HGNC Approved Gene Symbol: FGF10
SNOMEDCT: 22589009, 715656004; ICD9CM: 750.21;
Cytogenetic location: 5p12 Genomic coordinates (GRCh38): 5:44,300,247-44,389,420 (from NCBI)
| Location | Phenotype |
Phenotype MIM number |
Inheritance |
Phenotype mapping key |
|---|---|---|---|---|
| 5p12 | Aplasia of lacrimal and salivary glands | 180920 | Autosomal dominant | 3 |
| LADD syndrome 3 | 620193 | Autosomal dominant | 3 |
Emoto et al. (1997) isolated a cDNA encoding a novel member of the human fibroblast growth factor family from lung. The cDNA encodes a protein of 208 amino acids with high sequence identity (95.6%) to rat FGF10, suggesting that the protein is human FGF10. Both the human and rat FGF10 have a hydrophobic N terminus of approximately 40 amino acids, which may serve as a signal sequence. Evolutionary relationships of human FGFs indicated that FGF10 is closest to FGF7 (148180); in both structure and biologic activity, FGF10 is similar to FGF7. Recombinant human FGF10, of approximately 19 kD, showed mitogenic activity for fetal rat keratinizing epidermal cells, but essentially no activity for NIH 3T3 fibroblasts.
Bagai et al. (2002) cloned FGF10 by PCR of a urinary bladder cDNA library. The deduced protein contains 2 putative N-glycosylation sites, a heparin binding domain, and several putative phosphorylation sites. In situ hybridization demonstrated expression of FGF10 in fibroblasts of the lamina propria.
Bagai et al. (2002) determined that FGF10 contains 3 exons and spans at least 52.7 kb.
By radioactive in situ hybridization, Emoto et al. (1997) mapped the FGF10 gene to 5p13-p12. By FISH, Bagai et al. (2002) also mapped the FGF10 gene to chromosome 5p13-p12.
Using in situ hybridization and immunohistochemistry, Suzuki et al. (2000) detected expression of Fgf10 in the developing epidermis (17.5 dpc) and hair follicles (16.5-18.5 dpc and 11 days after birth) of normal mice.
Bagai et al. (2002) determined that recombinant FGF10 induced proliferation of human urothelial cells in vitro and induced proliferation of transitional epithelium of wildtype and Fgf7-null mice in vivo. Mechanistic studies with human cells indicated that FGF10 translocated into urothelial cell nuclei and initiated a signaling cascade that began with the heparin-dependent tyrosine phosphorylation of surface transmembrane receptors. Quiescent normal urothelial cells expressed negligible levels of FGF10. During proliferation, levels of FGF10 rose at the urothelial cell surface and/or within urothelial cell nuclei.
Sakaue et al. (2002) determined that Fgf10 is secreted by cultured mouse preadipocytes. Prevention of Fgf10 signaling inhibited the expression of C/EBP-beta (189965) and subsequent differentiation. In Fgf10-knockout mice, the expression of C/EBP-beta was reduced, and the ability of embryonic fibroblasts derived from Fgf10-knockout mice to differentiate into adipocytes was impaired.
Using clustering of synaptic vesicles in cultured neurons as an assay, Umemori et al. (2004) purified putative target-derived presynaptic organizing molecules from mouse brain and identified Fgf22 (605831) as a major active species. Fgf7 and Fgf10, the closest relatives of Fgf22, shared this activity; other Fgfs had distinct effects. Neutralization of Fgf7, Fgf10, and Fgf22 inhibited presynaptic differentiation of mossy fibers at sites of contact with granule cells in vivo. Inactivation of Fgfr2 (176943) had similar effects. These results indicated that FGF22 and its relatives are presynaptic organizing molecules in the mammalian brain.
Gros and Tabin (2014) showed that mesenchymal limb progenitors arise through localized epithelial-to-mesenchymal transition (EMT) of the coelomic epithelium specifically within the presumptive limb fields. This EMT is regulated at least in part by TBX5 (601620) and FGF10, 2 genes known to control limb initiation. Gros and Tabin (2014) showed that limb buds initiate earlier than had been thought, as a result of localized EMT rather than differential proliferation rates.
