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Surfactant protein A2
External IDs OMIM178642 HomoloGene121995 GeneCards: SFTPA2 Gene
Species Human Mouse
Entrez 729238 n/a
Ensembl ENSG00000185303 n/a
UniProt Q8IWL1 n/a
RefSeq (mRNA) NM_001098668 n/a
RefSeq (protein) NP_001092138 n/a
Location (UCSC) Chr 10:
79.56 – 79.56 Mb
PubMed search [1] n/a

Pulmonary surfactant-associated protein A2 (PSP-A) also known as surfactant protein A2 (SP-A2) is a protein that in humans is encoded by the SFTPA2 gene.[1][2]


The protein encoded by this gene (SP-A2) is primarily synthesized in lung alveolar type II cells (see type II pneumocyte), as part of a complex of lipids and proteins known as pulmonary surfactant. The function of this complex is to reduce surface tension in the alveolus and prevent collapse during expiration. The protein component of surfactant helps in the modulation of the innate immune response, and inflammatory processes.[3]

Alveolar sac region of the lung - TEM

SP-A2 is a member of a subfamily of C-type lectins called collectins. Together with SP-A1 (see SFTPA1), they are the most abundant proteins of pulmonary surfactant. SP-A2 binds to the carbohydrates found in the surface of several microorganisms and helps in the defense against respiratory pathogens.[4][5][6]

Surfactant homeostasis is critical for breathing (and thus survival) in the prematurely born infant, but also for maintaining lung health, and normal lung function throughout life. Quantitative and/or qualitative alterations in surfactant composition and/or function are associated with respiratory diseases.[7][8][9][10]

SFTPA2 expression[edit]

The lung is the main site of SFTPA2 synthesis, but SFTPA2 mRNA expression has also been detected in the trachea, prostate, pancreas, thymus, colon, eye, salivary gland and other tissues. While the majority of these tissues express both SFTPA2 and SFTPA1 transcripts, only SFTPA2 expression was found in the trachea and prostate.[11] Using specific monoclonal antibodies for Surfactant protein A, the protein can be detected in lung alveolar type II pneumocytes, Clara cells, and alveolar macrophages, but no extrapulmonary SP-A immunoreactivity was observed.[11]


SFTPA2 is located in the long arm of chromosome 10, close to SFTPA1. The SFTPA2 gene is 4556 base pairs in length, and 94% similar to SFTPA1. The structure of SFTPA2 consists of four coding exons (I-IV), and several 5'UTR untranslated exons (A, B, B’, C, C’,D, D’).[12][13] The expression of SFTPA2 is regulated by cellular factors including proteins, small RNAs (microRNAs), glucocorticoids, etc. Its expression is also regulated by epigenetic and environmental factors.[14]

Differences in the SFTPA2 gene sequence at the coding region determine SP-A genetic variants or haplotypes among individuals.[13] More than 30 variants have been identified and characterized for SFTPA2 (and SFTPA1) in the population. SFTPA2 variants result from nucleotide changes in the codons of amino acids 9, 91, 140, and 223. Three of these do not modify the SP-A2 protein sequence (amino acids 9, 91, and 223), whereas the remaining one results in an amino acid substitution (amino acid 140). Six SP-A2 variants (1A, 1A0, 1A1, 1A2, 1A3, 1A5) are in higher frequency in the general population. The most frequently found variant is 1A0.[15][16]


SP-A2 is a protein of 248 amino acids usually found in large oligomeric structures. The mature SP-A2 monomer is a 35kDa protein that differs from SP-A1 in four amino acids at the coding region. The structure of SP-A2 monomers consists of four domains: an N-terminal, a collagen-like domain, a neck region, and a carbohydrate recognition domain. The C-terminal carbohydrate recognition domain (CRD) allows binding to various types of microorganisms and molecules.[15][16] The amino acid differences that distinguish between SFTPA2 and SFTPA1 genes and between their corresponding variants are located at the collagen-like domain. The amino acid differences that distinguish among SFTPA2 variants are located both at the carbohydrate recognition and the collagen-like domains.[15][17]

SP-A2 monomers group with other SP-A2 or SP-A1 monomers in trimeric structural subunits of 105kDa. Six of these structures group in 630 kDa structures that resemble flower bouquets. These oligomers contain a total of eighteen SP-A2 and/or SP-A1 monomers.[15]


Innate immunity[edit]

