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Surfactant protein SP-D is a multimeric collagenous lectin, called collectin. SP-D is a multifunctional, pattern recognition innate immune molecule, which binds in a calcium dependent manner to an array of carbohydrates and lipids, thus offering resistance to invading pathogens, allergen challenge, and pulmonary inflammation. SP-D is predominantly found in the endoplasmic reticulum of type 2 pneumocytes and in the secretory granules of Clara or non-ciliated bronchiolar cells. The highest expression of SP-D is observed in the distal airways and alveoli. There is also an extra pulmonary existence of SP-D. The common sources of native full-length human SP-D are bronchoalveolar lavage (BAL) washings from normal or preferably patients suffering from alveolar proteinosis who overproduce SP-D in the lungs. Amniotic fluid collected at the term during parturition is another reasonable source. Here, we describe a simple and rapid method of purifying native SP-D away from SP-A which is also present in the same source. We also describe procedures of expressing and purifying a recombinant fragment of human SP-D (rhSP-D) comprising trimeric neck and carbohydrate recognition domains that has been shown to have therapeutic effects in murine models of allergy and infection. © 2014 Springer Science+Business Media, New York.

Original publication

DOI

10.1007/978-1-62703-724-2_22

Type

Journal article

Journal

Methods in Molecular Biology

Publication Date

01/01/2014

Volume

1100

Pages

273 - 290