Reviews
In their review, Frenz et al. (2010) noted that there is a critical period when development of the inner ear is dependent upon signaling through retinoic acid and its receptors (see 180240). They presented a model whereby either over- or underavailability of retinoic acid disrupts FGF3 (164950) and FGF10 activation, leading to altered expression of the downstream target genes DLX5 (600028) and DLX6 (600030) and defects in inner ear development.
Aplasia of Lacrimal and Salivary Glands
Aplasia of lacrimal and salivary glands (ALSG; 180920) is a rare condition characterized by irritable eyes and dryness of the mouth (xerostomia). In affected individuals, the misdiagnosis is often made of the more prevalent disorder Sjogren syndrome (270150), an autoimmune condition characterized by keratoconjunctivitis sicca and xerostomia. Entesarian et al. (2005) studied 2 extended Swedish families with ALSG in a total of 16 individuals. Thirteen of the individuals had absence of 1 or more lacrimal puncta. The segregation pattern suggested full penetrance. A genomewide screen showed linkage of ALSG to 5p13.2-q13.1. DNA sequence analysis identified a heterozygous 53-kb deletion in the FGF10 gene (602115.0002), including exons 2 and 3, and without the involvement of any flanking genes, in affected members of 1 family and a heterozygous arg193-to-ter substitution (R193X; 602115.0001), resulting in a truncated protein, in each of the 4 affected members of the other family. Both mutations were consistent with the idea that haploinsufficiency for FGF10 underlies ALSG. To clarify whether FGF10 mutations cause dry eyes and dry mouth in sporadic cases with symptoms identical to those in individuals with ALSG, Entesarian et al. (2005) screened DNA samples from 74 individuals diagnosed with dry eyes and/or dry mouth but without fulfilling the criteria for Sjogren syndrome for mutations in FGF10. No sequence alterations in the coding region of FGF10 were found in samples from these individuals. Entesarian et al. (2005) concluded that mutations in FGF10 appeared to be uncommon in individuals with nonspecific sicca syndromes.
Lacrimoauriculodentodigital Syndrome 3
Lacrimoauriculodentodigital (LADD) syndrome-3 (620193) is a multiple congenital anomaly mainly affecting lacrimal glands and ducts, salivary glands and ducts, ears, teeth, and distal limb segments. In a father and his 3 children with LADD, Rohmann et al. (2006) detected a 317G-T mutation in exon 1 of the FGF10 gene (602115.0003). Rohmann et al. (2006) also found LADD disease-causing mutations in the FGFR2 gene (176943) and the FGFR3 gene (134934). They noted that FGF10 is an FGFR ligand.
Milunsky et al. (2006) identified a heterozygous nonsense mutation in the FGF10 gene (602115.0005) in a mother with ALSG and her daughter with LADD syndrome. The findings in this family indicated that ALSG and LADD syndrome are allelic disorders and part of the same phenotypic spectrum. The authors suggested that differences in modifier genes, perhaps including FGFR2, may explain the less severe ALSG phenotype in the mother versus the LADD syndrome phenotype in her daughter.
In a 3-generation family segregating LADD syndrome, Zhang et al. (2023) identified a heterozygous frameshift mutation in the FGF10 gene (602115.0008); the variant was present in 6 affected family members and 2 unaffected members, indicating incomplete penetrance.
Associations Pending Confirmation
Klar et al. (2011) analyzed pulmonary function in 12 patients from the 2 Swedish ALSG families originally studied by Entesarian et al. (2005), and found that the FGF10-haploinsufficient patients exhibited nonreversible airway obstruction consistent with moderate or stage II chronic obstructive pulmonary disease (COPD; see 606963). Klar et al. (2011) concluded that FGF10 haploinsufficiency affects lung function measures, and proposed that genetic variants affecting the FGF10 signaling pathway are important determinants of lung function that may contribute to COPD.
