Junction Specificity and Transmembrane Linkages of Integrins

We have also isolated a monoclonal antibody, P4B2, which localizes to multiple adhesion junctions, namely, a subset of focal adhesions, the Z-disc of muscle, and neuromuscular junctions. Immunopurification of the antigen to this antibody from chicken brain tissue yielded a complex of three prominent proteins with mobilities of 36, 30 and 18 kD. Amino acid sequencing of the purified proteins identified the 36 kD protein as GAPDH. The other 2 protein bands were heterogeneous, containing proteins found in the synaptic vesicle fusion core complex. Immunolocalization of P4B2 antigen in developing cultured muscle cells showed that the antigen is incorporated into Z-lines soon after the sarcomeric architecture was positive for α-actinin. Together, the data indicate the P4B2 antigen is part of a unique GAPDH containing protein complex that may be involved in reinforcement of established cytoskeletal structures.

Name thesis:degree_name

Ph.D.

Level thesis:degree_level

Dissertation

Discipline thesis:degree_discipline

Biology

Grantor

University of Illinois at Urbana-Champaign

Year dc:date

2015

Author dc:creator

• McDonald, Kevin Alan

Contributors dc:contributor

• Horwitz, Alan F.

• Biology, Molecular

Language dc:language

eng

Identifier

(MiAaPQ)AAI9737192

OAI identifier oai:identifier

oai:www.ideals.illinois.edu:2142/85391