Fator de crescimento fibroblástico 10

FGF10
Estruturas disponíveis
PDB	Pesquisa Human UniProt: PDBe RCSB
Lista de códigos id do PDB
	1NUN
Identificadores
Nomes alternativos	FGF10
IDs externos	OMIM: 602115 HomoloGene: 3284 GeneCards: FGF10
Doenças Geneticamente Relacionadas
	cancro da próstata, LADD syndrome
Ontologia genética
Função molecular	• heparin binding; • type 2 fibroblast growth factor receptor binding; • growth factor activity; • GO:0001948, GO:0016582 ligação a proteínas plasmáticas; • fibroblast growth factor receptor binding; • chemoattractant activity; • protein tyrosine kinase activity; • 1-phosphatidylinositol-3-kinase activity; • phosphatidylinositol-4,5-bisphosphate 3-kinase activity;
Componente celular	• extracellular region; • núcleo celular; • cell surface; • GO:0005578 matriz extracelular; • membrana plasmática; • extracellular space; • collagen-containing extracellular matrix;
Processo biológico	• bud outgrowth involved in lung branching; • limb bud formation; • organ growth; • semicircular canal morphogenesis; • embryonic pattern specification; • bud elongation involved in lung branching; • positive regulation of canonical Wnt signaling pathway; • muscle cell fate commitment; • tear secretion; • positive regulation of Ras protein signal transduction; • positive regulation of urothelial cell proliferation; • regulation of branching involved in salivary gland morphogenesis by mesenchymal-epithelial signaling; • limb development; • radial glial cell differentiation; • female genitalia morphogenesis; • mesonephros development; • odontogenesis of dentin-containing tooth; • prostatic bud formation; • blood vessel remodeling; • regulation of saliva secretion; • angiogênese; • establishment of mitotic spindle orientation; • positive regulation of ERK1 and ERK2 cascade; • embryonic digestive tract morphogenesis; • animal organ morphogenesis; • hair follicle morphogenesis; • metanephros development; • lung saccule development; • lung epithelium development; • positive regulation of Notch signaling pathway; • negative regulation of cell population proliferation; • branch elongation involved in salivary gland morphogenesis; • branching involved in salivary gland morphogenesis; • positive regulation of white fat cell proliferation; • bronchiole morphogenesis; • limb morphogenesis; • blood vessel morphogenesis; • lung development; • thymus development; • positive regulation of fibroblast proliferation; • negative regulation of cell differentiation; • ERK1 and ERK2 cascade; • positive regulation of epithelial cell migration; • positive regulation of mitotic cell cycle; • spleen development; • smooth muscle cell differentiation; • GO:0060469, GO:0009371 positive regulation of transcription, DNA-templated; • positive regulation of Wnt signaling pathway; • Harderian gland development; • protein localization to cell surface; • respiratory system development; • epidermis development; • positive regulation of peptidyl-tyrosine phosphorylation; • metanephros morphogenesis; • pancreas development; • mammary gland bud formation; • positive chemotaxis; • mesenchymal-epithelial cell signaling involved in lung development; • positive regulation of hair follicle cell proliferation; • lacrimal gland development; • positive regulation of MAPK cascade; • diferenciação celular; • positive regulation of keratinocyte proliferation; • positive regulation of ATP-dependent activity; • positive regulation of epithelial cell proliferation involved in wound healing; • epithelial cell differentiation; • organ induction; • positive regulation of epithelial cell proliferation; • epidermis morphogenesis; • cicatrização de feridas; • epithelial cell proliferation; • regulation of activin receptor signaling pathway; • positive regulation of DNA replication; • quimiotaxia; • embryonic genitalia morphogenesis; • salivary gland development; • positive regulation of keratinocyte migration; • response to lipopolysaccharide; • thyroid gland development; • keratinocyte proliferation; • semicircular canal fusion; • mammary gland specification; • epithelial cell migration; • white fat cell differentiation; • regulação genética; • lung alveolus development; • branching morphogenesis of an epithelial tube; • embryonic digestive tract development; • lung proximal/distal axis specification; • fibroblast growth factor receptor signaling pathway involved in mammary gland specification; • actin cytoskeleton reorganization; • positive regulation of vascular endothelial growth factor receptor signaling pathway; • pituitary gland development; • response to estradiol; • secretion by lung epithelial cell involved in lung growth; • mesenchymal cell differentiation involved in lung development; • lung morphogenesis; • GO:1904578 response to organic cyclic compound; • somatic stem cell population maintenance; • tissue regeneration; • otic vesicle formation; • epithelial cell proliferation involved in salivary gland morphogenesis; • cell-cell signaling; • male genitalia morphogenesis; • GO:1900404 positive regulation of DNA repair; • salivary gland morphogenesis; • MAPK cascade; • embryonic camera-type eye development; • induction of positive chemotaxis; • urothelial cell proliferation; • animal organ formation; • fibroblast growth factor receptor signaling pathway; • regulation of smoothened signaling pathway; • determination of left/right symmetry; • inner ear morphogenesis; • positive regulation of cell population proliferation; • submandibular salivary gland formation; • type II pneumocyte differentiation; • negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; • digestive tract development; • regulation of epithelial cell proliferation; • epithelial tube branching involved in lung morphogenesis; • positive regulation of lymphocyte proliferation; • GO:0003257, GO:0010735, GO:1901228, GO:1900622, GO:1904488 positive regulation of transcription by RNA polymerase II; • phosphatidylinositol phosphate biosynthetic process; • phosphatidylinositol-3-phosphate biosynthetic process; • peptidyl-tyrosine phosphorylation; • regulation of signaling receptor activity; • positive regulation of protein kinase B signaling; • positive regulation of G1/S transition of mitotic cell cycle;
	Sources:Amigo / QuickGO
Ortólogos
	2255
	n/a
	ENSG00000070193
	n/a
	O15520
	n/a
	NM_004465
	n/a
	NP_004456
	n/a
	Wikidata
Ver/Editar Humano

