Tags

Type your tag names separated by a space and hit enter

Novel antilithiatic cationic proteins from human calcium oxalate renal stone matrix identified by MALDI-TOF-MS endowed with cytoprotective potential: an insight into the molecular mechanism of urolithiasis.
Clin Chim Acta. 2013 Jan 16; 415:181-90.CC

Abstract

BACKGROUND

No substantial work has been conducted to date in context to cationic proteins with antilithiatic activity. We explored the antilithiatic cationic proteins present in human calcium oxalate (CaOx) stones and also examined their molecular interactions with calcium oxalate crystals in silico.

METHODS

Proteins were isolated from the matrix of human CaOx containing kidney stones. Proteins having MW>3 kDa were subjected to cation exchange chromatography followed by molecular-sieve chromatography. The effect of these purified cationic proteins was tested against CaOx nucleation and growth and on oxalate injured MDCK cells for their activity. Proteins were identified by MALDI-TOF MS. Molecular interaction studies with COM crystals in silico were also investigated.

RESULTS

Three antilithiatic cationic proteins were identified as histone-lysine N-methyltransferase, inward rectifier K channel and protein Wnt-2 (MW~53, ~44, and ~42 kDa respectively) by MALDI-TOF MS based on database search with MASCOT server. Further molecular modeling calculations revealed the mode of interaction of these proteins with CaOx at the molecular level.

CONCLUSION

We identified histone-lysine N-methyltransferase, inward rectifier K channel and protein Wnt-2 as novel antilithiatic proteins which play a vital role in the kidney function and have been associated with various kidney diseases.

Authors+Show Affiliations

Department of Biotechnology and Bioinformatics, Jaypee University of Information Technology, Waknaghat, Solan-173234 HP, India.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

23123287

Citation

Aggarwal, Kanu Priya, et al. "Novel Antilithiatic Cationic Proteins From Human Calcium Oxalate Renal Stone Matrix Identified By MALDI-TOF-MS Endowed With Cytoprotective Potential: an Insight Into the Molecular Mechanism of Urolithiasis." Clinica Chimica Acta; International Journal of Clinical Chemistry, vol. 415, 2013, pp. 181-90.
Aggarwal KP, Tandon S, Naik PK, et al. Novel antilithiatic cationic proteins from human calcium oxalate renal stone matrix identified by MALDI-TOF-MS endowed with cytoprotective potential: an insight into the molecular mechanism of urolithiasis. Clin Chim Acta. 2013;415:181-90.
Aggarwal, K. P., Tandon, S., Naik, P. K., Singh, S. K., & Tandon, C. (2013). Novel antilithiatic cationic proteins from human calcium oxalate renal stone matrix identified by MALDI-TOF-MS endowed with cytoprotective potential: an insight into the molecular mechanism of urolithiasis. Clinica Chimica Acta; International Journal of Clinical Chemistry, 415, 181-90. https://doi.org/10.1016/j.cca.2012.10.040
Aggarwal KP, et al. Novel Antilithiatic Cationic Proteins From Human Calcium Oxalate Renal Stone Matrix Identified By MALDI-TOF-MS Endowed With Cytoprotective Potential: an Insight Into the Molecular Mechanism of Urolithiasis. Clin Chim Acta. 2013 Jan 16;415:181-90. PubMed PMID: 23123287.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Novel antilithiatic cationic proteins from human calcium oxalate renal stone matrix identified by MALDI-TOF-MS endowed with cytoprotective potential: an insight into the molecular mechanism of urolithiasis. AU - Aggarwal,Kanu Priya, AU - Tandon,Simran, AU - Naik,Pradeep Kumar, AU - Singh,Shrawan Kumar, AU - Tandon,Chanderdeep, Y1 - 2012/11/02/ PY - 2012/08/17/received PY - 2012/10/10/revised PY - 2012/10/10/accepted PY - 2012/11/6/entrez PY - 2012/11/6/pubmed PY - 2013/6/1/medline SP - 181 EP - 90 JF - Clinica chimica acta; international journal of clinical chemistry JO - Clin Chim Acta VL - 415 N2 - BACKGROUND: No substantial work has been conducted to date in context to cationic proteins with antilithiatic activity. We explored the antilithiatic cationic proteins present in human calcium oxalate (CaOx) stones and also examined their molecular interactions with calcium oxalate crystals in silico. METHODS: Proteins were isolated from the matrix of human CaOx containing kidney stones. Proteins having MW>3 kDa were subjected to cation exchange chromatography followed by molecular-sieve chromatography. The effect of these purified cationic proteins was tested against CaOx nucleation and growth and on oxalate injured MDCK cells for their activity. Proteins were identified by MALDI-TOF MS. Molecular interaction studies with COM crystals in silico were also investigated. RESULTS: Three antilithiatic cationic proteins were identified as histone-lysine N-methyltransferase, inward rectifier K channel and protein Wnt-2 (MW~53, ~44, and ~42 kDa respectively) by MALDI-TOF MS based on database search with MASCOT server. Further molecular modeling calculations revealed the mode of interaction of these proteins with CaOx at the molecular level. CONCLUSION: We identified histone-lysine N-methyltransferase, inward rectifier K channel and protein Wnt-2 as novel antilithiatic proteins which play a vital role in the kidney function and have been associated with various kidney diseases. SN - 1873-3492 UR - https://www.unboundmedicine.com/medline/citation/23123287/Novel_antilithiatic_cationic_proteins_from_human_calcium_oxalate_renal_stone_matrix_identified_by_MALDI_TOF_MS_endowed_with_cytoprotective_potential:_an_insight_into_the_molecular_mechanism_of_urolithiasis_ DB - PRIME DP - Unbound Medicine ER -