Karolak et al. (2019) studied a cohort of 26 deceased patients who had clinically and histopathologically diagnosed interstitial neonatal lung disorders: acinar dysplasia in 14 patients, congenital alveolar dysplasia in 2, and other lethal lung hypoplasias in 10. The authors identified rare copy number variants or deletions involving TBX4 (601719) (8 and 2, respectively) or FGF10 (2 and 2, respectively) in 16 (61%) of the 26 patients. Individuals with lung hypoplasia also harbored at least one noncoding single-nucleotide variant in the predicted lung-specific enhancer region. One of the patients (P042) with lung hypoplasia (265430) reported by Karolak et al. (2019) was compound heterozygous for the R193X mutation in the FGF10 gene (602115.0001) previously reported in patients with ALSG and a mutation (Q3415H) in the FRAS1 gene (607830). The infant was born at term and developed severe respiratory distress that did not improve with oscillatory ventilation, nitric oxide, or surfactant. Echocardiogram showed pulmonary hypertension. She died at 10 hours of age. Autopsy showed lung hypoplasia, apparent arrest of pulmonary maturation at the late canalicular stage. No extra-pulmonary features were noted. She had 2 healthy sibs and no family history. No functional studies were reported.
On the basis of its spatiotemporal expression pattern in the developing embryo, the FGF10 gene is predicted to function as a regulator of brain, lung, and limb development. To define the role of the Fgf10 gene, Sekine et al. (1999) generated Fgf10-deficient mice. Homozygous-deficient mice died at birth due to the lack of lung development. Trachea was formed, but subsequent pulmonary branching morphology was disrupted. In addition, mutant mice had complete truncation of the fore- and hindlimbs. In the homozygous-deficient embryos, limb bud formation was initiated, but outgrowth of the limb buds did not occur; however, formation of the clavicles was not affected. Analysis of the expression of marker genes in the mutant limb buds indicated that the apical ectodermal ridge (AER) and the zone of polarizing activity (ZPA) did not form. Thus, Sekine et al. (1999) showed that Fgf10 serves as an essential regulator of lung and limb formation. Hogan (1999) reviewed the function of mouse Fgf10 in lung morphogenesis.
Min et al. (1998) generated Fgf10-deficient mice by targeted disruption. Limb bud initiation was abolished in Fgf10 -/- mice. Strikingly, Fgf10 -/- fetuses continued to develop until birth, despite the complete absence of both fore- and hindlimbs. Fgf10 is necessary for AER formation and acts epistatically upstream of Fgf8 (600483), the earliest known AER marker in mice. Fgf10 -/- mice exhibited perinatal lethality associated with complete absence of lungs. Although tracheal development was normal, mainstem bronchial formation, as well as all subsequent pulmonary branching morphogenesis, was completely disrupted. The pulmonary phenotype of Fgf10 -/- mice is strikingly similar to that of the Drosophila mutant branchless (602465), an Fgf homolog.
In Fgf10 -/- mice, Suzuki et al. (2000) detected abnormalities in epidermal morphogenesis including a decrease in proliferating cells, a hypoplastic granular layer, and a lack of distinctive keratohyaline granules and tonofibrils. There was also a reduction of loricrin (152445) expression in skin. Because Fgf10-deficient mice die soon after birth, Suzuki et al. (2000) transplanted fetal skin onto nude mice to demonstrate that hair development can occur normally in Fgf10-deficient skin. The authors concluded that Fgf10 is required for embryonic epidermal morphogenesis, but is not essential for hair follicle development.
Kelly et al. (2001) analyzed a transgenic mouse line in which a LacZ reporter gene had integrated upstream of the Fgf10 gene. They detected transgene expression in the embryonic right ventricle and outflow tract of the heart and in contiguous splanchnic and pharyngeal mesoderm. After Dil labeling of cultured mouse embryos, they proposed that the embryonic heart is derived from 2 myocardial precursor cell populations: 1 which gives rise to the early heart tube and inflow region and 1, expressing Fgf10, in pharyngeal mesoderm which gives rise to the outflow tract and possibly also the embryonic right ventricle. Kelly et al. (2001) concluded that Fgf10-expressing cells in pharyngeal mesoderm give rise to the arterial pole of the mouse heart.