Fator de crescimento de fibroblastos 10 (FGF10) é uma proteína que em humanos é codificada pelo gene FGF10.^[3]^[4] É um polipeptídeo de 208 aminoácidos.^[5] O gene FGF10 humano é altamente homólogo (95,6%) ao FGF10 de rato, onde foi descoberto pela primeira vez.^[6]

Função

A proteína codificada por este gene é membro da família do fator de crescimento de fibroblastos (FGF). Os membros da família FGF possuem amplas atividades mitogênicas e de sobrevivência celular, e estão envolvidos em uma variedade de processos biológicos, incluindo desenvolvimento embrionário, crescimento celular, morfogênese, reparo tecidual, crescimento tumoral e invasão. O fator de crescimento de fibroblastos 10 é uma molécula de sinalização parácrina observada primeiro no desenvolvimento do broto do membro e na organogênese. O FGF10 inicia o desenvolvimento dos membros e está envolvido na ramificação da morfogênese em múltiplos órgãos, como pulmões, pele, ouvido e glândulas salivares. Durante o desenvolvimento dos membros, Tbx4/Tbx5 estimulam a produção de FGF10 no mesoderma da placa lateral [en], onde criará um sinal FGF epitelial-mesenquimal com FGF8. Este ciclo de feedback positivo aumentará a quantidade de mesênquima, resultando em uma protuberância. Posteriormente, o FGF10 induzirá a formação da crista ectodérmica apical [en] (AER), onde os pés e as mãos serão formados. O desenvolvimento pulmonar utiliza a mesma sinalização epitelial-mesenquimal do FGF10 no mesênquima do intestino anterior com o FGFR2 no epitélio do intestino anterior. A sinalização do FGF10 é necessária para a ramificação epitelial. Portanto, todos os órgãos morfógenos ramificados, como pulmões, pele, ouvido e glândulas salivares, exigiram a expressão constante de FGF10. Esta proteína exibe atividade mitogênica para células epidérmicas queratinizantes, mas essencialmente nenhuma atividade para fibroblastos, o que é semelhante à atividade biológica do FGF7.^[4]

Significado clínico

Mutações sem sentido também podem ocorrer com a ausência de FGF10, como na síndrome LADD e ALSG. No entanto, complicações podem surgir da sinalização do FGF10, como câncer de pâncreas e de mama. Além disso, estudos identificaram variantes próximas ao locus FGF10 como um fator de risco genético para suscetibilidade ao câncer de mama.^[7] Embora este gene também esteja implicado como um fator primário no processo de cicatrização de feridas.^[4] Variantes heterozigóticas de FGF10 e doença pulmonar intersticial infantil (child) ligadas a potenciais resultados letais precoces. Além disso, variantes de FGF10 foram associadas ao reparo epitelial anormal.^[8] A haploinsuficiência de FGF10 demonstrou aumentar o risco de doença pulmonar obstrutiva crônica (DPOC). Indivíduos com haploinsuficiência para FGF10 têm índice de Tiffeneau significativamente reduzido, assemelhando-se à doença pulmonar restritiva e obstrutiva crônica.^[9]