The role of SFTPA2 in innate immunity has been extensively studied. SP-A has the ability to bind and agglutinate bacteria, fungi, viruses, and other non-biological antigens. Some of the functions by which both SFTPA2 and SFTPA1 contribute to innate immunity include:

Environmental insults such as air pollution, and exposure to high concentrations of ozone and particulate matter can affect SP-A expression and function, via mechanisms that involve epigenetic regulation of SFTPA2 expression.[18]

Clinical significance[edit]

Deficiency in SP-A levels is associated with infant respiratory distress syndrome in prematurely born infants with developmental insufficiency of surfactant production and structural immaturity in the lungs.[19] Alterations of the relative levels of SP-A1 and SP-A2 have been found in BALF from patients with cystic fibrosis,[20] asthma,[21] and infection.[20]

SFTPA2 genetic variants, SNPs, haplotypes, and other genetic variations have been associated with acute and chronic lung disease in several populations of neonates, children, and adults.[7] Mutations in the SFTPA2 gene are found in patients with interstitial lung disease and lung cancer.[22] SFTPA2 mutations also associated with pulmonary fibrosis via mechanisms that involve protein instability and endoplasmic reticulum stress.[23] Methylation of SFTPA2 and SFTPA1 promoter sequences has also been found in lung cancer tissue.[24][25]

SFTPA2 mRNA transcript variants[edit]

Variant id 5’UTR splice Coding 3’UTR sequence GenBank id
ABD1A ABD 1A 1A HQ021432
ABD1A0 ABD 1A0 1A0 HQ021421
ABD1A1 ABD 1A1 1A1 HQ021422
ABD1A2 ABD 1A2 1A2 HQ021423
ABD1A3 ABD 1A3 1A3 HQ021424
ABD1A5 ABD 1A5 1A5 HQ021425
ABD'1A ABD' 1A 1A HQ021426
ABD'1A0 ABD' 1A0 1A0 HQ021427
ABD'1A1 ABD' 1A1 1A1 HQ021428
ABD'1A2 ABD' 1A2 1A2 HQ021429
ABD'1A3 ABD' 1A3 1A3 HQ021430
ABD'1A5 ABD' 1A5 1A5 HQ021431
SFTPA2 ABD’ 1A2 1A0 NM_001098668.2

Gene regulation[edit]

Gene expression of SFTPA2 is regulated at different levels including gene transcription, post-transcriptional processing, stability and translation (biology) of mature mRNA.[26] One of the important features of human surfactant protein A mRNAs is that they have a variable five prime untranslated region (5’UTR) generated from splicing variation of exons A, B, C, and D.[27][28] At least 10 forms of human SFTPA2 and SFTPA1 5’UTRs have been identified that differ in nucleotide sequence, length, and relative amount.[29] Most SFTPA2 specific 5’UTRs include exon B. This 30-nucleotide long sequence has been shown to enhance both gene transcription and protein translation (biology), and plays a key role in the differential regulation of SFTPA2 and SFTPA1 expression.[30] Both ABD and ABD’ are the most represented forms among SFTPA2 transcripts (~49% each),[29] and experimental work has shown that this sequence can stabilize mRNA, enhance translation, and activate cap-independent eukaryotic translation.[31][32][33][34] Exon B of SFTPA2 also binds specific proteins (e.g. 14-3-3) that may enhance translation, in a sequence- and secondary structure- specific way.[33] While differences at the 5’UTR are shown to regulate both transcription and translation,[30] polymorphisms at the 3’UTR of SP-A2 variants are shown to primarily, differentially affect translation efficiency [32] via mechanisms that involve binding of proteins [35] and/or [microRNAs].[32] The impact of this regulation on SFTPA2 relative protein levels may contribute to individual differences in susceptibility to lung disease.[20][21] Environmental insults and pollutants also affect SFTPA2 expression. Exposure of lung cells to particulate matter affects splicing of 5’UTR exons of SFTPA2 transcripts. Pollutants and viral infections also affect SFTPA2 translation mechanisms (see eukaryotic translation, translation (biology)).[31][36]

See also[edit]


