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J Biol Chem, Vol. 275, Issue 5, 3365-3370, February 4, 2000

The Role of Homodimers in Surfactant Protein B Function in Vivo*

David C. BeckDagger §, Machiko IkegamiDagger , Cheng-Lun NaDagger , Shahparak Zaltash, Jan Johansson, Jeffrey A. WhitsettDagger , and Timothy E. WeaverDagger par

From the Dagger  Division of Pulmonary Biology, Children's Hospital Medical Center, Cincinnati, Ohio 45229-3039 and the  Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, Sweden

Surfactant protein B (SP-B) is detected in the airways as a sulfhydryl-dependent dimer (Mr ~ 16,000). To test the hypothesis that formation of homodimers is critical for SP-B function, the cysteine residue reported to be involved in SP-B dimerization was mutated to serine (Cys248 right-arrow Ser) and the mutated protein was targeted to the distal respiratory epithelium of transgenic mice. Transgenic lines which demonstrated appropriate processing, sorting, and secretion of human SP-B monomer were crossed with SP-B +/- mice to achieve expression of human monomer in the absence of endogenous SP-B dimer (hSP-Bmon, mSP-B-/-). In two of three transgenic lines, hSP-Bmon, mSP-B-/- mice had normal lung structure, complete processing of SP-C proprotein, well formed lamellar bodies, and normal longevity. Pulmonary function studies revealed an altered hysteresis curve for hSP-Bmon, mSP-B-/- mice relative to wild type mice. Large aggregate surfactant fractions from hSP-Bmon, mSP-B-/- mice resulted in higher minimum surface tension in vitro compared with surfactant from wild type mice. Surfactant lipids supplemented with 2% hSP-B monomer resulted in slower adsorption and higher surface tension than surfactant with 2% hSP-B dimer. Taken together, these data indicate a role for SP-B dimer in surface tension reduction in the alveolus.

* This work was supported by National Institutes of Health Grants HL36055 and HL56285 (to T. E. W.), HL38859 (to J. A. W.), and HL61646 (to M. I.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ This work was done in partial fulfillment for the doctoral degree in Molecular and Developmental Biology and the Physician Scientist Training Program at the University of Cincinnati.

par To whom correspondence should be addressed: Children's Hospital Medical Center, Div. of Pulmonary Biology, TCHRF, 3333 Burnet Ave., Cincinnati, OH 45229-3039. Tel.: 513-636-7223; Fax: 513-636-7868; E-mail: Tim.Weaver@chmcc.org.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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