Estudos em animais

Camundongos knockout para FGF10 morrem logo após o nascimento. Os camundongos não apresentaram órgãos em desenvolvimento, como pulmões, glândulas salivares, rins ou membros definitivos, uma vez autopsiados. Estudos do homólogo em camundongos sugeriram que este gene é necessário para a morfogênese epidérmica embrionária, incluindo o desenvolvimento do cérebro, morfogênese pulmonar e início da formação do broto do membro.^[10] Camundongos knockout para FGF também apresentam expansão celular epicárdica prejudicada após lesão cardíaca neonatal, bem como expressão reduzida de marcadores epicárdicos Wt1 e Tbx18, e marcadores mesenquimais como Snai1, Twist1 e Postn.^[11] Camundongos deficientes em FGF10 falham em desenvolver glândulas mamárias normais.^[12] O modelo de cobaia mostrou que o anticorpo monoclonal FGF10 pode diminuir o número de células inflamatórias na derme e seu efeito inibitório sobre as células inflamatórias é semelhante ao do butirato de hidrocortisona.^[13]

Interações

FGF10 demonstrou interagir com heparam sulfato^[14] e receptores Toll-like.^[15]

Referências

↑ «Doenças geneticamente associadas a FGF10 ver/editar referências no wikidata»
↑ «Human PubMed Reference:»
↑ Emoto H, Tagashira S, Mattei MG, Yamasaki M, Hashimoto G, Katsumata T, Negoro T, Nakatsuka M, Birnbaum D, Coulier F, Itoh N (setembro de 1997). «Structure and expression of human fibroblast growth factor-10». The Journal of Biological Chemistry. 272 (37): 23191–23194. PMID 9287324. doi:10.1074/jbc.272.37.23191
↑ ^a ^b ^c «Entrez Gene: FGF10 fibroblast growth factor 10»
↑ Emoto H, Tagashira S, Mattei MG, Yamasaki M, Hashimoto G, Katsumata T, Negoro T, Nakatsuka M, Birnbaum D, Coulier F, Itoh N (setembro de 1997). «Structure and expression of human fibroblast growth factor-10». The Journal of Biological Chemistry (em English). 272 (37): 23191–23194. PMID 9287324. doi:10.1074/jbc.272.37.23191
↑ Lü J, Izvolsky KI, Qian J, Cardoso WV (fevereiro de 2005). «Identification of FGF10 targets in the embryonic lung epithelium during bud morphogenesis». The Journal of Biological Chemistry. 280 (6): 4834–4841. PMID 15556938. doi:10.1074/jbc.M410714200
↑ Rivetti S, Chen C, Chen C, Bellusci S (26 de junho de 2020). «Fgf10/Fgfr2b Signaling in Mammary Gland Development, Homeostasis, and Cancer». Frontiers in Cell and Developmental Biology (em English). 8. 415 páginas. PMC 7333592. PMID 32676501. doi:10.3389/fcell.2020.00415
↑ Schütz K, Schmidt A, Schwerk N, Renz DM, Gerard B, Schaefer E, Antal MC, Peters S, Griese M, Rapp CK, Engels H, Cremer K, Bergmann AK, Schmidt G, Auber B, Kamp JC, Laenger F, von Hardenberg S (novembro de 2023). «Variants in FGF10 cause early onset of severe childhood interstitial lung disease: A detailed description of four affected children». Pediatric Pulmonology. 58 (11): 3095–3105. PMID 37560881. doi:10.1002/ppul.26627
↑ Klar J, Blomstrand P, Brunmark C, Badhai J, Håkansson HF, Brange CS, Bergendal B, Dahl N (outubro de 2011). «Fibroblast growth factor 10 haploinsufficiency causes chronic obstructive pulmonary disease». Journal of Medical Genetics. 48 (10): 705–709. PMID 21742743. doi:10.1136/jmedgenet-2011-100166
↑ Itoh N, Ohta H (maio de 2014). «Fgf10: a paracrine-signaling molecule in development, disease, and regenerative medicine». Current Molecular Medicine. 14 (4): 504–509. PMID 24730525. doi:10.2174/1566524014666140414204829
↑ Clayton NS, Grose RP (24 de outubro de 2018). «Emerging Roles of Fibroblast Growth Factor 10 in Cancer». Frontiers in Genetics. 9. 499 páginas. PMC 6207577. PMID 30405704. doi:10.3389/fgene.2018.00499
↑ Mailleux AA, Spencer-Dene B, Dillon C, Ndiaye D, Savona-Baron C, Itoh N, Kato S, Dickson C, Thiery JP, Bellusci S (janeiro de 2002). «Role of FGF10/FGFR2b signaling during mammary gland development in the mouse embryo». Development. 129 (1): 53–60. PMID 11782400. doi:10.1242/dev.129.1.53
↑ Xia JX, Mei XL, Zhu WJ, Li X, Jin XH, Mou Y, Yu K, Wang YY, Li FQ (2014). «Effect of FGF10 monoclonal antibody on psoriasis-like model in guinea pigs». International Journal of Clinical and Experimental Pathology. 7 (5): 2219–2228. PMC 4069920. PMID 24966930
↑ Izvolsky KI, Shoykhet D, Yang Y, Yu Q, Nugent MA, Cardoso WV (junho de 2003). «Heparan sulfate-FGF10 interactions during lung morphogenesis». Developmental Biology. 258 (1): 185–200. PMID 12781692. doi:10.1016/S0012-1606(03)00114-3
↑ Liu L, Song C, Li J, Wang Q, Zhu M, Hu Y, Chen J, Chen C, Zhang JS, Dong N, Chen C (janeiro de 2020). «Fibroblast growth factor 10 alleviates particulate matter-induced lung injury by inhibiting the HMGB1-TLR4 pathway». Aging. 12 (2): 1186–1200. PMC 7053597. PMID 31958320. doi:10.18632/aging.102676