  1. ^ "Entrez Gene: SFTPA2 surfactant, pulmonary-associated protein A2". 
  2. ^ Silveyra P, Floros J (December 2013). "Genetic complexity of the human surfactant-associated proteins SP-A1 and SP-A2". Gene 531 (2): 126–32. doi:10.1016/j.gene.2012.09.111. PMC 3570704. PMID 23069847. 
  3. ^ Perez-Gil J, Weaver TE (June 2010). "Pulmonary surfactant pathophysiology: current models and open questions". Physiology (Bethesda) 25 (3): 132–41. doi:10.1152/physiol.00006.2010. PMID 20551227. 
  4. ^ Crouch EC (August 1998). "Collectins and pulmonary host defense". Am. J. Respir. Cell Mol. Biol. 19 (2): 177–201. doi:10.1165/ajrcmb.19.2.140. PMID 9698590. 
  5. ^ Crouch E, Hartshorn K, Ofek I (February 2000). "Collectins and pulmonary innate immunity". Immunol. Rev. 173: 52–65. doi:10.1034/j.1600-065x.2000.917311.x. PMID 10719667. 
  6. ^ Phelps DS (2001). "Surfactant regulation of host defense function in the lung: a question of balance". Pediatr Pathol Mol Med 20 (4): 269–92. doi:10.1080/15513810109168822. PMID 11486734. 
  7. ^ a b Silveyra P, Floros J (2012). "Genetic variant associations of human SP-A and SP-D with acute and chronic lung injury". Front. Biosci. 17: 407–29. doi:10.2741/3935. PMID 22201752. 
  8. ^ Floros J, Kala P (1998). "Surfactant proteins: molecular genetics of neonatal pulmonary diseases". Annu. Rev. Physiol. 60: 365–84. doi:10.1146/annurev.physiol.60.1.365. PMID 9558469. 
  9. ^ Floros J, Wang G (May 2001). "A point of view: quantitative and qualitative imbalance in disease pathogenesis; pulmonary surfactant protein A genetic variants as a model". Comp. Biochem. Physiol., Part A Mol. Integr. Physiol. 129 (1): 295–303. doi:10.1016/S1095-6433(01)00325-7. PMID 11369553. 
  10. ^ Whitsett JA, Wert SE, Weaver TE (2010). "Alveolar surfactant homeostasis and the pathogenesis of pulmonary disease". Annu. Rev. Med. 61: 105–19. doi:10.1146/annurev.med.60.041807.123500. PMID 19824815. 
  11. ^ a b Madsen, J.; Tornøe, I.; Nielsen, O.; Koch, C.; Steinhilber, W.; Holmskov, U. (2003). "Expression and Localization of Lung Surfactant Protein a in Human Tissues". American Journal of Respiratory Cell and Molecular Biology 29 (5): 591–597. doi:10.1165/rcmb.2002-0274OC. PMID 12777246. 
  12. ^ Floros J, Hoover RR (November 1998). "Genetics of the hydrophilic surfactant proteins A and D". Biochim. Biophys. Acta 1408 (2-3): 312–22. doi:10.1016/S0925-4439(98)00077-5. PMID 9813381. 
  13. ^ a b DiAngelo S, Lin Z, Wang G, Phillips S, Ramet M, Luo J, Floros J (December 1999). "Novel, non-radioactive, simple and multiplex PCR-cRFLP methods for genotyping human SP-A and SP-D marker alleles". Dis. Markers 15 (4): 269–81. doi:10.1155/1999/961430. PMID 10689550. 
  14. ^ Silveyra P, Floros J (2012). "Air pollution and epigenetics: effects on SP-A and innate host defence in the lung". Swiss Med Wkly 142: w13579. doi:10.4414/smw.2012.13579. PMC 3601480. PMID 22553125. 
  15. ^ a b c d Floros J, Wang G, Mikerov AN (2009). "Genetic complexity of the human innate host defense molecules, surfactant protein A1 (SP-A1) and SP-A2--impact on function". Crit. Rev. Eukaryot. Gene Expr. 19 (2): 125–37. doi:10.1615/critreveukargeneexpr.v19.i2.30. PMC 2967201. PMID 19392648. 
