Tissue Distribution of Surfactant Proteins A and D in the Mouse

Akiyama, Jennifer A.; Hoffman, Ari; Brown, Cynthia L.; Allen, Lennell; Edmondson, Jess; Poulain, Francis R; Hawgood, Samuel

doi:10.1177/002215540205000713

Cited by 96 publications

(79 citation statements)

References 14 publications

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“…Extrapulmonary organs such as the salivary gland, thymus, thyroid gland, testis and pancreas also produced clear signals for SP-D mRNA, while a variety of different tissues showed either weak or no expression. These findings, which parallel recent findings by Hawgood and coworkers [24], shows that SP-D and CRP-ductin are co-expressed in several tissues allowing interaction between the two molecules in vivo.…”

Section: Discussionsupporting

confidence: 90%

CRP‐ductin, the mouse homologue of gp‐340/deleted in malignant brain tumors 1 (DMBT1), binds gram‐positive and gram‐negative bacteria and interacts with lung surfactant protein D

et al. 2003

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CRP-ductin is a protein expressed mainly by mucosal epithelial cells in the mouse. Sequence homologies indicate that CRP-ductin is the mouse homologue of human gp-340, a glycoprotein that agglutinates microorganisms and binds the lung mucosal collectin surfactant protein-D (SP-D). Here we report that purified CRP-ductin binds human SP-D in a calcium-dependent manner and that the binding is not inhibited by maltose. The same properties have previously been observed for gp-340 binding of SP-D. CRP-ductin also showed calcium-dependent binding to both gram-positive and -negative bacteria. A polyclonal antibody raised against gp-340 reacted specifically with CRP-ductin in Western blots. Immunoreactivity to CRP-ductin was found in the exocrine pancreas, in epithelial cells throughout the gastrointestinal tract and in the parotid ducts. A panel of RNA preparations from mouse tissues was screened for CRP-ductin and SP-D expression by reverse transcription-PCR. The pancreas was the main site of synthesis of CRP-ductin, but transcripts were also readily amplified from salivary gland, the gastrointestinal tract, liver, testis, uterus and lung. Lung was the main site of synthesis of SP-D, but transcripts were also amplified from uterus, salivary gland, thymus, thyroid gland, pancreas and testis. We conclude that CRP-ductin is the mouse homologue of human gp-340 and that its capacity to bind SP-D as well as gramnegative and gram-positive bacteria suggests a role in mucosal immune defense.

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Section: Discussionsupporting

confidence: 90%

CRP‐ductin, the mouse homologue of gp‐340/deleted in malignant brain tumors 1 (DMBT1), binds gram‐positive and gram‐negative bacteria and interacts with lung surfactant protein D

et al. 2003

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“…As proposed for the collectin lung surfactant protein D, which was found to be expressed on several mucosal surfaces in humans and mice, MBL-C as part of the innate immune system could be seen as a counterpart of secretory IgA of the acquired immune system (18,19). Due to its capability to bind to various micro-organisms, MBL-C as well as IgA may protect the small intestine against invading pathogens.…”

Section: Discussionmentioning

confidence: 96%

Differential Expression of the Murine Mannose-Binding Lectins A and C in Lymphoid and Nonlymphoid Organs and Tissues

Wagner

Lynch

Walter

et al. 2003

The Journal of Immunology

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Mannose-binding lectin (MBL), a member of the collectin family, binds to carbohydrate structures on the surfaces of micro-organisms and may serve as a recognition molecule of the lectin pathway of complement activation. In rodents two forms, MBL-A and MBL-C, were described and shown to be products of two related, but uncoupled, genes. The liver is the main source of MBL biosynthesis. For rat MBL-A, expression has also been described in the kidney. Here we report that the two forms of murine MBL are differentially expressed in a number of nonhepatic tissues. Real-time RT-PCR revealed that the liver is the major site of expression for both MBL genes. Lower copy numbers were found in kidney, brain, spleen, and muscle. In testis, only the MBL-A gene is expressed, whereas MBL-C is exclusively expressed in small intestine. Using in situ hybridization and immunohistochemistry, we demonstrate that both MBLs are synthesized by hepatocytes and show MBL expression in cells of the monocyte/macrophage lineage. In the kidney MBL-A, but not MBL-C, was found to be synthesized. Vice versa, only MBL-C biosynthesis was detected in endothelial cells of the small intestine. The latter finding may support the view that MBL-C, as part of the innate immune system, may be a counterpart of secretory IgA of the acquired immune system in preventing, for example, microbial invasion and colonization. Our findings demonstrate that MBL-A and MBL-C are differentially expressed, implying distinct biological roles for both recognition molecules of the murine lectin pathway of complement.

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“…SP-A1 and SP-A2 are expressed in the type II cells; SP-A2 is expressed in human tracheal and bronchial submucosal gland cells (15,18). The presence of SP-A in nonciliated bronchiolar epithelial cells has been inconsistent for human lungs (14,19,20), but consistent positive staining of SP-A has been observed in the nonciliated bronchiolar epithelial cells in rodents (21,22). Although a 2:1 ratio of SP-A1 to SP-A2 was suggested in a model of SP-A oligomerization by Voss et al (23), experimental data have indicated a range beyond the proposed 2:1 ratio at the mRNA (24) and protein levels (25).…”

mentioning

confidence: 99%

Humanized SFTPA1 and SFTPA2 Transgenic Mice Reveal Functional Divergence of SP-A1 and SP-A2

Wang

Guo

DiAngelo

et al. 2010

Journal of Biological Chemistry

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Tissue Distribution of Surfactant Proteins A and D in the Mouse

Cited by 96 publications

References 14 publications

CRP‐ductin, the mouse homologue of gp‐340/deleted in malignant brain tumors 1 (DMBT1), binds gram‐positive and gram‐negative bacteria and interacts with lung surfactant protein D

CRP‐ductin, the mouse homologue of gp‐340/deleted in malignant brain tumors 1 (DMBT1), binds gram‐positive and gram‐negative bacteria and interacts with lung surfactant protein D

Differential Expression of the Murine Mannose-Binding Lectins A and C in Lymphoid and Nonlymphoid Organs and Tissues

Humanized SFTPA1 and SFTPA2 Transgenic Mice Reveal Functional Divergence of SP-A1 and SP-A2

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