摘要:

Monoclonal and polyclonal antibodies have been produced against a lens fiber cell extrinsic membrane protein, with a relative molecular weight of approximately 115 kd. Enzyme Linked Immunosorbent Assays (ELISA) of retina, ciliary body-iris, liver, and skeletal muscle, utilizing these antibodies, suggest that the antigen is unique to the lens. Immunocytochemistry indicates that the antigen is present only in the differentiated fiber cell, and is absent from the lens epithelium. Further, immunocytochemical reactivity is predominantly associated with the fiber cell plasma membrane. However, sequential extraction of fiber cell homogenate, followed by quantitative, competitive ELISA analysis, indicates that most of the antigen is recovered in the neutral buffer extract. ELISA analysis using monoclonal antibodies indicates that an analogous antigen is present in human and rabbit lenses. On the basis of these results we characterize this antigen as a conserved extrinsic membrane protein, which is unique to the differentiated lens fiber cell. The relationship of this antigen to a previously described Mr95 beaded filament-associated protein is discussed.

ISSN:0271-3683    

DOI:10.3109/02713688809033228

出版商:Taylor&Francis    

年代:1988

数据来源: Taylor

摘要:

Western blot analysis using a monoclonal antibody raised against a lens fiber cell-specific, extrinsic membrane protein reveals several immunologically related bands in fractions derived from bovine lens. Previous work suggests that the parent molecule is the Mr115 species, and that lower molecular weight bands represent the products of a progressive, step-wise, posttranslational degradation. In this report we compare the extent of proteolytic degradation in extracts prepared from the lens cortex and lens nucleus, using both protease-suppressive and protease-permissive isolation protocols. The results suggest that the observed degradation is a result ofin vivopost-translational modification of the Mr115 antigen, and thus represents physiologic aging of this protein. This analysis also suggests that degradation alters the solubility and/or membrane affinity of this antigen, resulting in a progressive shift to the insoluble phase.

ISSN:0271-3683    

DOI:10.3109/02713688809033229

出版商:Taylor&Francis    

年代:1988

数据来源: Taylor