  16. ^ a b Floros J, Wang G, Lin Z (2005). "Genetic Diversity of Human SP-A, a Molecule with Innate host Defense and Surfactant-Related Functions; Characteristics, Primary Function, and Significance". Current Pharmacogenomics 3 (2): 87–95. doi:10.2174/1570160054022935. 
  17. ^ Wang G, Myers C, Mikerov A, Floros J (July 2007). "Effect of cysteine 85 on biochemical properties and biological function of human surfactant protein A variants". Biochemistry 46 (28): 8425–35. doi:10.1021/bi7004569. PMC 2531219. PMID 17580966. 
  18. ^ Silveyra, P.; Floros, J. (2012). "Air pollution and epigenetics: Effects on SP-A and innate host defence in the lung". Swiss Medical Weekly 142: w13579. doi:10.4414/smw.2012.13579. PMC 3601480. PMID 22553125. 
  19. ^ deMello DE, Heyman S, Phelps DS, Floros J (May 1993). "Immunogold localization of SP-A in lungs of infants dying from respiratory distress syndrome". Am. J. Pathol. 142 (5): 1631–40. PMC 1886897. PMID 8494055. 
  20. ^ a b c Tagaram HR, Wang G, Umstead TM, Mikerov AN, Thomas NJ, Graff GR, Hess JC, Thomassen MJ, Kavuru MS, Phelps DS, Floros J (May 2007). "Characterization of a human surfactant protein A1 (SP-A1) gene-specific antibody; SP-A1 content variation among individuals of varying age and pulmonary health". Am. J. Physiol. Lung Cell Mol. Physiol. 292 (5): L1052–63. doi:10.1152/ajplung.00249.2006. PMID 17189324. 
  21. ^ a b Wang Y, Voelker DR, Lugogo NL, Wang G, Floros J, Ingram JL, Chu HW, Church TD, Kandasamy P, Fertel D, Wright JR, Kraft M (October 2011). "Surfactant protein A is defective in abrogating inflammation in asthma". Am. J. Physiol. Lung Cell Mol. Physiol. 301 (4): L598–606. doi:10.1152/ajplung.00381.2010. PMC 3191759. PMID 21784968. 
  22. ^ Maitra, M.; Cano, C. A.; Garcia, C. K. (2012). "Mutant surfactant A2 proteins associated with familial pulmonary fibrosis and lung cancer induce TGF- 1 secretion". Proceedings of the National Academy of Sciences 109 (51): 21064–21069. doi:10.1073/pnas.1217069110. PMC 3529022. PMID 23223528. 
  23. ^ Maitra, M.; Wang, Y.; Gerard, R. D.; Mendelson, C. R.; Garcia, C. K. (2010). "Surfactant Protein A2 Mutations Associated with Pulmonary Fibrosis Lead to Protein Instability and Endoplasmic Reticulum Stress". Journal of Biological Chemistry 285 (29): 22103–22113. doi:10.1074/jbc.M110.121467. PMC 2903395. PMID 20466729. 
  24. ^ Vaid, M.; Floros, J. (2009). "Surfactant protein DNA methylation: A new entrant in the field of lung cancer diagnostics? (Review)". Oncology reports 21 (1): 3–11. PMC 2899699. PMID 19082436. 
  25. ^ Lin, Z.; Thomas, N. J.; Bibikova, M.; Seifart, C.; Wang, Y.; Guo, X.; Wang, G.; Vollmer, E.; Goldmann, T.; Garcia, E. W.; Zhou, L.; Fan, J. B.; Floros, J. (2007). "DNA methylation markers of surfactant proteins in lung cancer". International journal of oncology 31 (1): 181–191. doi:10.3892/ijo.31.1.181. PMID 17549420. 
  26. ^ Silveyra, P.; Floros, J. (2012). "Genetic complexity of the human surfactant-associated proteins SP-A1 and SP-A2". Gene: S0378–S1119(12)S1119–6 S1119.1016/S1119.gene.S1119.09.S1119. doi:10.1016/j.gene.2012.09.111. PMC 3570704. PMID 23069847. 
