Publication for SFTPC and SFTPA2

Species	Symbol	Function*	Entrez Gene ID*	Other ID	Gene coexpression	CoexViewer
hsa	SFTPC	surfactant protein C	6440			[link]
hsa	SFTPA2	surfactant protein A2	729238

Pubmed ID	Priority	Text
30333828	0.98	SFTPA2 (4), SFTPB (4), SFTPC (2), and SFTPD (2)), and identified SP SNP associations by applying quantitative genetic principles.
	0.98	SFTPA2 (n = 1; Figure 1A), SFTPC (n = 2), and SFTPD (n = 2; Figure 1B).
	0.97	SFTPA2, SFTPB, SFTPC, and/or SFTPD, are associated with CF or disease severity subgroups (mild and moderate/severe) through single genetic variations within a gene, and through intragenic or intergenic interactions between variants of a single gene or variants of two different genes.
	0.97	SP-C variants play a critical differential role in pulmonary CF and that functions imparted by SP-A1/SP-A2 and SP-D variants further enhance the CF disease progression.
	0.97	SFTPA2 SNP rs1059046 appears to stand out from the other SFTPA2 SNPs studied, as this SNP (1) is associated with CF via five of the total nine interactions observed with the other SP genes, (2) is the only SNP that shows interactions with two SFTPA1 SNPs, and (3) shows interactions with both hydrophobic surfactant proteins SFTPB and SFTPC (Figure 1A).
	0.97	SFTPC) to be individually associated with CF; b) Three intragenic interactions (2 of SFTPA1 and one of SFTPB) to associate with CF; c) A total of 34 intergenic interactions of different combinations between the various genes studied, except between SFTPD and SFTPA1 or SFTPA2, to associate with CF; A summary of all the significant intragenic and intergenic interactions is shown in Supplementary Table 3, and Figure 2.
	0.96	SFTPC SNPs studied, rs4715 and rs1124, are associated with CF through 18 intergenic SNP-SNP interactions with SNPs in SFTPA1, SFTPA2, SFTPC, and SFTPD (X2 is 2.2285-8.4508, p = 0.0487-0.0007) (Table 4).
	0.96	SFTPA2 (n = 2), SFTPB (n = 3), and SFTPC (n = 8) (X2 is 2.2285-7.8947, p = 0.0487-0.0007) (Table 4, Figure 1A).
	0.96	SFTPC encoding the hydrophobic surfactant proteins, and only two interactions are with SFTPA2 that encodes the hydrophilic surfactant protein A2 (Figure 1A), whereas no interactions are observed with SFTPD.
	0.94	SP-A2) the structural organization of surfactant, indicating that SP-A1 and SP-C may cooperatively affect surfactant structure, which in turn may affect surfactant function and lung function.
	0.93	SFTPA2 (n = 2), SFTPC (n = 1), and SFTPD (n = 2).
	0.93	SFTPA2, SFTPB, SFTPC, and SFTPD to CF and disease severity subgroups by genetic association analysis of single SNP and intragenic and intergenic SNP-SNP interactions.
	0.92	SFTPC encoding the other hydrophobic surfactant protein, whereas 14 interactions are with genes encoding the hydrophilic surfactant proteins, seven are with SFTPA (3 for SFTPA1 and 4 for SFTPA2) (Figure 1A) and seven with SFTPD (Figure 1B).
	0.90	SFTPC, but as noted above no interactions were observed with SFTPA1 or SFTPA2.
	0.90	SFTPC also has 14 intergenic interactions, eight with SFTPA1, three with SFTPA2 and only 3 with SFTPD.
	0.89	SFTPA2 encoding the hydrophilic surfactant proteins, SP-A1 and SP-A2 and on the right SNPs of the surfactant genes SFTPB and SFTPC, encoding the hydrophobic proteins, SP-B and SP-C, are shown (B).
	0.88	SFTPC SNP-SNP interactions, only 4 are with SFTPB the gene that encodes the other hydrophobic surfactant protein, whereas 14 interactions are with genes encoding the hydrophilic surfactant proteins (8 for SFTPA1, 3 for SFTPA2, and 3 for SFTPD).
	0.84	SFTPC (X2 is 2.2285-8.4508, p = 0.0487-0.0007); 13 interactions for SFTPA1 (X2 is 2.2285-7.8947, p = 0.0487-0.0007), 9 interactions for SFTPA2 (X2 is 2.4172-6.4974, p = 0.0485-0.0038), and 10 interactions for SFTPD (X2 is 2.2285-8.4508, p = 0.0487-0.0007).
