Human surfactant protein D: SP-D contains a C-type lectin carbohydrate recognition domain

Rust, Kevin; Grosso, Leonard E.; Zhang, Vivian; Chang, Donald; Persson, Anders; Longmore, William J.; Cai, Guang-zuan; Crouch, Edmond C.

doi:10.1016/0003-9861(91)90597-c

Cited by 84 publications

(51 citation statements)

References 39 publications

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“…Therefore, although the requirement for hydroxyl-groups of the mannose-or galactose-type within the binding-site on the carbohydrate molecules is determined by the E-N/Q-D pair of residues, other differences seen in the sequences of the lectin domains, and of the extensive loop carrying the binding sites in particular, seem to be also involved in ligand selection in the in vivo interaction of C-type lectins with complex carbohydrate structures. Domains identified by sequence comparison and predicted to have an overall folding similar to that seen in the crystal structure of the C-type lectin domain of MBP (Weis et al, 1991b), but lacking some of the characteristic residues involved in calcium/carbohydrate binding, are seen in a number of type I1 membrane proteins ( QPD-E-WND gal Tanaka et al, 1988 QPD-E-WND gal Zimmerman & Ruoslahti, 1989 QPD-E-WND gal Drickamer, 1981Spiess & Lodish, 1985Drickamer et al, 1984Ii et al, 1990Hoyle & Hill, 1991Sat0 et al, 1992Curtis et al, 1992Suter et al, 1987Yokoyama et al, 1989Chan & Takei, 1989Giorda et al, 1990Van Hoegen et al, 1990Houchins et al, 1991Wong et al, 1991Yoshimatsu et al, 1992Lee et al, 1991Taylor et al, 1989Drickamer et al, 1986White et al, 1985Benson et al, 1985Rust et al, 1991Holmskov et al, 1993bHolmskov et al, 1993aLasky et al, 1989Bevilacqua et al, 1991Johnson et al, 1989Christa et al, 1994Ng & Hew, 1992Ewart et al, 1992Rouquier et al, 1991Taylor et al, 1990 EPN-E-WND man (Drickamer, 1992). Not all of the carbohydrate specificities have been determined (*), and certain proteins, although a Proteins containing C-type lectin domains or regions w...…”

Section: The Iectin Domainmentioning

confidence: 99%

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Collectins — soluble proteins containing collagenous regions and lectin domains — and their roles in innate immunity

1994

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The collectins are a group of mammalian lectins containing collagen-like regions. They include mannan binding protein, bovine conglutinin, lung surfactant protein A, lung surfactant protein D, and a newly discovered bovine protein named collectin-43. These proteins share a very similar modular domain composition and overall 3-dimensional structure. They also appear to play similar biological roles in the preimmune defense against microorganisms in both serum and lung surfactant. The close evolutionary relationship between the collectins is further emphasized by a common pattern of exons in their genomic structures and the presence of a gene cluster on chromosome 10 in humans that contains the genes known for the human collectins. Studies on the structure/function relationships within the collectins could provide insight into the properties of a growing number of proteins also containing collagenous regions such as Clq, the hibernation protein, the a-and 0-ficolins, as well as the membrane acetylcholinesterase and the macrophage scavenger receptor.

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Section: The Iectin Domainmentioning

confidence: 99%

“…Human SP-D has been cloned at the cDNA (Rust et al, 1991;Lu et al, 1992) and genomic (Crouch et al, 1993) levels. The human SP-D gene (gene symbol SFTP 4) is approximately 11 kb long and contains 8 exons (Fig.…”

Section: Cdna and Genomic Cloning Of The Collectinsmentioning

confidence: 99%

Collectins — soluble proteins containing collagenous regions and lectin domains — and their roles in innate immunity

1994

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“…The CRDs of SP-A and SP-D have about 35 % and 48%, respectively, residues identical to the MBP CRD (Rust et al, 1991). Structural features concerning the SP-A and SP-D CRDs and neck regions can hence be inferred from determined crystal structures of the CRD and CRD plus neck fragments of human (Sherrif et a]., 1994) and rat (Weis et al, 1991(Weis et al, , 1992Weis and Drickamer, 1994) MBP.…”

Section: Structural Properties Of the Collectins Sp-a And Sp-dmentioning

confidence: 99%

Molecular Structures and Interactions of Pulmonary Surfactant Components

Johansson

Curstedt

1997

European Journal of Biochemistry

272

217

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The dominating functional property of pulmonary surfactant is to reduce the surface tension at the alveolar aidliquid interface, and thereby prevent the lungs from collapsing at the end of expiration. In addition, the system exhibits host-defense properties. Insufficient amounts of pulmonary surfactant in premature infants causes respiratory distress syndrome, a serious threat which nowadays can be effectively treated by airway instillation of surfactant preparations. Surfactant is a mixture of many molecular species, mainly phospholipids and specific proteins, surfactant protein A (SP-A), SP-B, SP-C and SP-D. SP-A and SP-D are water-soluble and belong to the collectins, a family of large multimeric proteins which structurally exhibit collagenousAectin hybrid properties and functionally are Caz+-dependent carbohydrate binding proteins involved in innate host-defence functions. SP-A and SP-D also bind lipids and SP-A is involved in organization of alveolar surfactant phospholipids. SP-B belongs to another family of proteins, which includes also lipid-interacting polypeptides with antibacterial and lytic properties. SP-B is a 17.4-kDa homodimer and each subunit contains three intrachain disulphides and has been proposed to contain four amphipathic helices oriented pairwise in an antiparallel fashion. SP-A, SP-B and SP-D all have been detected also in the gastrointestinal tract. SP-C, in contrast, appears to be a unique protein with extreme structural and stability properties and to exist exclusively in the lungs. SP-C is a lipopeptide containing covalently linked palmitoyl chains and is folded into a 3.7-nm a-helix with a central 2.3-nm all-aliphatic part, making it perfectly suited to interact in a transmembranous way with a fluid bilayer composed of dipalmitoylglycerophosphocholine, the main component of surfactant. Homozygous genetic deficiency of proSP-B causes lethal respiratory distress soon after birth and is associated with aberrant processing of the precursor of SP-C. This review focuses on the chemical composition, structures and interactions of the pulmonary surfactant, in particular the associated proteins.

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“…Both rat and human SP-D are 355 amino acids long and share 72% homology. Human SP-D has a short amino terminus of 25 amino acids containing two cysteins followed by a collagenlike domain comprising 177 amino acids with 59 uninterrupted repeats of Gly-Xaa-Yaa and a carboxyl terminus of 153 amino acids that represents a carbohydrate recognition domain [64,65]. Both rat and human SP-D show greater homology to conglutinin (66-67% homology) than to SP-A (36-37% homology).…”

Section: Type I Cellmentioning

confidence: 99%

Host defence capacities of pulmonary surfactant: evidence for ‘non‐surfactant’ functions of the surfactant system

Pison

Max

Neuendank

et al. 1994

Eur J Clin Investigation

142

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Human surfactant protein D: SP-D contains a C-type lectin carbohydrate recognition domain

Cited by 84 publications

References 39 publications

Collectins — soluble proteins containing collagenous regions and lectin domains — and their roles in innate immunity

Collectins — soluble proteins containing collagenous regions and lectin domains — and their roles in innate immunity

Molecular Structures and Interactions of Pulmonary Surfactant Components

Host defence capacities of pulmonary surfactant: evidence for ‘non‐surfactant’ functions of the surfactant system

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