Neutrophils Show Chemotaxis to Type IV Collagen and Its 7S Domain and Contain a 67 kD Type IV Collagen Binding Protein with Lectin Properties

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Abstract
Neutrophils were found to demonstrate chemotactic responses to pepsinized human placental type IV collagen and its purified aminoterminal 7S domain. The maximal chemotactic responses occur at approximately 400 ng/ml and approximately 30 ng/ml of type IV collagen and 7S collagen, respectively, and are similar in magnitude to the chemotactic response of neutrophils to 10(-8) M FMLP. Human leukemic cells of the HL 60 line display chemotaxis to type IV collagen and 7S collagen only after they are differentiated along the neutrophilic pathway with dimethyl sulfoxide. When detergent extracts of neutrophils are applied to type IV collagen-Affi-Gel resin, a 67 kD protein is retained by the resin and is eluted with guanidine/octyl-beta-glucoside or lactose. This 67 kD polypeptide has an amino acid composition resembling the 67 kD component of the elastin receptor complex, displays immunologic cross-reactivity with antibody to the 67 kD component of the elastin receptor, and binds to elastin and laminin affinity resins. Neutrophil chemotaxis to type IV collagen and 7S collagen is selectively abolished by exposing the test neutrophils to lactose or elastin peptides. We conclude that neutrophils may migrate in vivo to proteolytic fragments of type IV collagen and that this response may be mediated by a lectin-like protein that is similar to the 67 kD component of the elastin receptor.