	0.82	SFTPC with CF by single SNP, and intragenic and intergenic SNP-SNP interactions between SFTPB and SFTPC, and with SFTPA1 and SFTPA2.
	0.77	SFTPA2, SFTPB, SFTPC, and SFTPD With Cystic Fibrosis
	0.69	SFTPA2, one SNP in SFTPC, and one SNP in SFTPD.
	0.68	SFTPA2 gene is associated with CF through 9 intergenic SNP-SNP interactions with SFTPA1 (n = 2), SFTPB (n = 4), and SFTPC (n = 3) (X2 is 2.4172-6.4974, p = 0.0485-0.0038, Figure 1A).
	0.59	SP-C) are primarily involved in surface properties of surfactant and are important for normal lung function; the hydrophilic proteins (SP-A1, SP-A2, and SP-D) are primarily involved in host defense, although SP-A1 and SP-A2 exhibit differential effects on the surfactant structural reorganization, on the organization of phospholipid monolayers containing SP-B, and lung mechanics.
	0.57	SFTPC exhibited significant SNP-SNP interactions with SFTPA1/SFTPA2 (n = 11), SFTPB (n = 4) and SFTPD (n = 3).
24996423	0.98	pspA and pspC mutants to the stress hormone showed them to have a central involvement in the catecholamine response mechanism.
	0.97	pspA, pspC, and pspA and pspC mutants, but to our surprise binding of Tf was no less than that of the wildtype (data not shown).
	0.97	pspA and pspC mutants.
	0.96	pspA (pspA-), pspC (pspC-) and pspAC (pspAC-) mutant uptake of Tf-complexed Fe (in the form of 55Fe) +/-
	0.96	pspA and pspC mutants, grown in serum-medium in the presence and absence of added NE.
	0.95	pspA and pspC appeared to be non-NE responsive in the growth context, we also investigated if these proteins were in some way involved in the inotrope uptake.
	0.95	pspA and pspC mutants to the stress hormone showed them to have a central involvement in the catecholamine response mechanism.
	0.93	PspA and PspC in the response mechanism.
	0.92	pspA and pspC double mutant showed similar uptake levels to the single pspC mutant.
	0.92	pspA or pspC abolished NE responsiveness, reduced NE uptake and blocked catecholamine-induced gene responsiveness.
	0.92	PspA and PspC relay NE mediated messages.
	0.91	pspA, pspC and pspAC mutants in serum-medium in the absence (black line) or presence of 10 muM NE (red line).
	0.91	pspA and pspC appears to have blocked NE-induced elevations in expression of many of the genes which in wild type D39 showed a NE-induced increase.
	0.90	PspA and PspC in pneumococcal catecholamine responsiveness.
	0.89	pspA and pspC single mutants the effects of NE exposure on the expression of 14 functionally diverse genes involved in pneumococcal metabolism and virulence in order to identify genes involved in stress hormone responsiveness of S. pneumoniae.
	0.89	PspA and PspC have been shown to elicit protective antibody response against invasive pneumococcal infection, hence they are considered to be promising vaccine candidates.
	0.86	PspA and PspC are involved in stress hormone mediated effects in S. pneumoniae given these proteins are coded by paralogous genes, and previous studies have demonstrated their involvement in similar biological events.
	0.84	pspA and pspC are involved in pneumococcal catecholamine inotrope responsiveness
	0.81	PspA and PspC should be so important in mediating catecholamine responsiveness in the pneumococcus is unclear.
	0.78	pspA and pspC mutants.
	0.73	pspA and pspC mutants, singly or in combination, showed no significant growth induction by the catecholamine.
	0.68	PspA and a strain mutated in pspA, it was shown that PspA, but not PspC, is responsible for pneumococcal binding to human lactoferrin, which was suggested to be important to overcome the iron limitation at mucosal surfaces.
18166586	0.98	PspA, PspC, serine protease, IgA1 protease, and histidine triad proteins SP1003, SP1004, SP1174, SP1175, NanA, LytC, and LytA :with high frequency (Table I).
	0.98	PspA and PspC, which have been described previously as highly immunogenic antigens, were selected in all 12 screens performed.
