OBJECTIVES: Surfactant protein D (SP-D) is a member of the collectin family of proteins, which are involved in host defense mechanisms in the lung. In the present study, we found that SP-D is produced in the human prostate where it may play a role in innate immunity. METHODS AND RESULTS: Using reverse-transcriptase PCR and Western blot analysis, we demonstrate that SP-D mRNA and protein are present in human prostate tissue. In situ hybridization and immunohistochemistry revealed that SP-D mRNA and protein are localized in epithelial cells of prostate glands. Prostate glands that are surrounded by inflammatory cells produce increased amounts of SP-D protein. We also show that SP-D inhibits the infection of LNCaP and P69SV40T prostate epithelial cells by Chlamydia trachomatis in an in vitro infection assay. Furthermore, using truncated human SP-D mutants, we demonstrate that SP-D binds to Chlamydia trachomatis via its carboxy-terminal lectin domains. CONCLUSIONS: Our in vitro studies suggest that SP-D protects the prostate from infection by pathogens. SP-D protein levels are increased at sites of inflammation in the prostate, suggesting SP-D may also contribute more generally to inflammatory regulation in the prostate. Copyright 2005 Wiley-Liss, Inc
OBJECTIVES:Surfactant protein D (SP-D) is a member of the collectin family of proteins, which are involved in host defense mechanisms in the lung. In the present study, we found that SP-D is produced in the human prostate where it may play a role in innate immunity. METHODS AND RESULTS: Using reverse-transcriptase PCR and Western blot analysis, we demonstrate that SP-D mRNA and protein are present in human prostate tissue. In situ hybridization and immunohistochemistry revealed that SP-D mRNA and protein are localized in epithelial cells of prostate glands. Prostate glands that are surrounded by inflammatory cells produce increased amounts of SP-D protein. We also show that SP-D inhibits the infection of LNCaP and P69SV40T prostate epithelial cells by Chlamydia trachomatis in an in vitro infection assay. Furthermore, using truncated humanSP-D mutants, we demonstrate that SP-D binds to Chlamydia trachomatis via its carboxy-terminal lectin domains. CONCLUSIONS: Our in vitro studies suggest that SP-D protects the prostate from infection by pathogens. SP-D protein levels are increased at sites of inflammation in the prostate, suggesting SP-D may also contribute more generally to inflammatory regulation in the prostate. Copyright 2005 Wiley-Liss, Inc
Authors: Fengqi Hu; Guohua Ding; Zhiyong Zhang; Louis A Gatto; Samuel Hawgood; Francis R Poulain; Robert N Cooney; Guirong Wang Journal: Innate Immun Date: 2015-10-28 Impact factor: 2.680
Authors: Juan Pablo Mackern-Oberti; Mariana Maccioni; Cecilia Cuffini; Gerardo Gatti; Virginia E Rivero Journal: Infect Immun Date: 2006-09-05 Impact factor: 3.441
Authors: A F Christensen; S V Hoegh; T Lottenburger; U Holmskov; I Tornoe; K Hørslev-Petersen; G L Sørensen; P Junker Journal: Rheumatol Int Date: 2010-05-29 Impact factor: 2.631
Authors: Yan Zhou; Jianghua Ming; Yaming Li; Xianjin Du; Ming Deng; Bin He; Jianlin Zhou; Guirong Wang; Shiqing Liu Journal: Biochem Biophys Res Commun Date: 2017-10-31 Impact factor: 3.575
Authors: Rebecca E Oberley; Kelli L Goss; Amado A Quintar; Cristina A Maldonado; Jeanne M Snyder Journal: Reprod Biol Endocrinol Date: 2007-11-07 Impact factor: 5.211
Authors: Stephanie Beileke; Horst Claassen; Walter Wagner; Cord Matthies; Christian Ruf; Arndt Hartmann; Fabian Garreis; Friedrich Paulsen; Martin Schicht; Lars Bräuer Journal: PLoS One Date: 2015-11-24 Impact factor: 3.240