Leitura adicional

Igarashi M, Finch PW, Aaronson SA (maio de 1998). «Characterization of recombinant human fibroblast growth factor (FGF)-10 reveals functional similarities with keratinocyte growth factor (FGF-7)». The Journal of Biological Chemistry. 273 (21): 13230–13235. PMID 9582367. doi:10.1074/jbc.273.21.13230
Sekine K, Ohuchi H, Fujiwara M, Yamasaki M, Yoshizawa T, Sato T, Yagishita N, Matsui D, Koga Y, Itoh N, Kato S (janeiro de 1999). «Fgf10 is essential for limb and lung formation». Nature Genetics. 21 (1): 138–141. PMID 9916808. doi:10.1038/5096
Jimenez PA, Rampy MA (fevereiro de 1999). «Keratinocyte growth factor-2 accelerates wound healing in incisional wounds». The Journal of Surgical Research. 81 (2): 238–242. PMID 9927546. doi:10.1006/jsre.1998.5501
Ropiquet F, Giri D, Kwabi-Addo B, Schmidt K, Ittmann M (setembro de 2000). «FGF-10 is expressed at low levels in the human prostate». The Prostate. 44 (4): 334–338. PMID 10951499. doi:10.1002/1097-0045(20000901)44:4<334::AID-PROS11>3.0.CO;2-G
Marchese C, Felici A, Visco V, Lucania G, Igarashi M, Picardo M, Frati L, Torrisi MR (abril de 2001). «Fibroblast growth factor 10 induces proliferation and differentiation of human primary cultured keratinocytes». The Journal of Investigative Dermatology. 116 (4): 623–628. PMID 11286634. doi:10.1046/j.0022-202x.2001.01280.x
Bagai S, Rubio E, Cheng JF, Sweet R, Thomas R, Fuchs E, Grady R, Mitchell M, Bassuk JA (junho de 2002). «Fibroblast growth factor-10 is a mitogen for urothelial cells». The Journal of Biological Chemistry. 277 (26): 23828–23837. PMID 11923311. doi:10.1074/jbc.M201658200
Yeh BK, Igarashi M, Eliseenkova AV, Plotnikov AN, Sher I, Ron D, Aaronson SA, Mohammadi M (março de 2003). «Structural basis by which alternative splicing confers specificity in fibroblast growth factor receptors». Proceedings of the National Academy of Sciences of the United States of America. 100 (5): 2266–2271. Bibcode:2003PNAS..100.2266Y. PMC 151329. PMID 12591959. doi:10.1073/pnas.0436500100
Upadhyay D, Lecuona E, Comellas A, Kamp DW, Sznajder JI (junho de 2003). «Fibroblast growth factor-10 upregulates Na,K-ATPase via the MAPK pathway». FEBS Letters. 545 (2–3): 173–176. Bibcode:2003FEBSL.545..173U. PMID 12804770. doi:10.1016/S0014-5793(03)00527-1
Izvolsky KI, Zhong L, Wei L, Yu Q, Nugent MA, Cardoso WV (outubro de 2003). «Heparan sulfates expressed in the distal lung are required for Fgf10 binding to the epithelium and for airway branching». American Journal of Physiology. Lung Cellular and Molecular Physiology. 285 (4): L838–L846. PMID 12818887. doi:10.1152/ajplung.00081.2003