	0.98	PspA, SP0641, SP1175, PspC, and PcsB; Fig. 3).
	0.98	PspA and PspC, were strongly positive, confirming the validity of this analysis.
	0.98	PspA and PspC, and four novel antigens, SP0368, SP0667, StkP, and PcsB. The functions of SP0368, a choline-binding protein, and SP0667, pneumococcal surface protein, have not been revealed yet.
	0.98	PspA and PspC are highly variable, which is thought to be a result of immune pressure.
	0.97	PspA and PspC as well as the highly toxic nature of pneumolysin limit their use as vaccine candidates.
	0.96	PspA, PspC, and pneumolysin.
	0.96	PspA and PspC) and 4 novel ones (SP0368, SP0667, StkP, and PcsB), whereas the other antigens, such as SP0082, were clearly negative in these experiments (Fig. 4 A; and Fig. S1 A, available at http://www.jem.org/cgi/content/full/jem.20071168/DC1).
	0.93	PspA and PspC, the known protective pneumococcal antigens were excluded from this preselection.
	0.83	PspA, SP0368, SP0454, SP0609, SP0749, SP1891, SP2108, PspC, and PcsB. An additional 10 novel conserved candidates were selected for animal testing in spite of the lack of positive FACS data, as this could be attributed to insufficient epitope-specific antibodies in hyperimmune mouse sera or a lack of in vitro expression.
	0.82	PspA, PspC, and histidine triad proteins.
	0.67	PspA, PspC, and PcsB were the most frequently selected antigens in the genomic library screens.
	0.52	PspA and PspC, as well as of SP0368 and SP0667 (unpublished data), would necessitate several clade variants to be included in a broad coverage vaccine.
22815690	0.98	SP-A2, SP-C, and SP-D, respectively, correlated significantly and positively with each other (p>0.95, p<0.001 in all comparisons).
	0.97	SP-A2, SP-B, SP-C and SP-D in isolated adult human primary AEC-II.
	0.97	SP-A2 and SP-C mRNA expression remain constant (Figure 2).
	0.97	SP-A2, SP-B, SP-C and SP-D mRNA expression level of human AEC-II (freshly isolated or cultured for 24 h) were measured by real-time PCR.
	0.96	SP-C and SP-D mRNA was found highest compared with SP-B, SP-A2 and SP-A1.
	0.96	SP-C and SP-D still showed a significant and positive correlation (p = 0.9, p<0.0001), whereas the correlation of SP-A1 and SP-A2 decreased (p = 0.6, p<0.01) and no further correlation could be observed.
	0.87	SP-A2; SP-B; SP-C and SP-D mRNA were measured by real-time PCR after culture.
	0.82	SP-A2 and SP-C remained stable.
30592459	0.98	PspA, 6.00 for PspC) than the average number of such domains across all variants on the array (6.97 for PspA, 6.17 for PspC).
	0.98	PspA and PspC (Figure 5).
	0.98	PspA and PspC, attached to cell wall polysaccharide through choline-binding domains, and ZmpA, covalently attached to the cell wall via sortase activity.
	0.97	PspC and ZmpB proteins, whereas PspA- and ZmpA-induced antibodies recognised a broader set of alleles.
	0.97	PspA, PspC, ZmpA and ZmpB were excluded.
	0.97	PspA, as this PspC allele is not closely related to the WCV PspA. Hence this may represent a relatively poor immune response to PspC, owing to its weakened association with the cell surface following the loss of some of its CBDs, that triggers recognition of a specific epitope unique to variant 42.
	0.96	PspA) and C (PspC), and the zinc metalloproteases A (ZmpA) and B (ZmpB).
	0.96	pspA and pspC. The array contained no variant highly similar to RM200's PspA or PspC sequences.
29152081	0.98	SFTPA2, SFPTA1, CHIPA2, SFTPC and RPL13AP17 were 0.9760, 0.9558, 0.9641, 0.9564, 0.9972 and 0.9803 respectively (Figure 3B; Table 1).
	0.97	SFTPA2, SFPTA1, CHIPA2, SFTPC and RPL13AP17 were 0.9749, 0.9525, 0.9715, 0.9519, 0.9988 and 0.9673 respectively in the test group.
	0.97	SFTPA2, SFTPA1, CHIPA2, SFTPC, and RPL13AP17 were 0.9749, 0.9525, 0.9715, 0.9519, 0.9988 and 0.9673 in the test group (n=267).