In Fgf10 -/-, Fgf receptor-2b -/-, and Sonic hedgehog (SHH; 600725) -/- mice, which all exhibit cleft palate, Rice et al. (2004) showed that Shh is a downstream target of Fgf10/Fgfr2b signaling. Using BrdU staining, they demonstrated that mesenchymal Fgf10 regulates the epithelial expression of Shh, which in turn signals back to the mesenchyme. This was confirmed by the finding that cell proliferation was decreased not only in the palatal epithelium but also in the mesenchyme of Fgfr2b -/- mice. Rice et al. (2004) concluded that coordinated epithelial-mesenchymal interactions are essential during the initial stages of palate development and require an FGF-SHH signaling network.
After finding mutations in the FGF10 gene in human cases of aplasia of lacrimal salivary glands, Entesarian et al. (2005) reexamined Fgf10 +/- mice. These mice were found also to have aplasia of lacrimal glands and hypoplasia of salivary glands. Other internal organs, including lung, liver, spleen, heart, stomach, thyroid, pancreas, intestines, and ovaries, were macroscopically normal.
During organogenesis, the foregut endoderm gives rise to the many different cell types that comprise the hepatopancreatic system, including hepatic, pancreatic, and gallbladder cells, as well as the epithelial cells of the hepatopancreatic ductal system that connects these organs together and with the intestine. In a study of the mechanisms responsible for demarcating ducts versus organs, Dong et al. (2007) showed that Fgf10 signaling from the adjacent mesenchyme is responsible for refining the boundaries between the hepatopancreatic duct and organs. In zebrafish fgf10 mutants, the hepatopancreatic ductal epithelium was severely dysmorphic, and cells of the hepatopancreatic ductal system and adjacent intestine misdifferentiated toward hepatic and pancreatic fates. Furthermore, Fgf10 functions to prevent the differentiation of the proximal pancreas and liver into hepatic and pancreatic cells, respectively. These data shed light onto how the multipotent cells of the foregut endoderm, and subsequently those of the hepatopancreatic duct, are directed toward different organ fates.
In zebrafish, mechanosensory organs called neuromasts are deposited at regular intervals by the migrating posterior lateral line (pLL) primordium. The pLL primordium is organized into polarized rosettes representing protoneuromasts, each with a central atoh1a-positive focus of mechanosensory precursors. Nechiporuk and Raible (2008) showed that rosettes form cyclically from a progenitor pool at the leading zone of the primordium as neuromasts are deposited from the trailing region. Fgf3 (164950) and Fgf10 signals localized to the leading zone are required for rosette formation, atoh1a expression, and primordium migration. Nechiporuk and Raible (2008) proposed that the fibroblast growth factor source controls primordium organization, which, in turn, regulates the periodicity of neuromast deposition.
Watanabe et al. (2010) generated compound Fgf8 and Fgf10 mutant mice in the cardiac and pharyngeal mesoderm. They found that pharyngeal arch artery (PAA) development was perturbed by Fgf8 deletion. The frequency and severity of PAA and outflow tract (OFT) defects increased with decreasing expression of Fgf8 and Fgf10. Watanabe et al. (2010) concluded that there is functional overlap of mesodermal FGF8 and FGF10 during second heart field/OFT and PAA development, and that FGF10 has a role in formation of the arterial pole of the heart. The findings indicated that the sensitivity of these processes is influenced by incremental reductions in FGF levels.
In 4 affected members spanning 3 successive generations of a Swedish family with aplasia of lacrimal and salivary glands (ALSG; 180920), Entesarian et al. (2005) identified a heterozygous 577C-T transition in exon 3 of the FGF10 gene, resulting in an arg193-to-ter (R193X) substitution and a truncated protein.
In 12 affected members, including 6 different sibships, spanning 4 generations of a Swedish family with aplasia of lacrimal and salivary glands (ALSG; 180920), Entesarian et al. (2005) identified a 53-kb deletion in the FGF10 gene that included exons 2 and 3 and did not involve any flanking genes.
