Abstract
Cold-insoluble globulin (CIG), which is immunochemically indistinguishable from the fibroblast surface protein known as large external transformation-sensitive glycoprotein and fibronectin, was detected immunologically in connective tissue fractions from adult human lung. The fractions tested were (a) intact parenchyma, (b) acidic structural glycoproteins (ASG) extracted from lung parenchyma with 0.3 M acetic acid, and (c) isolated alveolar basement membrane (ABM). For comparison with ABM, preparations of human glomerular basement membrane and human trophoblast basement membrane (TBM) were tested. CIG was not detected in glomerular basement membrane but was present in large amounts in TBM. The CIG antigen could be solubilized from the parenchyma and from ABM by collagenase digestion which indicates that CIG occurs in lung connective tissue in association with collagen. Fibrinogen antigenic determinants were present in the ASG fraction, but the question of whether CIG and fibrin(ogen) are associated in lung connective tissue requires further study. When CIG was quantified by electroimmunoassay, intact lung parenchyma contained approximately equal to 0.4% CIG, ASG contained 3-4.5% CIG, ABM contained 0.1-0.9% CIG and TBM contained 1.5%-7.2% Cg. the evidence suggests that CIG is a chemical constituent of lung connective tissue matrix where it may influence the function of alveoli.