Heparin-binding EGF-like growth factor: Information from Answers.com

edit

Heparin-binding EGF-like growth factor

PDB rendering based on 1xdt.

Available structures

1xdt

Identifiers

Symbols

HBEGF; DTR; DTS; DTSF; HEGFL

External IDs

OMIM: 126150 MGI: 96070 HomoloGene: 1466

Gene ontology
Molecular function	• receptor activity • epidermal growth factor receptor binding • growth factor activity • heparin binding
Cellular component	• extracellular space • integral to plasma membrane • cell surface • membrane
Biological process	• signal transduction • epidermal growth factor receptor signaling pathway • muscle development • regulation of heart contraction • wound healing, spreading of epidermal cells • positive regulation of smooth muscle cell proliferation • positive regulation of keratinocyte migration

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq

NM_001945 (mRNA)

NM_010415 (mRNA)

NP_001936 (protein)

NP_034545 (protein)

Location

Chr 5:
139.69 - 139.71 Mb

Chr 18:
36.63 - 36.64 Mb

PubMed search

[1]

[2]

Heparin-binding EGF-like growth factor (HB-EGF) is a member of the EGF family of proteins. It has been shown to play a role in wound healing, cardiac hypertrophy and heart development and function.^[1]

1 Interactions
2 References
3 Further reading
4 External links

Interactions

Heparin-binding EGF-like growth factor has been shown to interact with NRD1,^[2] Zinc finger and BTB domain-containing protein 16^[3]^[4] and BAG1.^[5]

References

^ Nanba D. and Higashiyama S. (2004). "Dual intracellular signaling by proteolytic cleavage of membrane-anchored heparin-binding EGF-like growth factor". Cytokine Growth Factor Rev. 15 (1): 13–19. doi:10.1016/j.cytogfr.2003.10.002. PMID 14746810.
^ Nishi, E; Prat A, Hospital V, Elenius K, Klagsbrun M (Jul. 2001). "N-arginine dibasic convertase is a specific receptor for heparin-binding EGF-like growth factor that mediates cell migration". EMBO J. (England) 20 (13): 3342–50. doi:10.1093/emboj/20.13.3342. ISSN 0261-4189. PMID 11432822.
^ Nanba, Daisuke; Mammoto Akiko, Hashimoto Koji, Higashiyama Shigeki (Nov. 2003). "Proteolytic release of the carboxy-terminal fragment of proHB-EGF causes nuclear export of PLZF". J. Cell Biol. (United States) 163 (3): 489–502. doi:10.1083/jcb.200303017. ISSN 0021-9525. PMID 14597771.
^ Nanba, Daisuke; Toki Fujio, Higashiyama Shigeki (Jul. 2004). "Roles of charged amino acid residues in the cytoplasmic domain of proHB-EGF". Biochem. Biophys. Res. Commun. (United States) 320 (2): 376–82. doi:10.1016/j.bbrc.2004.05.176. ISSN 0006-291X. PMID 15219838.
^ Lin, J; Hutchinson L, Gaston S M, Raab G, Freeman M R (Aug. 2001). "BAG-1 is a novel cytoplasmic binding partner of the membrane form of heparin-binding EGF-like growth factor: a unique role for proHB-EGF in cell survival regulation". J. Biol. Chem. (United States) 276 (32): 30127–32. doi:10.1074/jbc.M010237200. ISSN 0021-9258. PMID 11340068.