	0.95	SFTPA2, SFTPA1, CHIPA2, SFTPC, and RPL13AP17 were 0.9760, 0.9558, 0.9641, 0.9564, 0.9972 and 0.9803 in the validate group (n=268).
	0.94	SFTPA2, SFTPA1, CHIPA2, SFTPC, and RPL13AP17) with high diagnostic power in LUAD across 27 types of cancer
	0.93	SFTPA2 and SFTPC, surfactant genes which have been reported to express exclusively in type II penumocytes, have showed their unique roles in LUAD.
23117565	0.98	SP-A and pro SP-C) on EpCAMhi/T1alpha- cells sorted from COPD or non-COPD lungs.
	0.97	SP-A or pro-SP-C-positive cells in the EpCAMhi/T1alpha- cells isolated from COPD (n=3) or non-COPD lungs (n=3).
	0.94	SP-A+ or pro-SP-C+ cells in the EpCAMhi/T1alpha- cells sorted from COPD or non-COPD lungs (figure 1B and C).
	0.88	SP-A, surfactant protein-A; pro-SP-C, pro-surfactant protein-C.
22853774	0.98	SFTPC, SFTPA2, TERT,TERC).
	0.96	surfactant protein C (SFTPC) and in surfactant protein A2 (SFTPA2) have also been indentified in familial IIP patients, but these genes appear to be infrequently mutated in familial and sporadic cohorts, with the exception of the Dutch cohort reported in 2010.
	0.88	SFTPC, SFTPA2, TERC and TERT.
24391588	0.98	SFTPC (encoding surfactant protein C), SFTPA2 (encoding surfactant protein A2), MUC5B (encoding a mucin constituent of the mucus), as well as TERT and TERC (encoding components of the telomerase complex) to be associated with pulmonary fibrosis (Nogee et al.,; Thomas et al.,; Armanios et al.,; Tsakiri et al.,; Wang et al.,; van Moorsel et al.,; Ono et al.,; Seibold et al.,).
	0.97	SFTPA2, SFTPC, MUC5B as well as DSP (encoding desmoplakin) as risk factors for pulmonary fibrosis suggest that the integrity of the barrier function is critically important in maintaining lung homeostasis (Fingerlin et al.,).
25621661	0.98	SFTPA2 likely disrupt normal routing and processing of the protein, supporting the concept that, like mutations in SFTPC, SP-A-related disease results from misfolding of the protein in alveolar type II epithelial cells.
	0.96	SFTPC, and SFTPA2 account for only 15-20% of familial IPF cases, indicating novel genes are involved that have not yet been identified.
19390477	0.98	SP-A plus human SP-C surfactant treatment of preterm lambs with ventilation-induced lung injury stimulated acute neutrophil influx into the lung.
25506193	0.98	SFTPC, SFTPA2, and telomerase genes TERT and TERC.
29657097	0.98	SFTPA2, SFTPB, SFTPC, and SFTPD) along with other AEC2-selective transcripts that encode lamellar body genes, including NAPSA and PGC (Figures 6D and 6E; Table S4).
25553246	0.97	SFTPC, SFTPA2 and TERT occur in patients with sporadic and familial IPF.
	0.94	SFTPA2, SFTPC and TERT are collectively over-represented in individuals with IPF.
	0.94	surfactant protein A2 (SFTPA2, Gene ID 729238), surfactant protein C (SFTPC, Gene ID 6440) and the ATP-binding cassette member A3 (ABCA3, Gene ID 21).
	0.82	SFTPA2, SFTPC and TERT.
	0.78	SFTPA2 (n=1), SFTPC (n=5), ABCA3 (n=4) and TERT (n=5)).
	0.69	SFTPA2, SFTPC, (surfactant proteins) and TERT (telomerase) were found in individuals with idiopathic pulmonary fibrosis (IPF) but not those with chronic obstructive pulmonary disease.
	0.65	SFTPA2), and C (SFTPC), the ATP binding cassette member A3 (ABCA3), telomerase (TERT), thyroid transcription factor (NKX2-1) and mucin 5B (MUC5B) and compared the collapsed frequencies of rare (minor allele frequency <1%), computationally predicted deleterious variants in each cohort.