In a family of Turkish extraction with LADD syndrome (LADD3; 620193), Rohmann et al. (2006) identified a 317G-T transversion in exon 1 of the FGF10 gene that resulted in a cys106-to-phe (C106F) substitution. Heterozygous loss-of-function mutations in FGF10 caused by a nonsense mutation and gene deletion had been shown by Entesarian et al. (2005) to cause lacrimal system and salivary gland aplasia in humans and in heterozygous Fgf10 +/- knockout mice. In contrast, the FGF10 mutation identified by Rohmann et al. (2006) was a missense mutation. Rohmann et al. (2006) considered it plausible that the effect of this missense mutation is different from the loss-of-function mutations described in isolated anomalies of the lacrimal system and salivary glands and that a dominant-negative effect of C106F might explain why this mutation affected additional organs in the LADD syndrome.
In a girl with LADD syndrome (LADD3; 620193), Milunsky et al. (2006) identified a heterozygous de novo 467T-G transversion in exon 3 of the FGF10 gene, resulting in an ile156-to-arg (I156R) substitution in the middle of 1 of the sites for the interaction between FGF10 and the b isoform of FGFR2 (176943). The mutation was not detected in either parent or in 500 control chromosomes.
In a mother with aplasia of lacrimal and salivary glands (ALSG; 180920) and her daughter with LADD syndrome (LADD3; 620193), Milunsky et al. (2006) identified a heterozygous 409A-T transversion in exon 2 of the FGF10 gene, resulting in a lys137-to-ter (K137X) substitution. The mutation was predicted to result in a truncated protein with a loss of 73 amino acids, eliminating 1 of the sites for the interaction between FGF10 and the b isoform of FGFR2 (176943). The mutation was not identified in 200 control chromosomes. The findings in this family indicated that ALSG and LADD syndrome are allelic disorders. The authors suggested that differences in modifier genes, perhaps including FGFR2, may explain the less severe ALSG phenotype in the mother versus the LADD syndrome phenotype in her daughter.
In a 3-year-old Caucasian boy with aplasia of lacrimal and salivary glands (ALSG; 180920), Entesarian et al. (2007) identified a heterozygous 240A-C transversion in exon 1 of the FGF10 gene, predicted to result in an arg80-to-ser (R80S) substitution at a highly conserved residue. The patient's father, who had absent tears, dry mouth, difficulty swallowing, and extensive caries, was also heterozygous for the mutation. The unaffected mother did not have the mutation, which was not found in 308 control chromosomes. The patient and his mother both carried another heterozygous change, a 620A-C transversion in exon 3 of FGF10, predicted to cause a his207-to-pro (H207P) substitution at a nonconserved residue and presumed to be a rare polymorphism, as it was not found in 330 control chromosomes.
In a 4-year-old Caucasian boy with aplasia of lacrimal and salivary glands (ALSG; 180920), Entesarian et al. (2007) identified a de novo heterozygous 413G-A transition in exon 2 of the FGF10 gene, resulting in a gly138-to-glu (G138E) substitution at a highly conserved residue. The mutation was not found in either of the patient's unaffected parents or in 296 control chromosomes. The patient had coronal hypospadias but no other urogenital abnormalities; his hearing was normal, and he had no anomalies of the digits, ears, or primary teeth.
In a multigenerational Chinese family segregating LADD syndrome (LADD3; 620193), Zhang et al. (2023) identified heterozygosity for a duplication of cytosine at nucleotide 234 (c.234dupC, NM_004465.1) in the FGF10 gene, resulting in a trp79-to-leu substitution with a frameshift downstream (Trp79LeufsTer15). The variation was detected in 6 affected family members and 2 unaffected members (the proband's mother and maternal aunt), indicating incomplete penetrance. The mutation was identified by whole-exome sequencing and confirmed by Sanger sequencing. The mutation was expected to cause protein truncation or mRNA degradation through nonsense-mediated mRNA decay.
