Disease relevance of Tm9sf1

• Cloned cDNAs coding for eye-lens fibre cell-membrane proteins, MIP and MP70, were used to detect restriction fragment length polymorphisms (RFLPs) in genomic DNA from inbred mice with autosomally inherited cataracts [1].

High impact information on Tm9sf1

• Both immunofluorescence microscopy and SDS PAGE reveal an abundance of MP70 in the lens outer cortex that coincides with a high frequency of fiber gap junctions in the same region [2].
• A 70,000-D membrane protein (MP70), which is restricted to the eye lens fibers and is present in immunologically homologous form in many vertebrate species, has been identified [2].
• The N-terminal amino acid sequence of MP70 closely matches the sequence predicted by the clone [3].
• Both MP70 phosphorylation and the endogenous protein kinase activity were restricted to the lens outer cortical region [4].
• The Cx50 (MP70) protein coding region and flanking sequences were amplified from normal parental as well as heterozygous and homozygous mutant genomic DNAs [5].

Biological context of Tm9sf1

• We used primers corresponding to the amino-terminal sequence shared by rat connexin-46 and ovine MP70 and a consensus sequence of the second extracellular loop conserved in all connexins to amplify and subsequently clone from chick genomic DNA a new member of the connexin family of gap junction proteins, chick connexin-56 [6].

Analytical, diagnostic and therapeutic context of Tm9sf1

• A monoclonal antibody directed against MP70 and an anti-Cx50 antibody produced against a synthetic peptide identify the same proteins on western blots and produce identical patterns of immunofluorescence on frozen sections of rodent lens [3].
• Molecular cloning of sheep connexin49 and its identity with MP70 [7].

References