Higashiyama S, Lau K, Besner GE, et al. (1992). "Structure of heparin-binding EGF-like growth factor. Multiple forms, primary structure, and glycosylation of the mature protein.". J. Biol. Chem. 267 (9): 6205–12. PMID 1556128.
Yoshizumi M, Kourembanas S, Temizer DH, et al. (1992). "Tumor necrosis factor increases transcription of the heparin-binding epidermal growth factor-like growth factor gene in vascular endothelial cells.". J. Biol. Chem. 267 (14): 9467–9. PMID 1577791.
Higashiyama S, Abraham JA, Miller J, et al. (1991). "A heparin-binding growth factor secreted by macrophage-like cells that is related to EGF.". Science 251 (4996): 936–9. doi:10.1126/science.1840698. PMID 1840698.
Iwamoto R, Senoh H, Okada Y, et al. (1991). "An antibody that inhibits the binding of diphtheria toxin to cells revealed the association of a 27-kDa membrane protein with the diphtheria toxin receptor.". J. Biol. Chem. 266 (30): 20463–9. PMID 1939101.
Hayes H, Kaneda Y, Uchida T, Okada Y (1988). "Regional assignment of the gene for diphtheria toxin sensitivity using subchromosomal fragments in microcell hybrids.". Chromosoma 96 (1): 26–32. doi:10.1007/BF00285879. PMID 3436221.
Bennett KL, Jackson DG, Simon JC, et al. (1995). "CD44 isoforms containing exon V3 are responsible for the presentation of heparin-binding growth factor.". J. Cell Biol. 128 (4): 687–98. doi:10.1083/jcb.128.4.687. PMID 7532176.
Pathak BG, Gilbert DJ, Harrison CA, et al. (1995). "Mouse chromosomal location of three EGF receptor ligands: amphiregulin (Areg), betacellulin (Btc), and heparin-binding EGF (Hegfl).". Genomics 28 (1): 116–8. doi:10.1006/geno.1995.1116. PMID 7590736.
Mitamura T, Higashiyama S, Taniguchi N, et al. (1995). "Diphtheria toxin binds to the epidermal growth factor (EGF)-like domain of human heparin-binding EGF-like growth factor/diphtheria toxin receptor and inhibits specifically its mitogenic activity.". J. Biol. Chem. 270 (3): 1015–9. doi:10.1074/jbc.270.3.1015. PMID 7836353.
Hashimoto K, Higashiyama S, Asada H, et al. (1994). "Heparin-binding epidermal growth factor-like growth factor is an autocrine growth factor for human keratinocytes.". J. Biol. Chem. 269 (31): 20060–6. PMID 8051092.
Kobrin MS, Funatomi H, Friess H, et al. (1994). "Induction and expression of heparin-binding EGF-like growth factor in human pancreatic cancer.". Biochem. Biophys. Res. Commun. 202 (3): 1705–9. doi:10.1006/bbrc.1994.2131. PMID 8060360.
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.
Thompson SA, Higashiyama S, Wood K, et al. (1994). "Characterization of sequences within heparin-binding EGF-like growth factor that mediate interaction with heparin.". J. Biol. Chem. 269 (4): 2541–9. PMID 8300582.
Fen Z, Dhadly MS, Yoshizumi M, et al. (1993). "Structural organization and chromosomal assignment of the gene encoding the human heparin-binding epidermal growth factor-like growth factor/diphtheria toxin receptor.". Biochemistry 32 (31): 7932–8. doi:10.1021/bi00082a014. PMID 8347598.
Elenius K, Paul S, Allison G, et al. (1997). "Activation of HER4 by heparin-binding EGF-like growth factor stimulates chemotaxis but not proliferation.". EMBO J. 16 (6): 1268–78. doi:10.1093/emboj/16.6.1268. PMID 9135143.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (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.
Louie GV, Yang W, Bowman ME, Choe S (1998). "Crystal structure of the complex of diphtheria toxin with an extracellular fragment of its receptor.". Mol. Cell 1 (1): 67–78. doi:10.1016/S1097-2765(00)80008-8. PMID 9659904.
Borer JG, Park JM, Atala A, et al. (1999). "Heparin-binding EGF-like growth factor expression increases selectively in bladder smooth muscle in response to lower urinary tract obstruction.". Lab. Invest. 79 (11): 1335–45. PMID 10576204.
Nakamura K, Mitamura T, Takahashi T, et al. (2000). "Importance of the major extracellular domain of CD9 and the epidermal growth factor (EGF)-like domain of heparin-binding EGF-like growth factor for up-regulation of binding and activity.". J. Biol. Chem. 275 (24): 18284–90. doi:10.1074/jbc.M907971199. PMID 10749879.
Duque JL, Adam RM, Mullen JS, et al. (2001). "Heparin-binding epidermal growth factor-like growth factor is an autocrine mediator of human prostate stromal cell growth in vitro.". J. Urol. 165 (1): 284–8. doi:10.1097/00005392-200101000-00080. PMID 11125426.
Lin J, Hutchinson L, Gaston SM, et al. (2001). "BAG-1 is a novel cytoplasmic binding partner of the membrane form of heparin-binding EGF-like growth factor: a unique role for proHB-EGF in cell survival regulation.". J. Biol. Chem. 276 (32): 30127–32. doi:10.1074/jbc.M010237200. PMID 11340068.

PDB Gallery

1xdt: COMPLEX OF DIPHTHERIA TOXIN AND HEPARIN-BINDING EPIDERMAL GROWTH FACTOR

External links

MeSH heparin-binding+EGF-like+growth+factor

This article on a gene on chromosome 5 is a stub. You can help Wikipedia by expanding it.

This cell biology article is a stub. You can help Wikipedia by expanding it.

v • d • e Growth factors

Fibroblast	FGF receptor ligands: FGF1/FGF2/FGF5 · FGF3/FGF4/FGF6 · KGF (FGF7/FGF10/FGF22) · FGF8/FGF17/FGF18 · FGF9/FGF16/FGF20 FGF homologous factors: FGF11 · FGF12 · FGF13 · FGF14 hormone-like: FGF19 · FGF21 · FGF23

EGF-like domain	TGFα · EGF · HB-EGF

TGFβ pathway	TGF-β (TGF-β1, TGF-β2, TGF-β3)

Insulin-like	IGF-1 · IGF-1

Platelet-derived	PDGFA · PDGFB · PDGFC · PDGFD

Vascular endothelial	VEGF-A · VEGF-B · VEGF-C · VEGF-D · PGF

Other	Nerve · Hepatocyte

see also growth factor receptors

This entry is from Wikipedia, the leading user-contributed encyclopedia. It may not have been reviewed by professional editors (see full disclaimer)

Donate to Wikimedia

	What are important human growth factors? Read answer...
	What are factors affect growth of trees? Read answer...
	What are the factors affecting urban growth? Read answer...

	Which of the following most likely would be an immediate result of growth factor binding to its receptor?
	Describe how a transcription factor would work where would it bind what would it do when it binds there what do specific factors like the TATA binding protein do?
	What factor most likely led to the formation and growth of the Grange Movement?

Heparin-binding EGF-like growth factor

Contents

Interactions

References

Further reading

External links