	0.63	SFTPC (p.T138N and p.S186N) and SFTPA2 (p.A91P) were present in similar frequencies in the IPF and COPD cohorts compared to the general population, as were the common synonymous variants in ABCA3 (p.F353F, p.P585P and p.S1372S) (see online supplementary table S1).
	0.53	SFTPA2, SFTPC or TERT.
23749296	0.97	PspA, anti-PspC, anti-PcpA, and anti-PLY levels.
	0.97	PspA, PspC, and PcpA) and intracytoplasmic pneumococcal antigen (PLY), given the reported protective effect of these antibodies against pneumococcal infections or colonization.
	0.96	pneumococcal surface protein A (PspA), pneumococcal surface protein C (PspC), pneumococcal choline-binding protein A (PcpA), and pneumolysin (PLY) were measured by ELISA assays.
	0.95	PspA, anti-PspC, anti-PcpA, and anti-PLY antibody levels between asthmatics and non-asthmatics.
	0.95	PspA inhibits classical pathway complement activation, while PspC binds human factor H and thereby inhibits the alternative (amplification) complement pathway.
	0.94	PspA, anti-PcpA, anti-PspC, and anti-PLY, between individuals with and without asthma.
	0.78	PspA anti-PcpA levels, however, a significant inverse correlation was noted between IL-5 secretion by PBMC cultured with SEB at day 7 and anti-PspC antibody levels (r= -0.53, p=0.003).
	0.59	PspA, PspC, PcpA, and PLY.
25629011	0.97	PspC formed less structured, more antibiotic-sensitive biofilms, whereas pneumococci lacking PspA that is not associated with early colonization showed normal biofilm formation (Marks et al.,).
	0.97	PspC- and PspA-negative mutant, that when colonized alone was rapidly cleared.
	0.94	PspC- and PspA-negative strain (TRE121; erythromycin-resistant and tetracycline resistant) to investigate whether the pspC locus required for colonization (Balachandran et al.,) could be repaired if grown in the presence of the wild-type strain.
26893575	0.97	surfactant protein C, SFTPC; surfactant protein A2, SFTPA2; and ATP-binding cassette member A3, ABCA3) were detected to concentrate in FPF.
	0.97	SP-C, together with SP-A, SP-B, and SP-D, constitutes 10% of the protein components of pulmonary surfactant in humans, and the remaining 90% is lipids.
30042329	0.97	SFTPC and SFTPA2, telomerase genes are also expressed by extrapulmonary cells, especially stem cells.
	0.92	SFTPC and SFTPA2, respectively).
24349316	0.97	PspA, PspC) have been identified as being involved in the inhibition of complement deposition on the surface of S. pneumoniae.
28540997	0.97	SP-A, SP-B, SP-C, and SP-D. Two hydrophilic proteins, SP-A and SP-D, involve surfactant synthesis and release, anti-inflammatory action, and immunologic response.
24324223	0.96	pspC and pspA failed to amplify for one isolate.
	0.93	pspA and pspC were detected.
	0.91	PspA, PspC is also a candidate for a protein-based pneumococcal vaccine.
	0.71	pspA alleles and pspC polymorphisms.
30841014	0.96	Surfactant protein C (SPC) and surfactant protein A2 (SPA2) are exclusively synthesized by type II AECs.
	0.94	SPC and SPA mutations have been shown to cause incorrect protein folding and processing, thereby activating the cells' endoplasmic reticulum (ER) stress response.
21741354	0.96	SP-C) but lack the hydrophilic surfactant proteins, including SP-A, which is also important in reducing inhibition.
29804726	0.96	surfactant protein A2 [SFTPA2], surfactant protein C [SFTPC] and adenosine triphosphate-binding cassette subfamily A member 3 [ABCA3]) among others, but also telomere biology-associated genes such TERT, TERC, RTEL1, TINF2 and PARN.
30854216	0.95	SFTPA2, and SFTPC; ABCA3 (ATP-binding cassette - type 3); genes related to telomerases, including TERT, and TERC; DKC1 (dyskeratin); TINF2; or RTEL1.
	0.81	SFTPC, SFTPA2, TERT, and TERC clarify a maximum of 20% of all FIP cases.
21514128	0.95	PspA, and choline binding protein (Cbp) (also referred to as PspC) (see table 1).
26167183	0.95	SPA, SPB, SPC, and SPD), and phospholipids.
16356236	0.94	SP-A, SP-B, SP-C and SP-D, play an important role in surfactant homeostasis and protection against inhibition by plasma proteins or serum.