Bagai, S., Rubio, E., Cheng, J.-F., Sweet, R., Thomas, R., Fuchs, E., Grady, R., Mitchell, M., Bassuk, J. A. Fibroblast growth factor-10 is a mitogen for urothelial cells. J. Biol. Chem. 277: 23828-23837, 2002. [PubMed: 11923311] [Full Text: https://doi.org/10.1074/jbc.M201658200]
Dong, P. D. S., Munson, C. A., Norton, W., Crosnier, C., Pan, X., Gong, Z., Neumann, C. J., Stainier, D. Y. R. Fgf10 regulates hepatopancreatic ductal system patterning and differentiation. Nature Genet. 39: 397-402, 2007. [PubMed: 17259985] [Full Text: https://doi.org/10.1038/ng1961]
Emoto, H., Tagashira, S., Mattei, M.-G., Yamasaki, M., Hashimoto, G., Katsumata, T., Negoro, T., Nakatsuka, M., Birnbaum, D., Coulier, F., Itoh, N. Structure and expression of human fibroblast growth factor-10. J. Biol. Chem. 272: 23191-23194, 1997. [PubMed: 9287324] [Full Text: https://doi.org/10.1074/jbc.272.37.23191]
Entesarian, M., Dahlqvist, J., Shashi, V., Stanley, C. S., Falahat, B., Reardon, W., Dahl, N. FGF10 missense mutations in aplasia of lacrimal and salivary glands (ALSG). Europ. J. Hum. Genet. 15: 379-382, 2007. [PubMed: 17213838] [Full Text: https://doi.org/10.1038/sj.ejhg.5201762]
Entesarian, M., Matsson, H., Klar, J., Bergendal, B., Olson, L., Arakaki, R., Hayashi, Y., Ohuchi, H., Falahat, B., Bolstad, A. I., Jonsson, R., Wahren-Herlenius, M., Dahl, N. Mutations in the gene encoding fibroblast growth factor 10 are associated with aplasia of lacrimal and salivary glands. Nature Genet. 37: 125-128, 2005. [PubMed: 15654336] [Full Text: https://doi.org/10.1038/ng1507]
Frenz, D. A., Liu, W., Cvekl, A., Xie, Q., Wassef, L., Quadro, L., Niederreither, K., Maconochie, M., Shanske, A. Retinoid signaling in inner ear development: a 'Goldilocks' phenomenon. Am. J. Med. Genet. 152A: 2947-2961, 2010. [PubMed: 21108385] [Full Text: https://doi.org/10.1002/ajmg.a.33670]
Gros, J., Tabin, C. J. Vertebrate limb bud formation is initiated by localized epithelial-to-mesenchymal transition. Science 343: 1253-1256, 2014. [PubMed: 24626928] [Full Text: https://doi.org/10.1126/science.1248228]
Hogan, B. L. M. Morphogenesis. Cell 96: 225-233, 1999. [PubMed: 9988217] [Full Text: https://doi.org/10.1016/s0092-8674(00)80562-0]
Karolak, J. A., Vincent, M., Deutsch, G., Gambin, T., Cogne, B., Pichon, O., Vetrini, F., Mefford, H. C., Dines, J. N., Golden-Grant, K., Dipple, K., Freed, A. S., and 61 others. Complex compound inheritance of lethal lung developmental disorders due to disruption of the TBX-FGF pathway. Am. J. Hum. Genet. 104: 213-228, 2019. [PubMed: 30639323] [Full Text: https://doi.org/10.1016/j.ajhg.2018.12.010]
Kelly, R. G., Brown, N. A., Buckingham, M. E. The arterial pole of the mouse heart forms from Fgf10-expressing cells in pharyngeal mesoderm. Dev. Cell 1: 435-440, 2001. [PubMed: 11702954] [Full Text: https://doi.org/10.1016/s1534-5807(01)00040-5]
Klar, J., Blomstrand, P., Brunmark, C., Badhai, J., Hakansson, H. F., Brange, C. S., Bergendal, B., Dahl, N. Fibroblast growth factor 10 haploinsufficiency causes chronic obstructive pulmonary disease. J. Med. Genet. 48: 705-709, 2011. [PubMed: 21742743] [Full Text: https://doi.org/10.1136/jmedgenet-2011-100166]