  27. ^ Karinch, A. M.; Deiter, G.; Ballard, P. L.; Floros, J. (1998). "Regulation of expression of human SP-A1 and SP-A2 genes in fetal lung explant culture". Biochimica et biophysica acta 1398 (2): 192–202. doi:10.1016/S0167-4781(98)00047-5. PMID 9689918. 
  28. ^ Karinch, A. M.; Floros, J. (1995). "Translation in vivo of 5' untranslated-region splice variants of human surfactant protein-A". The Biochemical journal. 307 ( Pt 2) (Pt 2): 327–330. PMC 1136651. PMID 7733864. 
  29. ^ a b Karinch, A. M.; Floros, J. (1995). "5' splicing and allelic variants of the human pulmonary surfactant protein a genes". American Journal of Respiratory Cell and Molecular Biology 12 (1): 77–88. doi:10.1165/ajrcmb.12.1.7811473. PMID 7811473. 
  30. ^ a b Silveyra, P.; Raval, M.; Simmons, B.; Diangelo, S.; Wang, G.; Floros, J. (2011). "The untranslated exon B of human surfactant protein A2 mRNAs is an enhancer for transcription and translation". AJP: Lung Cellular and Molecular Physiology 301 (5): L795–L803. doi:10.1152/ajplung.00439.2010. PMC 3290452. PMID 21840962. 
  31. ^ a b Wang, G.; Guo, X.; Silveyra, P.; Kimball, S. R.; Floros, J. (2009). "Cap-independent translation of human SP-A 5'-UTR variants: A double-loop structure and cis-element contribution". AJP: Lung Cellular and Molecular Physiology 296 (4): L635–L647. doi:10.1152/ajplung.90508.2008. PMC 2670766. PMID 19181744. 
  32. ^ a b c Silveyra, P.; Wang, G.; Floros, J. (2010). "Human SP-A1 (SFTPA1) variant-specific 3' UTRs and poly(A) tail differentially affect the in vitro translation of a reporter gene". AJP: Lung Cellular and Molecular Physiology 299 (4): L523–L534. doi:10.1152/ajplung.00113.2010. PMC 2957414. PMID 20693318. 
  33. ^ a b Noutsios, G. T.; Silveyra, P.; Bhatti, F.; Floros, J. (2013). "Exon B of human surfactant protein A2 mRNA, alone or within its surrounding sequences interacts with 14-3-3; role of cis elements and secondary structure". AJP: Lung Cellular and Molecular Physiology 304 (11): L722–35. doi:10.1152/ajplung.00324.2012. PMID 23525782. 
  34. ^ Wang, G.; Guo, X.; Floros, J. (2005). "Differences in the translation efficiency and mRNA stability mediated by 5'-UTR splice variants of human SP-A1 and SP-A2 genes". AJP: Lung Cellular and Molecular Physiology 289 (3): L497–L508. doi:10.1152/ajplung.00100.2005. PMID 15894557. 
  35. ^ Wang, G.; Guo, X.; Floros, J. (2003). "Human SP-A 3'-UTR variants mediate differential gene expression in basal levels and in response to dexamethasone". American journal of physiology. Lung cellular and molecular physiology 284 (5): L738–L748. doi:10.1152/ajplung.00375.2002. PMID 12676764. 
  36. ^ Bruce, S. R.; Atkins, C. L.; Colasurdo, G. N.; Alcorn, J. L. (2009). "Respiratory syncytial virus infection alters surfactant protein a expression in human pulmonary epithelial cells by reducing translation efficiency". AJP: Lung Cellular and Molecular Physiology 297 (4): L559–L567. doi:10.1152/ajplung.90507.2008. PMC 2770795. PMID 19525387. 

