Analysis of Chimeric Proteins Identifies the Regions in the Carbohydrate Recognition Domains of Rat Lung Collectins That Are Essential for Interactions with Phospholipids, Glycolipids, and Alveolar Type II Cells

Sano, Hitomi; Kuroki, Yoshio; Honma, Toshio; Ogasawara, Yoshinori; Sohma, Hitoshi; Voelker, Dennis R.; Akino, Toyoaki

doi:10.1074/jbc.273.8.4783

Cited by 56 publications

(74 citation statements)

References 48 publications

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“…Specifically, SP-D maintains normal surfactant ultrastructure by selectively interacting with small aggregate surfactant, thereby facilitating surfactant uptake by type II cells. The lipid binding specificity of collectins is mediated by the CRD in vitro (42)(43)(44)(45) and intranasal administration of trimeric CRDs decreased intra-alveolar lipid accumulations in Sftpd Ϫ/Ϫ mice (15,24). In contrast, the SP-D CRD and neck domain in the rSftpa/d fusion protein failed to correct surfactant lipid ultrastructure or lower the phospholipid levels when expressed in Sftpd Ϫ/Ϫ mice (22).…”

Section: Discussionmentioning

confidence: 99%

Correction of Pulmonary Abnormalities in Sftpd-/- Mice Requires the Collagenous Domain of Surfactant Protein D

Kingma

Zhang

Ikegami

et al. 2006

Journal of Biological Chemistry

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Section: Discussionmentioning

confidence: 99%

Correction of Pulmonary Abnormalities in Sftpd-/- Mice Requires the Collagenous Domain of Surfactant Protein D

Kingma

Zhang

Ikegami

et al. 2006

Journal of Biological Chemistry

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“…26. Lipids (dioleoylphosphatidylcholine or dioleoyl-phosphatidic acid) were dried under a stream of nitrogen and incubated in TBS (50 mM TrisHCl, pH 7, 0.1 M NaCl) at 37°C for 1 h, followed by vigorous vortexing for 5 min.…”

Section: Methodsmentioning

confidence: 99%

A 25-Amino Acid Sequence of the Arabidopsis TGD2 Protein Is Sufficient for Specific Binding of Phosphatidic Acid

Benning²

2009

Journal of Biological Chemistry

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“…26. Lipids (phosphatidylcholine or a mixture of phosphatidylcholine and PA at 6:4 wt͞wt) were incubated in TBS (50 mM Tris⅐HCl, pH 7͞0.1 M NaCl) at 37°C for 1 h followed by vigorous vortexing for 5 min.…”

Section: Methodsmentioning

confidence: 99%

A phosphatidic acid-binding protein of the chloroplast inner envelope membrane involved in lipid trafficking

Awai

Tamot

et al. 2006

Proc. Natl. Acad. Sci. U.S.A.

202

209

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The biogenesis of the photosynthetic thylakoid membranes inside plant chloroplasts requires enzymes at the plastid envelope and the endoplasmic reticulum (ER). Extensive lipid trafficking is required for thylakoid lipid biosynthesis. Here the trigalactosyldiacylglycerol2 (tgd2) mutant of Arabidopsis is described. To the extent tested, tgd2 showed a complex lipid phenotype identical to the previously described tgd1 mutant. The aberrant accumulation of oligogalactolipids and triacylglycerols and the reduction of molecular species of galactolipids derived from the ER are consistent with a disruption of the import of ER-derived lipids into the plastid. The TGD1 protein is a permease-like component of an ABC transporter located in the chloroplast inner envelope membrane. The TGD2 gene encodes a phosphatidic acid-binding protein with a predicted mycobacterial cell entry domain. It is tethered to the inner chloroplast envelope membrane facing the outer envelope membrane. Presumed bacterial orthologs of TGD1 and TGD2 in Gram-negative bacteria are typically organized in transcriptional units, suggesting their involvement in a common biological process. Expression of the tgd2-1 mutant cDNA caused a dominantnegative effect replicating the tgd2 mutant phenotype. This result is interpreted as the interference of the mutant protein with its native protein complex. It is proposed that TGD2 represents the substrate-binding or regulatory component of a phosphatidic acid͞lipid transport complex in the chloroplast inner envelope membrane.Arabidopsis ͉ membrane transporter ͉ glycerolipids ͉ ABC transporter ͉ substrate-binding protein A s plant leaves expand the demand on the lipid biosynthetic machinery is high because leaf cells contain one of the most extensive membrane systems found in nature, the photosynthetic thylakoid membrane of chloroplasts. The most abundant thylakoid lipids include nonphosphorous galactolipids. Galactolipid biosynthesis involves the formation of phosphatidic acid (PA) in the plastid and at the endoplasmic reticulum (ER) in many plants (1, 2), including Arabidopsis. Fatty acids derived from de novo synthesis in the plastid are assembled into PA in the plastid or at the ER. In Arabidopsis, diacylglycerols derived from the plastid pathway or the ER pathway are present in galactolipids in approximately equal proportion (3). The Arabidopsis lipid galactosyltransferases MGD1 and DGD1, which successively galactosylate diacylglycerol, are associated with the inner and the outer chloroplast envelope membranes, respectively (4). The topology of the galactolipid biosynthetic machinery and the involvement of the ER pathway require extensive subcellular lipid trafficking, most of which is mechanistically not understood.To date, two mutants of Arabidopsis have been described that affect lipid trafficking from the ER to the plastid. The act1(ats1) mutant is deficient in the plastidic glycerol 3-phopshate acyltransferase, and most of the galactolipids in this mutant are derived from the ER pathway (5). In contrast, gala...

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Analysis of Chimeric Proteins Identifies the Regions in the Carbohydrate Recognition Domains of Rat Lung Collectins That Are Essential for Interactions with Phospholipids, Glycolipids, and Alveolar Type II Cells

Abstract: Pulmonary surfactant proteins A (SP-A

Cited by 56 publications

References 48 publications

Correction of Pulmonary Abnormalities in Sftpd-/- Mice Requires the Collagenous Domain of Surfactant Protein D

Correction of Pulmonary Abnormalities in Sftpd-/- Mice Requires the Collagenous Domain of Surfactant Protein D

A 25-Amino Acid Sequence of the Arabidopsis TGD2 Protein Is Sufficient for Specific Binding of Phosphatidic Acid

A phosphatidic acid-binding protein of the chloroplast inner envelope membrane involved in lipid trafficking

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