Details

Autor(en) / Beteiligte

• Shimizu, H
• Fisher, J H
• Papst, P
• Benson, B
• Lau, K
• Mason, R J
• Voelker, D R

Titel

Primary structure of rat pulmonary surfactant protein D. cDNA and deduced amino acid sequence

Ist Teil von

• The Journal of biological chemistry, 1992-01, Vol.267 (3), p.1853-1857

Ort / Verlag

Bethesda, MD: Elsevier Inc

Erscheinungsjahr

1992

Link zum Volltext

Quelle

MEDLINE

Beschreibungen/Notizen

• Surfactant protein D (SP-D) is a carbohydrate-binding glycoprotein containing a collagen-like domain that is synthesized by alveolar type II epithelial cells. The complete primary structure of rat SP-D has been determined by sequencing of a cloned cDNA. The protein consists of three regions: an NH2-terminal segment of 25 amino acids, a collagen-like domain consisting of 59 Gly-X-Y repeats, and a COOH-terminal carbohydrate recognition domain of 153 amino acids. There are 6 cysteine residues present in rat SP-D: 2 in the NH2-terminal noncollagenous segment and 4 in the COOH-terminal carbohydrate-binding domain. The collagenous domain contains one possible N-glycosylation site. The protein is preceded by a cleaved, NH2-terminal signal peptide. SP-D shares considerable homology with the C-type mammalian lectins. Hybridization analysis demonstrates that rat SP-D is encoded by a 1.3-kilobase mRNA which is abundant in lung and highly enriched in alveolar type II cells. Extensive homology exists between rat SP-D and bovine conglutinin.