Further reading[edit]

  • Floros J, Hoover RR (1999). "Genetics of the hydrophilic surfactant proteins A and D.". Biochim. Biophys. Acta 1408 (2-3): 312–22. doi:10.1016/S0925-4439(98)00077-5. PMID 9813381. 
  • Katyal SL, Singh G, Locker J (1992). "Characterization of a second human pulmonary surfactant-associated protein SP-A gene.". Am. J. Respir. Cell Mol. Biol. 6 (4): 446–52. doi:10.1165/ajrcmb/6.4.446. PMID 1372511. 
  • Voss T, Melchers K, Scheirle G, Schäfer KP (1991). "Structural comparison of recombinant pulmonary surfactant protein SP-A derived from two human coding sequences: implications for the chain composition of natural human SP-A.". Am. J. Respir. Cell Mol. Biol. 4 (1): 88–94. doi:10.1165/ajrcmb/4.1.88. PMID 1986781. 
  • Haagsman HP, White RT, Schilling J, Lau K, Benson BJ, Golden J, Hawgood S, Clements JA (1990). "Studies of the structure of lung surfactant protein SP-A.". Am. J. Physiol. 257 (6 Pt 1): L421–9. PMID 2610270. 
  • White RT, Damm D, Miller J, Spratt K, Schilling J, Hawgood S, Benson B, Cordell B (1985). "Isolation and characterization of the human pulmonary surfactant apoprotein gene.". Nature 317 (6035): 361–3. doi:10.1038/317361a0. PMID 2995821. 
  • Floros J, Steinbrink R, Jacobs K, Phelps D, Kriz R, Recny M, Sultzman L, Jones S, Taeusch HW, Frank HA (1986). "Isolation and characterization of cDNA clones for the 35-kDa pulmonary surfactant-associated protein.". J. Biol. Chem. 261 (19): 9029–33. PMID 3755136. 
  • Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1-2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298. 
  • McCormick SM, Boggaram V, Mendelson CR (1994). "Characterization of mRNA transcripts and organization of human SP-A1 and SP-A2 genes.". Am. J. Physiol. 266 (4 Pt 1): L354–66. PMID 8179012. 
  • Kölble K, Lu J, Mole SE, Kaluz S, Reid KB (1993). "Assignment of the human pulmonary surfactant protein D gene (SFTP4) to 10q22-q23 close to the surfactant protein A gene cluster.". Genomics 17 (2): 294–8. doi:10.1006/geno.1993.1324. PMID 8406480. 
  • Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library.". Gene 200 (1-2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149. 
  • Stuart GR, Lynch NJ, Day AJ, Schwaeble WJ, Sim RB (1998). "The C1q and collectin binding site within C1q receptor (cell surface calreticulin).". Immunopharmacology 38 (1-2): 73–80. doi:10.1016/S0162-3109(97)00076-3. PMID 9476117. 
  • Karinch AM, Deiter G, Ballard PL, Floros J (1998). "Regulation of expression of human SP-A1 and SP-A2 genes in fetal lung explant culture.". Biochim. Biophys. Acta 1398 (2): 192–202. doi:10.1016/S0167-4781(98)00047-5. PMID 9689918. 
  • Saitoh H, Okayama H, Shimura S, Fushimi T, Masuda T, Shirato K (1998). "Surfactant protein A2 gene expression by human airway submucosal gland cells.". Am. J. Respir. Cell Mol. Biol. 19 (2): 202–9. doi:10.1165/ajrcmb.19.2.3239. PMID 9698591. 
  • Goss KL, Kumar AR, Snyder JM (1998). "SP-A2 gene expression in human fetal lung airways.". Am. J. Respir. Cell Mol. Biol. 19 (4): 613–21. doi:10.1165/ajrcmb.19.4.3155. PMID 9761758. 
  • Dias Neto E, Correa RG, Verjovski-Almeida S, Briones MR, Nagai MA, da Silva W Jr, Zago MA, Bordin S, Costa FF, Goldman GH, Carvalho AF, Matsukuma A, Baia GS, Simpson DH, Brunstein A, de Oliveira PS, Bucher P, Jongeneel CV, O'Hare MJ, Soares F, Brentani RR, Reis LF, de Souza SJ, Simpson AJ (2000). "Shotgun sequencing of the human transcriptome with ORF expressed sequence tags.". Proc. Natl. Acad. Sci. U.S.A. 97 (7): 3491–6. doi:10.1073/pnas.97.7.3491. PMC 16267. PMID 10737800. 
  • Wang G, Phelps DS, Umstead TM, Floros J (2000). "Human SP-A protein variants derived from one or both genes stimulate TNF-alpha production in the THP-1 cell line.". Am. J. Physiol. Lung Cell Mol. Physiol. 278 (5): L946–54. PMID 10781424. 
  • Berg T, Leth-Larsen R, Holmskov U, Højrup P (2001). "Structural characterisation of human proteinosis surfactant protein A.". Biochim. Biophys. Acta 1543 (1): 159–73. doi:10.1016/S0167-4838(00)00184-9. PMID 11087951. 
  • Lin Z, deMello D, Phelps DS, Koltun WA, Page M, Floros J (2002). "Both human SP-A1 and Sp-A2 genes are expressed in small and large intestine.". Pediatric pathology & molecular medicine 20 (5): 367–86. doi:10.3109/15513810109168621. PMID 11552738. 
  • Madan T, Saxena S, Murthy KJ, Muralidhar K, Sarma PU (2003). "Association of polymorphisms in the collagen region of human SP-A1 and SP-A2 genes with pulmonary tuberculosis in Indian population.". Clin. Chem. Lab. Med. 40 (10): 1002–8. doi:10.1515/CCLM.2002.174. PMID 12476938.