Milunsky, J. M., Zhao, G., Maher, T. A., Colby, R., Everman, D. B. LADD syndrome is caused by FGF10 mutations. Clin. Genet. 69: 349-354, 2006. [PubMed: 16630169] [Full Text: https://doi.org/10.1111/j.1399-0004.2006.00597.x]
Min, H., Danilenko, D. M., Scully, S. A., Bolon, B., Ring, B. D., Tarpley, J. E., DeRose, M., Simonet, W. S. Fgf-10 is required for both limb and lung development and exhibits striking functional similarity to Drosophila branchless. Genes Dev. 12: 3156-3161, 1998. [PubMed: 9784490] [Full Text: https://doi.org/10.1101/gad.12.20.3156]
Nechiporuk, A., Raible, D. W. FGF-dependent mechanosensory organ patterning in zebrafish. Science 320: 1774-1777, 2008. [PubMed: 18583612] [Full Text: https://doi.org/10.1126/science.1156547]
Rice, R., Spencer-Dene, B., Connor, E. C., Gritli-Linde, A., McMahon, A. P., Dickson, C., Thesleff, I., Rice, D. P. C. Disruption of Fgf10/Fgfr2b-coordinated epithelial-mesenchymal interactions causes cleft palate. J. Clin. Invest. 113: 1692-1700, 2004. [PubMed: 15199404] [Full Text: https://doi.org/10.1172/JCI20384]
Rohmann, E., Brunner, H. G., Kayserili, H., Uyguner, O., Nurnberg, G., Lew, E. D., Dobbie, A., Eswarakumar, V. P., Uzumcu, A., Ulubil-Emeroglu, M., Leroy, J. G., Li, Y., and 9 others. Mutations in different components of FGF signaling in LADD syndrome. Nature Genet. 38: 414-417, 2006. Note: Erratum: Nature Genet. 38: 495 only, 2006. [PubMed: 16501574] [Full Text: https://doi.org/10.1038/ng1757]
Sakaue, H., Konishi, M., Ogawa, W., Asaki, T., Mori, T., Yamasaki, M., Takata, M., Ueno, H., Kato, S., Kasuga, M., Itoh, N. Requirement of fibroblast growth factor 10 in development of white adipose tissue. Genes Dev. 16: 908-912, 2002. [PubMed: 11959839] [Full Text: https://doi.org/10.1101/gad.983202]
Sekine, K., Ohuchi, H., Fujiwara, M., Yamasaki, M., Yoshizawa, T., Sato, T., Yagishita, N., Matsui, D., Koga, Y, Itoh, N., Kato, S. Fgf10 is essential for limb and lung formation. Nature Genet. 21: 138-141, 1999. Note: Erratum: Nature Genet. 51: 921 only, 2019. [PubMed: 9916808] [Full Text: https://doi.org/10.1038/5096]
Suzuki, K., Yamanishi, K., Mori, O., Kamikawa, M., Andersen, B., Kato, S., Toyoda, T., Yamada, G. Defective terminal differentiation and hypoplasia of the epidermis in mice lacking the Fgf10 gene. FEBS Lett. 481: 53-56, 2000. [PubMed: 10984614] [Full Text: https://doi.org/10.1016/s0014-5793(00)01968-2]
Umemori, H., Linhoff, M. W., Ornitz, D. M., Sanes, J. R. FGF22 and its close relatives are presynaptic organizing molecules in the mammalian brain. Cell 118: 257-270, 2004. [PubMed: 15260994] [Full Text: https://doi.org/10.1016/j.cell.2004.06.025]
Watanabe, Y., Miyagawa-Tomita, S., Vincent, S. D., Kelly, R. G., Moon, A. M., Buckingham, M. E. Role of mesodermal FGF8 and FGF10 overlaps in the development of the arterial pole of the heart and pharyngeal arch arteries. Circ. Res. 106: 495-503, 2010. [PubMed: 20035084] [Full Text: https://doi.org/10.1161/CIRCRESAHA.109.201665]
Zhang, H. Y., Zhang, C. Y., Wang, F., Tao, H., Tian, Y. P., Zhou, X. B., Bai, F., Wang, P., Cui, J. Y., Zhang, M. J., Wang, L. H. Identification of a novel mutation in the FGF10 gene in a Chinese family with obvious congenital lacrimal duct dysplasia in lacrimo-auriculo-dento-digital syndrome. Int. J. Ophthal. 16: 499-504, 2023. [PubMed: 37077496] [Full Text: https://doi.org/10.18240/ijo.2023.04.02]