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Domain IV of mouse laminin beta 1 and beta 2 chains - Structure, glycosaminoglycan modification and immunochemical analysis of tissue contents

MPG-Autoren
http://pubman.mpdl.mpg.de/cone/persons/resource/persons78606

Sasaki,  T.
Former Research Groups, Max Planck Institute of Biochemistry, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons78355

Mann,  K.
Mann, Matthias / Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Max Planck Society;
Huber, Robert / Structure Research, Max Planck Institute of Biochemistry, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons78797

Timpl,  R.
Former Research Groups, Max Planck Institute of Biochemistry, Max Planck Society;

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Zitation

Sasaki, T., Mann, K., Miner, J. H., Miosge, N., & Timpl, R. (2002). Domain IV of mouse laminin beta 1 and beta 2 chains - Structure, glycosaminoglycan modification and immunochemical analysis of tissue contents. European Journal of Biochemistry, 269(2), 431-442.


Zitierlink: http://hdl.handle.net/11858/00-001M-0000-0010-7000-A
Zusammenfassung
Domain IV, consisting of about 230 residues, represents a particular protein module so far found only in laminin beta1 and beta2 chains. Both domains were obtained by recombinant production in mammalian cells. They showed a globular structure, as expected from electron microscopic examination of laminins. Fragment beta1IV was obtained as a monomer and a disulfide-bonded dimer, and both were modified to approximate to50% by a single chondroitin sulfate chain attached to Ser721 of an SGD consensus sequence. Dimerization is caused by an odd number of cysteines, with three of them having a partial thiol character. Whether both modifications also occur in tissue forms of laminin remains to be established. Fragment beta21V was only obtained as a monomer, as it lacked one crucial cysteine and the SGD sequence. It required, however, the presence of two adjacent LE modules for proper folding. Polyclonal antibodies raised against both fragments showed no cross-reaction with each other and allowed establishment of beta chain-specific radioimmunoassays and light and electron microscopic immunostaining of tissues. This demonstrated a 5- 25-fold lower content of beta2 compared with beta1 chains in various tissue extracts of adult mice. Tissues derived from beta2-deficient mice failed to react with the beta2-specific antibodies but showed a twofold higher content of beta1 than heterozygotes. The antibodies to beta2 showed broader tissue staining than reported previously, including in particular a distinct reaction with the extra-synaptic endomysium of skeletal muscle. Immunogold staining localized both beta chains primarily to basement membranes of kidney, muscle and various other tissues.