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SP-D  -  surfactant protein D

Ovis aries

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Disease relevance of SP-D

  • In conclusion, cell-associated SP-D protein expression significantly decreases within hyperplastic epithelium of lungs from infected animals during chronic bronchopneumonia [1].
  • The purpose of this study was to determine the extent to which parainfluenza type 3 virus infection in neonatal lambs alters expression of sheep beta-defensin 1 (SBD-1), SP-A, and SP-D, all of which are constitutively transcribed by respiratory epithelia [2].
  • At 15 and 45 days post-inoculation, areas of lung had peribronchiolar inflammatory cell infiltrate, epithelial cell hyperplasia, tortuosity of the airway lumens, and decreased intensity of SP-D protein staining and number of positive cells [1].
  • Since a hallmark of bronchopneumonia is the initiation of inflammation in the bronchi and bronchoalveolar junction, we chose a classic ruminant model of bronchopneumonia caused by Mannheimia haemolytica to study the expression of SP-D within the bronchioles of infected lambs [1].
  • Exhaustion of SP-D protein reserves and absence of SP-D gene upregulation during the progression of bacterial pneumonia into chronicity may result in failure to clear the pathogen from the lung and/or cause animals to be more susceptible to re-infection [1].

High impact information on SP-D


Analytical, diagnostic and therapeutic context of SP-D


  1. Surfactant protein D expression in normal and pneumonic ovine lung. Grubor, B., Gallup, J.M., Ramírez-Romero, R., Bailey, T.B., Crouch, E.C., Brogden, K.A., Ackermann, M.R. Vet. Immunol. Immunopathol. (2004) [Pubmed]
  2. Enhanced surfactant protein and defensin mRNA levels and reduced viral replication during parainfluenza virus type 3 pneumonia in neonatal lambs. Grubor, B., Gallup, J.M., Meyerholz, D.K., Crouch, E.C., Evans, R.B., Brogden, K.A., Lehmkuhl, H.D., Ackermann, M.R. Clin. Diagn. Lab. Immunol. (2004) [Pubmed]
  3. A recombinant homotrimer, composed of the alpha helical neck region of human surfactant protein D and C1q B chain globular domain, is an inhibitor of the classical complement pathway. Kishore, U., Strong, P., Perdikoulis, M.V., Reid, K.B. J. Immunol. (2001) [Pubmed]
  4. Regulation of surfactant protein and defensin mRNA expression in cultured ovine type II pneumocytes by all-trans retinoic acid and VEGF. Grubor, B., Meyerholz, D.K., Lazic, T., Demacedo, M.M., Derscheid, R.J., Hostetter, J.M., Gallup, J.M., Demartini, J.C., Ackermann, M.R. International journal of experimental pathology. (2006) [Pubmed]
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