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Both migration inhibitory factory (MIF) and alpha1-antitrypsin (A1-AT) interact with macrophages. MIF interactions occur during cell-mediated immune responses while A1AT interacts by inhibiting proteolytic enzymes released by macrophages. A comparison of the characteristics of guinea pig MIF and human A1AT in the current literature indicates that both are glycoproteins containing sialic acid with molecular weights of approximately 50,000 daltons. To determine the comparative characteristics of MIF and A1AT, this study partially characterized MIF and A1AT from the dog and evaluated their effect on the in vitro migration of canine pulmonary alveolar macrophages. Canine MIF was produced by stimulating peripheral blood lymphocytes with phytohemagglutinin (PHA) for 72 hr in tissue culture medium. PHA and MIF were separated from culture supernatants by fractionation using Sephadex G-100 Superfine. Canine MIF activity was found in the fractionation pool corresponding to 13,700 daltons. Canine A1AT was isolated from plasma using gel filtration, affinity, and ion-exchange chromatography. The isolated A1AT inhibited trypsin and porcine elastase and had a molecular weight of approximately 110,000 daltons on Sephadex G-100 Superfine and 57,00 daltons after sodium dodecyl sulfate (SDS) electrophoresis. Although the addition of 215 mg A1AT/ml to pulmonary alveolar macrophages inhibited their migration by 28%, much higher concentrations of A1AT are needed to inhibit macrophage migration than those reported for MIF. Furthermore, differences in their molecular weights rule out the possibility of A1AT and MIF being identical molecules. However, A1AT modulated the suggesting that A1AT has the potential of regulating the pulmonary alveolar macrophages’ response to lymphokines.



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Department Name

UNM Biology Department

First Committee Member (Chair)

Oswald G. Baca

Second Committee Member

Roger Orville McClellan

Third Committee Member

David Lee Lundgren

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Biology Commons