Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Practical bioinformatics for proteomics.

Visith Thongboonkerd1, Jon B Klein

  • 1Core Proteomics Laboratory, Kidney Disease Program, Department of Medicine, University of Louisville, Louisville, Ky., USA. thongboonkerd@dr.com

Contributions to Nephrology
|December 3, 2003
PubMed
Summary
This summary is machine-generated.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Lactobacillus acidophilus abolishes oxalate-mediated renal epithelial barrier disruption and calcium oxalate monohydrate crystal adhesion to renal epithelial cells.

Cellular & molecular biology letters·2026
Same author

Epigallocatechin-3-gallate, L-theanine and theophylline abolish high-glucose-induced renal cell senescence and subsequent epithelial-mesenchymal transition and fibroblast activation via SIRT1/PGC-1α axis: Implications for diabetic kidney disease.

Chemico-biological interactions·2026
Same author

Chlorogenic acid mitigates calcium oxalate monohydrate crystal-induced epithelial-to-mesenchymal transition in renal epithelial cells via suppression of HSP60 expression and p38 signaling.

Cellular & molecular biology letters·2026
Same author

Neutrophil Secretory Proteins Inhibit Calcium Oxalate Crystallisation and Crystal Growth, but Promote Crystal Aggregation.

Immunology·2026
Same author

Promoting Effects of Urinary Proteins from Stone Formers and Influence of Their Physicochemical Properties on Calcium Oxalate Kidney Stone Formation.

Computational and structural biotechnology journal·2026
Same author

Deciphering the impact of <i>SNAI1</i> gene on renal tubular cell proteome, nucleolar stress, ribosome biogenesis, senescence, DNA damage response, and focal adhesion dynamics.

Genes & diseases·2026
Same journal

Adsorption of Pathogens and Blockade of Sepsis Cascade.

Contributions to nephrology·2023
Same journal

Hemoadsorption: Research Agenda and Potential Future Applications.

Contributions to nephrology·2023
Same journal

Hemoperfusion in Poisoning and Drug Overdose.

Contributions to nephrology·2023
Same journal

Hemoperfusion in Burns.

Contributions to nephrology·2023
Same journal

Sequential Extracorporeal Therapy in Sepsis.

Contributions to nephrology·2023
Same journal

The Use of Adsorption in Extracorporeal Liver Support: The Double Plasma Molecular Adsorption System (DPMAS).

Contributions to nephrology·2023
See all related articles

Researchers identified an unknown protein in mouse diabetic kidneys as phosphatidylethanolamine-binding protein (PEBP). This protein contains protein kinase C (PKC) motifs, suggesting a role in diabetic nephropathy pathogenesis.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Bioinformatics

Background:

  • Diabetic nephropathy is a significant complication of diabetes, characterized by kidney damage.
  • The pathogenesis of diabetic nephropathy involves complex molecular pathways, including protein kinase C (PKC) signaling.
  • Identification and characterization of novel proteins involved in disease progression are crucial for understanding and treating diabetic nephropathy.

Purpose of the Study:

  • To identify and characterize an unknown protein upregulated in mouse diabetic kidneys.
  • To investigate the potential role of this protein in the pathogenesis of diabetic nephropathy, particularly in relation to PKC pathways.

Main Methods:

  • Utilized bioinformatic tools to analyze an unknown protein (gi|12841975) identified in mouse diabetic kidneys.

Related Experiment Videos

  • Performed motif scanning to identify conserved functional domains within the protein.
  • Leveraged peptide mass fingerprinting data for protein identification.

    • Main Results:

    • The unknown protein was identified as phosphatidylethanolamine-binding protein (PEBP).
    • Motif scanning revealed the presence of several kinase motifs, notably protein kinase C (PKC) motifs.
    • PEBP was found to be upregulated in mouse diabetic kidneys.

    Conclusions:

    • The study identified PEBP as a protein upregulated in diabetic nephropathy.
    • The presence of PKC motifs suggests PEBP may play a functional role in PKC-dependent pathogenic pathways of diabetic nephropathy.
    • Further research into PEBP phosphorylation and its substrates is warranted to elucidate its role in diabetic kidney disease.