Tomlinson DC, Grindley JC, Thomson AA (abril de 2004). «Regulation of Fgf10 gene expression in the prostate: identification of transforming growth factor-beta1 and promoter elements». Endocrinology. 145 (4): 1988–1995. PMID 14726452. doi:10.1210/en.2003-0842
Upadhyay D, Bundesmann M, Panduri V, Correa-Meyer E, Kamp DW (julho de 2004). «Fibroblast growth factor-10 attenuates H2O2-induced alveolar epithelial cell DNA damage: role of MAPK activation and DNA repair». American Journal of Respiratory Cell and Molecular Biology. 31 (1): 107–113. PMID 14975937. doi:10.1165/rcmb.2003-0064OC
Theodorou V, Boer M, Weigelt B, Jonkers J, van der Valk M, Hilkens J (agosto de 2004). «Fgf10 is an oncogene activated by MMTV insertional mutagenesis in mouse mammary tumors and overexpressed in a subset of human breast carcinomas». Oncogene. 23 (36): 6047–6055. PMID 15208658. doi:10.1038/sj.onc.1207816
Ibrahimi OA, Yeh BK, Eliseenkova AV, Zhang F, Olsen SK, Igarashi M, Aaronson SA, Linhardt RJ, Mohammadi M (janeiro de 2005). «Analysis of mutations in fibroblast growth factor (FGF) and a pathogenic mutation in FGF receptor (FGFR) provides direct evidence for the symmetric two-end model for FGFR dimerization». Molecular and Cellular Biology. 25 (2): 671–684. PMC 543411. PMID 15632068. doi:10.1128/MCB.25.2.671-684.2005
Entesarian M, Matsson H, Klar J, Bergendal B, Olson L, Arakaki R, Hayashi Y, Ohuchi H, Falahat B, Bolstad AI, Jonsson R, Wahren-Herlenius M, Dahl N (fevereiro de 2005). «Mutations in the gene encoding fibroblast growth factor 10 are associated with aplasia of lacrimal and salivary glands». Nature Genetics. 37 (2): 125–127. PMID 15654336. doi:10.1038/ng1507
Kovacs D, Falchi M, Cardinali G, Raffa S, Carducci M, Cota C, Amantea A, Torrisi MR, Picardo M (fevereiro de 2005). «Immunohistochemical analysis of keratinocyte growth factor and fibroblast growth factor 10 expression in psoriasis». Experimental Dermatology. 14 (2): 130–137. PMID 15679583. doi:10.1111/j.0906-6705.2005.00261.x
Ye F, Duvillié B, Scharfmann R (fevereiro de 2005). «Fibroblast growth factors 7 and 10 are expressed in the human embryonic pancreatic mesenchyme and promote the proliferation of embryonic pancreatic epithelial cells». Diabetologia. 48 (2): 277–281. PMID 15690149. doi:10.1007/s00125-004-1638-6
Beer HD, Bittner M, Niklaus G, Munding C, Max N, Goppelt A, Werner S (agosto de 2005). «The fibroblast growth factor binding protein is a novel interaction partner of FGF-7, FGF-10 and FGF-22 and regulates FGF activity: implications for epithelial repair». Oncogene. 24 (34): 5269–5277. PMID 15806171. doi:10.1038/sj.onc.1208560

Ligações externas

Entrada OMIM sobre aplasia das glândulas lacrimais e salivares

[1] «Doenças geneticamente associadas a FGF10 ver/editar referências no wikidata»

[2] «Human PubMed Reference:»

