Heparin-binding EGF-like growth factor

Heparin-binding EGF-like growth factor
Heparin-binding EGF-like growth factor

PDB rendering based on 1xdt.
Identifiers
Symbols HBEGF; DTR; DTS; DTSF; HEGFL
External IDs OMIM126150 MGI96070 HomoloGene1466 GeneCards: HBEGF Gene
RNA expression pattern
PBB GE HBEGF 38037 at tn.png
PBB GE HBEGF 203821 at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 1839 15200
Ensembl ENSG00000113070 ENSMUSG00000024486
UniProt Q99075 Q5FW64
RefSeq (mRNA) NM_001945.2 NM_010415.2
RefSeq (protein) NP_001936.1 NP_034545.1
Location (UCSC) Chr 5:
139.71 – 139.73 Mb
Chr 18:
36.66 – 36.68 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]

Contents

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

  1. ^ 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. 
  2. ^ 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. PMC 125525. PMID 11432822. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=125525. 
  3. ^ 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. PMC 2173632. PMID 14597771. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2173632. 
  4. ^ 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. 
  5. ^ 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. 

Further reading

  • 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. PMC 2199889. PMID 7532176. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2199889. 
  • 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. PMC 1169725. PMID 9135143. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1169725. 
  • 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. 

External links



Wikimedia Foundation. 2010.

Игры ⚽ Нужен реферат?

Look at other dictionaries:

  • Epidermal growth factor — or EGF is a growth factor that plays an important role in the regulation of cell growth, proliferation, and differentiation by binding to its receptor EGFR. Human EGF is a 6045 Da protein with 53 amino acid residues and three intramolecular… …   Wikipedia

  • Fibroblast growth factor receptor 1 — PDB rendering based on 1agw …   Wikipedia

  • Fibroblast growth factor receptor 2 — PDB rendering based on 1djs …   Wikipedia

  • NRD1 — Nardilysin (N arginine dibasic convertase) Identifiers Symbols NRD1; hNRD1; hNRD2 External IDs …   Wikipedia

  • ERBB4 — V erb a erythroblastic leukemia viral oncogene homolog 4 (avian) PDB rendering based on 2ahx …   Wikipedia

  • ADAM9 — ADAM metallopeptidase domain 9 (meltrin gamma), also known as ADAM9, is a human gene.cite web | title = Entrez Gene: ADAM9 ADAM metallopeptidase domain 9 (meltrin gamma)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene Cmd=ShowDetailView… …   Wikipedia

  • LTBP3 — Latent transforming growth factor beta binding protein 3, also known as LTBP3, is a human gene.cite web | title = Entrez Gene: LTBP3 latent transforming growth factor beta binding protein 3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene… …   Wikipedia

  • CD82 (gene) — CD82 (Cluster of Differentiation 82) is a human protein encoded by the gene|CD82 gene.cite web | title = Entrez Gene: CD82 CD82 molecule| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene Cmd=ShowDetailView TermToSearch=3732| accessdate = ]… …   Wikipedia

  • Diphtheria — Classification and external resources Diphtheria causes a characteristic swollen neck, sometimes referred to as “bull neck”. ICD 10 A …   Wikipedia

  • Toxine diphterique — Toxine diphtérique La toxine diphtérique est une exotoxine produite par le Corynebacterium diphtheriae, responsable de la diphtérie. Cette maladie fut la plus grande cause de mortalité infantile vers la fin du XIXe siècle et fut aussi la… …   Wikipédia en Français

Share the article and excerpts

Direct link
Do a right-click on the link above
and select “Copy Link”