Major intrinsic polypeptide (MIP26K) of the lens membrane: covalent change in an internal sequence during human senile cataractogenesis.
Polyclonal antisera to three synthetic peptides of bovine MIP26K have been used in combination with Western blot analysis to probe for changes of the MIP26K molecule during human senile cataractogenesis. Anti-MIP26K229-237 binds well to the 26K component from cataractous lens membranes, but binds poorly to the same component from normal lens. In contrast, antisera to two other sequences of MIP26K (anti-MIP26K252-259 and anti-MIP26K256-263) bind approximately equally well to the 26K component from either cataractous or normal lens. Together, these results demonstrate that during cataract development there is a selective covalent change in a region of the MIP26K molecule that may have profound effects upon the ability of this molecule to facilitate intercellular communication between lens fiber cells.
D000595:Amino Acid Sequence; D020346:Aquaporins; D002386:Cataract / Q000378:metabolism*; D003101:Collodion; D005136:Eye Proteins / Q000378:metabolism*; D006801:Humans; D007159:Immunologic Tests; D007908:Lens, Crystalline / Q000378:metabolism*; D008562:Membrane Glycoproteins
D020346:Aquaporins; D005136:Eye Proteins; D008562:Membrane Glycoproteins; C030328:aquaporin 0; D003101:Collodion