25278226	0.94	SFTPA2, SFTPB, SFTPC, and SFTPD remain unchanged with respect to insulin treatment (Figure 1).
21613931	0.93	surfactant protein C (SFTPC), surfactant protein A2 (SFTPA2), telomerase reverse transcriptase (TERT), and telomerase RNA component (TERC).
	0.92	SFTPC, SFTPA2, TERT, and TERC likely account for only 15-20% of all cases of FIP.
	0.77	SFTPC and SFTPA2 mutations, recent reports have linked mutations in genes for the two key components of the telomerase complex, TERC and TERT.
	0.53	SFTPC and SFTPA2 mutations suggest that type II AECs are the cell population that is central to the initiation and progression of disease.
	0.51	surfactant protein C (SFTPC), surfactant protein A2 (SFTPA2), telomerase RNA component (TERC),; and telomerase reverse transcriptase (TERT).; A fifth gene, ELMOD2, whose role remains largely undefined, has been associated with FIP by a linkage study in a report from Finland.
26886749	0.93	spa types and harboured similar resistance genes including blaZ, tet(M) and spc with 2/3 isolates also harbouring erm(C) and exhibiting ciprofloxacin resistance (Table 1).
21613930	0.92	SFTPC and SFTPA2 suggest the possibility that aberrant surfactant protein processing could be a primary abnormality in IPF.; Some of these SFTPC mutations have been shown to induce endoplasmic reticulum (ER) stress, which can induce apoptosis of AECs.;; The search for inciting events in IPF is an important area of investigation since identification of these processes holds much promise for better defining the pathogenesis of disease.
24730976	0.92	SFTPA2, SFTPC and genes encoding for telomerase components (TERT, TERC) accounts for approximately 22% of these cases.
31309122	0.91	SPC and SPA2 have been described in association with FIP and rarely with sporadic IPF.
24009156	0.89	pneumococcal surface protein A (PspA) and pneumococcal choline-binding protein C (PspC).
	0.85	pneumococcal surface protein A (PspA), pneumococcal choline-binding protein A (PcpA), and pneumococcal surface protein C (PspC).
28965766	0.88	SFTPC, SFTPA1, SFTPA2, and NAPSA expression in the otherwise similar Tom+ versus Tom- cells on day 35 (Figure S5F), we further explored the possibility that Tom+ cells might represent a more mature state of iAEC2s compared with Tom- cells.
	0.85	SFTPC, SFTPB, and ABCA3, and additional AEC2 maturation transcripts, SFTPA1, SFTPA2, NAPSA, pepsinogen C (PGC), SLC34A2, and LAMP3, with only LAMP3 being expressed at a lower level than primary (week 21) human fetal lung alveolar cell controls (Figure 6E; Figure S6).
22018035	0.88	SP-C, SP-A and SP-D. Decreased amounts of this transcription factor during development could result in decreased amounts of these protein products.
31092817	0.85	PspC (CbpA), PspA, and ZmpA. For all of the antigen alleles with enough observations (Supplementary Table 7), we performed an association test against all imputed human variants as above, using a more accurate imputation of the CFH region due to its potential relevance in these interactions.
25837031	0.82	SFTPC, SFTPA2, and telomerase-related genes including TERT, hTR, DKC1 and RTEL1 is available from commercial and academic sources.
23919474	0.77	SP-A, SP-B, SP-C and SP-D. Surfactant proteins SP-B and SP-C are critically important hydrophobic proteins responsible for surfactant adsorption and helping to attain low surface tension.
	0.74	SP-C surfactant was more resistant to inhibition than the modified natural surfactants but less resistant than natural lavage surfactant containing SP-A. This may indicate that recombinant hydrophobic surfactant proteins or synthetic analogs of these proteins can be used for the design of new surfactant formulations that are comparatively resistant to inactivation and therefore suitable for ARDS treatment.
23075428	0.75	SFTPC and SFTPA2 are individually very rare, but have a large effect in the kindreds in which they are found.
23798474	0.75	SP-A, SP-B, SP-C, and ABCA3, all cause epithelial cell dysfunction and/or surfactant deficiency that underlie epithelial cell injury, inflammation and remodeling that are associated with respiratory failure and ILD in children and adults.
27799632	0.57	SFTPA2 and SFTPC) have been associated with adult-onset pulmonary fibrosis.