[pmid9287324-3] Emoto H, Tagashira S, Mattei MG, Yamasaki M, Hashimoto G, Katsumata T, Negoro T, Nakatsuka M, Birnbaum D, Coulier F, Itoh N (setembro de 1997). «Structure and expression of human fibroblast growth factor-10». The Journal of Biological Chemistry. 272 (37): 23191–23194. PMID 9287324. doi:10.1074/jbc.272.37.23191

[entrez-4] «Entrez Gene: FGF10 fibroblast growth factor 10»

[5] Emoto H, Tagashira S, Mattei MG, Yamasaki M, Hashimoto G, Katsumata T, Negoro T, Nakatsuka M, Birnbaum D, Coulier F, Itoh N (setembro de 1997). «Structure and expression of human fibroblast growth factor-10». The Journal of Biological Chemistry (em English). 272 (37): 23191–23194. PMID 9287324. doi:10.1074/jbc.272.37.23191

[6] Lü J, Izvolsky KI, Qian J, Cardoso WV (fevereiro de 2005). «Identification of FGF10 targets in the embryonic lung epithelium during bud morphogenesis». The Journal of Biological Chemistry. 280 (6): 4834–4841. PMID 15556938. doi:10.1074/jbc.M410714200

[7] Rivetti S, Chen C, Chen C, Bellusci S (26 de junho de 2020). «Fgf10/Fgfr2b Signaling in Mammary Gland Development, Homeostasis, and Cancer». Frontiers in Cell and Developmental Biology (em English). 8. 415 páginas. PMC 7333592. PMID 32676501. doi:10.3389/fcell.2020.00415

[8] Schütz K, Schmidt A, Schwerk N, Renz DM, Gerard B, Schaefer E, Antal MC, Peters S, Griese M, Rapp CK, Engels H, Cremer K, Bergmann AK, Schmidt G, Auber B, Kamp JC, Laenger F, von Hardenberg S (novembro de 2023). «Variants in FGF10 cause early onset of severe childhood interstitial lung disease: A detailed description of four affected children». Pediatric Pulmonology. 58 (11): 3095–3105. PMID 37560881. doi:10.1002/ppul.26627

[9] Klar J, Blomstrand P, Brunmark C, Badhai J, Håkansson HF, Brange CS, Bergendal B, Dahl N (outubro de 2011). «Fibroblast growth factor 10 haploinsufficiency causes chronic obstructive pulmonary disease». Journal of Medical Genetics. 48 (10): 705–709. PMID 21742743. doi:10.1136/jmedgenet-2011-100166

[Itoh_2014-10] Itoh N, Ohta H (maio de 2014). «Fgf10: a paracrine-signaling molecule in development, disease, and regenerative medicine». Current Molecular Medicine. 14 (4): 504–509. PMID 24730525. doi:10.2174/1566524014666140414204829

[11] Clayton NS, Grose RP (24 de outubro de 2018). «Emerging Roles of Fibroblast Growth Factor 10 in Cancer». Frontiers in Genetics. 9. 499 páginas. PMC 6207577. PMID 30405704. doi:10.3389/fgene.2018.00499

[12] Mailleux AA, Spencer-Dene B, Dillon C, Ndiaye D, Savona-Baron C, Itoh N, Kato S, Dickson C, Thiery JP, Bellusci S (janeiro de 2002). «Role of FGF10/FGFR2b signaling during mammary gland development in the mouse embryo». Development. 129 (1): 53–60. PMID 11782400. doi:10.1242/dev.129.1.53

[13] Xia JX, Mei XL, Zhu WJ, Li X, Jin XH, Mou Y, Yu K, Wang YY, Li FQ (2014). «Effect of FGF10 monoclonal antibody on psoriasis-like model in guinea pigs». International Journal of Clinical and Experimental Pathology. 7 (5): 2219–2228. PMC 4069920. PMID 24966930

[14] Izvolsky KI, Shoykhet D, Yang Y, Yu Q, Nugent MA, Cardoso WV (junho de 2003). «Heparan sulfate-FGF10 interactions during lung morphogenesis». Developmental Biology. 258 (1): 185–200. PMID 12781692. doi:10.1016/S0012-1606(03)00114-3

[15] Liu L, Song C, Li J, Wang Q, Zhu M, Hu Y, Chen J, Chen C, Zhang JS, Dong N, Chen C (janeiro de 2020). «Fibroblast growth factor 10 alleviates particulate matter-induced lung injury by inhibiting the HMGB1-TLR4 pathway». Aging. 12 (2): 1186–1200. PMC 7053597. PMID 31958320. doi:10.18632/aging.102676

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