Abstract

PURPOSE
To understand the mechanism of the function of paired box 6 (Pax6), a master regulator of eye development and functions, Pax6-interacting proteins were studied. It is presumed that the interaction of Pax6 with proteins in terms of morphogenesis and the maintenance of the functional anatomy of the eyes cannot be ignored. The interaction of Pax6 with matricellular protein and transforming growth factors (TGFs) is explored and presented in this report.
METHODS
Co-localization was studied through fluorescence microscopy. The physical interaction of Pax6 interacting proteins was explored through co-immunoprecipitation assay of samples from murine eyes.
RESULTS
It was interesting to observe the co-localization and physical interaction of Pax6, transforming growth factor-beta (TGF-β), and secreted protein acidic and rich in cysteine (SPARC) in murine eyes.
CONCLUSIONS
The interaction of Pax6, TGF-β, and SPARC in murine eyes indicates that Pax6 function is regulated through TGF-β, and SPARC influences the shuttling of Pax6 via the TGF-β/Smad signaling pathway.

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Authors

Shubham K, Mishra R

Institution

Department of Zoology, Banaras Hindu University, Varanasi, India.

Source

Molecular vision 18: 2012 pg 951-6

MeSH

Animals
Eye
Eye Proteins
Homeodomain Proteins
Immunoprecipitation
Mice
Microscopy, Fluorescence
Microtomy
Osteonectin
Paired Box Transcription Factors
Repressor Proteins
Signal Transduction
Tissue Embedding
Transforming Growth Factor beta

Pub Type(s)

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

Language

eng

PubMed ID

22539874