A monoclonal antibody targeted to the functional peptide of ?B-crystallin inhibits the chaperone and anti-apoptotic activities.

ABSTRACT: ?B-Crystallin is a member of the small heat shock protein family. It is a molecular chaperone and an anti-apoptotic protein. Previous studies have shown that the peptide (73DRFSVNLDVKHFSPEELKVKV93, hereafter referred to as peptain-1) from the core domain of ?B-crystallin exhibits both chaperone and anti-apoptotic properties similar to the parent protein. We developed a mouse monoclonal antibody against peptain-1 with the aim of blocking the functions of ?B-crystallin. The antibody reacted with peptain-1, it did not react with the chaperone peptide of ?A-crystallin. The antibody strongly reacted with human recombinant ?B-crystallin but weakly with Hsp20; it did not react with ?A-crystallin or Hsp27. The antibody specifically reacted with ?B-crystallin in human and mouse lens proteins but not with ?A-crystallin. The antibody reacted with ?B-crystallin in human lens epithelial cells, human retinal endothelial cells, and with peptain-1 in peptain-1-transduced cells. Unlike the commercial antibodies against ?B-crystallin, the antibody against peptain-1 inhibited the chaperone and anti-apoptotic activities of peptain-1. The antibody might find use in inhibiting ?B-crystallin's chaperone and anti-apoptotic activities in diseases where ?B-crystallin is a causative or contributing factor.

SUBMITTER: Nahomi RB 

PROVIDER: S-EPMC6677275 | biostudies-literature | 2019 Apr

REPOSITORIES: biostudies-literature