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Distribution of MP17 in isolated lens fibre membranes
C E Voorter1, J Kistler, W T Gruijters
1Department of Biochemistry, Center for Eye Research, University of Nijmegen, The Netherlands.
Current Eye Research
|July 1, 1989
Abstract:
MP17 is the second most abundant integral membrane protein in the mammalian lens. It has some common features with the major intrinsic polypeptide MIP26, but amino terminal sequencing shows that MP17 is a separate gene product. Both MP17 and MIP26 are abundant in isolated lens fibre membrane vesicles and are not detectable in the fibre gap junctions.
Insights
MP17 is a distinct protein from MIP26 in mammalian eye lenses. Both proteins are found in lens fiber membranes but not in fiber gap junctions.
Area of Science:
- Ophthalmology
- Molecular Biology
- Cell Biology
Background:
- The mammalian lens contains abundant integral membrane proteins crucial for its transparency and function.
- Major intrinsic polypeptide (MIP26) is a well-characterized lens membrane protein.
- The identity and localization of other abundant lens membrane proteins require further elucidation.
Purpose of the Study:
- To characterize MP17, the second most abundant integral membrane protein in the mammalian lens.
- To determine the relationship between MP17 and MIP26.
- To investigate the cellular localization of MP17 and MIP26 within the lens.
Main Methods:
- Integral membrane protein isolation from mammalian lens.
- Amino terminal sequencing for protein identification.
- Analysis of isolated lens fiber membrane vesicles and fiber gap junctions.
Main Results:
- MP17 shares some characteristics with MIP26 but is confirmed as a separate gene product via amino terminal sequencing.
- Both MP17 and MIP26 are highly abundant in isolated lens fiber membrane vesicles.
- Neither MP17 nor MIP26 were detected in isolated fiber gap junctions.
Conclusions:
- MP17 represents a distinct protein entity within the mammalian lens.
- MP17 and MIP26 are localized to the lens fiber membrane, not the fiber gap junctions.
- This finding contributes to understanding the protein composition and organization of the lens membrane.