Properties of the globular domain of type IV collagen and its relationship to the Goodpasture antigen.

Abstract

The globular domain of type IV collagen from bovine glomerular basement membrane was solubilized by collagenase digestion. Components of this domain include several monomer-size and structurally related dimer-size polypeptides. The monomer-size polypeptides were resolved into three fractions (M1, M2, and M3) with slightly different mobilities upon sodium dodecyl sulfate-polyacrylamide gel electrophoresis (nonreduced Mr = 24,500-28,300). Chemical and immunochemical studies indicate that each is a distinct component. M2 is reactive with antibodies from patients with Goodpasture syndrome. The molecular weight by sedimentation equilibrium was 32,000 for M2 and 28,000 for M1. The dimers were characterized as two classes, D1 and D2. D1 consists of two sets of nonreactive components (D1a-d and D1a,c) whereas D2 contains one set of four components (D2a-d), each of which is reactive with Goodpasture sera. Chemical and immunochemical studies indicate that a monomer-dimer relationship exists between M1 and D1 and between M2 and D2. The origin of M3 remains undetermined. Rabbit antibodies to type IV collagen alpha chains react with M1 and M2, and antibodies to M1 and M2 react with type IV collagen alpha chains, which provides additional evidence for the localization of the Goodpasture antigen to one of the chains of type IV collagen.