Fibrin adherence to biologic tissues

Studies have been done to determine the biologic adherence characteristics of fibrin to tissue. The presence of fibrin bound to tissue was traced and confirmed by immunofluorescent microscopy utilizing rabbit anti-human fibrin fluorescein isothiocyanate. The connective tissue content of dog skin, ligamentum nuchae, and Achille's tendon were modified by both enzymatic and alkaline hydrolysis treatment to selectively eliminate either collagen or elastin fibers prior to determining whether fibrin would bond to the remaining connective tissue element. Fibrin was found to bond preferentially to collagen fibers, but it also apparently bonded to elastin fibers after alkaline hydrolysis. Whether the hydrolytic process failed to remove all collagen and/or changed native elastin to a collagenlike protein, or whether fibrin bonds equally well to elastin is as yet undecided. These studies therefore indicate that if there is a biologic specificity of fibrin bonding, that specificity is for collagen, not elastin. Whether fibrin will bond to native elastin in the absence of collagen has not been definitely determined.