDa) showed neutrophil defensin 3 precursor, calgranulin A, calgranulin C, and histone H4. The modifications and deamidations found from the mass pattern of these proteins may provide information for the study of matrix proteins. Various lower molecular weight proteins can be extracted from calcium oxalate stones. The characteristic patterns and their functions of those proteins should be further tested to investigate their roles in stone formation. J. Clin. Lab. Anal. 22:77–85, 2008. © 2008 Wiley‐Liss, Inc.

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Simultaneous measurements of calcium oxalate crystal nucleation and aggregation: impact of various modifiers

Cited by 70 publications

References 18 publications

Role of Tamm-Horsfall protein and uromodulin in calcium oxalate crystallization

Role of Tamm-Horsfall protein and uromodulin in calcium oxalate crystallization

Structural and Functional Modification of THP on Nitration: Comparison with Stone Formers THP

Mass spectroscopic characteristics of low molecular weight proteins extracted from calcium oxalate stones: preliminary study

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