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ALKBH1  -  alkB, alkylation repair homolog 1 (E. coli)

Homo sapiens

Synonyms: ABH, ABH1, ALKBH, Alkylated DNA repair protein alkB homolog 1, Alpha-ketoglutarate-dependent dioxygenase ABH1, ...
 
 
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Disease relevance of ALKBH1

  • Using a human challenge model, we showed that 29% of our study population was homozygous recessive for the alpha(1,2)fucosyltransferase gene (FUT2) in the ABH histo-blood group family and did not express the H type-1 oligosaccharide ligand required for Norwalk virus binding [1].
  • Neoexpression of ABH and Lewis blood group antigens in human hepatocellular carcinomas [2].
  • Degradation of blood group antigens in human colon ecosystems. I. In vitro production of ABH blood group-degrading enzymes by enteric bacteria [3].
  • In contrast, none of 16 other fecal Bacteroides, Escherichia coli, Streptococcus faecalis, and Bifidobacterium strains produced ABH blood group-degrading enzymes; other glycosidases produced by these strains were predominantly cell bound except for extracellular beta-N-acetylhexosaminidases produced by the five S. faecalis strains [4].
  • In general, areas affected by carcinoma in situ showed deletion of ABH, as did invasive carcinomas, as demonstrated by other investigators [5].
 

Psychiatry related information on ALKBH1

  • The presence of globo-A and globo-H as the major ABH blood group antigens in undifferentiated NTERA-2 cells suggests that globo-series blood group antigens are embryonic antigens, synthesis of which switches to lacto-series during human development [6].
  • Seven of 14 lesions lacked ABH antigens, the loss of blood group structures could not however be correlated with any specific histological features and was not limited to the loss of A and B substances [7].
 

High impact information on ALKBH1

  • Immunoblotting, monosaccharide composition analysis, and selective glycosidase digestions revealed that the CHIP-associated oligosaccharide contains ABH determinants and resembles a band 3-type glycan that cannot be cleaved from intact membranes by Peptide:N-glycosidase F [8].
  • We show that SGG and DSGG are selectively expressed by epithelial cells of nonsecretors, presumably as a result of sialylation of the gal-globoside precursor glycolipid, which in secretors is fucosylated and processed to ABH antigens [9].
  • Mucin degradation in human colon ecosystems. Isolation and properties of fecal strains that degrade ABH blood group antigens and oligosaccharides from mucin glycoproteins [4].
  • Fibroblasts present in the primary thyroid cultures were invariably negative for ABH antigens [10].
  • This work serves as a foundation for studying the structural and chemical biology of arginase I in the immune response, and we demonstrate the inhibition of arginase activity by ABH in human and murine myeloid cells [11].
 

Chemical compound and disease context of ALKBH1

  • A panel of mouse monoclonal antibodies was used to determine the expression of blood group ABH-related antigens carried by type 1 chain (H, Lea, Leb, ALed, ALeb) and type 2 chain (N-acetyllactosamine, H, Lex, Ley, A/ALey) core structures in biopsies of urothelium from patients with chronic cystitis [12].
  • Biotinylated sarcolectin, neoglycoproteins with lactose or N-acetylglucosamine residues, and polyacrylamide-attached trisaccharides, that represent the ABH histo-blood group antigens, were applied to sections of 187 primary lung carcinomas [13].
  • As to linkage relationships of C3 with marker systems and with myotonic dystrophy, there was evidence (most of it first presented at the 6th International Congress of Human Genetics, Jerusalem 1981) for synteny with ABH secretion (Se): C3-Se (males) z = 4.35, theta = 0.12 and with Lewis secretion (LES): C3-LES (males z = 3.63, theta = 0.04) [14].
  • Adenocarcinomas showed topographical rather than quantitative changes in blood group antigen expression with more extensive luminal expression of ABH, Lewis and Ii structures than that seen in normal glands [15].
  • PCR products of Rhodococcus sp., Nocardioides sp., Gordona sp. and Sphingomonas sp. growing additionally or solely with medium-chain n-alkane as hexadecane had only few sequence identity with alkB though hybridizing with the gene probe [16].
 

Biological context of ALKBH1

  • The hABH gene, which maps to chromosome 14q24, was ubiquitously expressed in 16 human tissues examined [17].
  • The full-length human AlkB homolog (hABH) cDNA clone contains a 924 bp open reading frame encoding a 34 kDa protein which is 52% similar and 23% identical to E.coli AlkB [17].
  • All the H-deficient phenotypes tested were nonsecretors of ABH in their saliva, and one-third were Lewis negative [18].
  • ABH expression undergoes developmental modulation in the human colorectal tract from positive to negative during embryogenesis, and is lost in adult cells [19].
  • Loss of ABH antigen expression in bladder cancer is not caused by loss of heterozygosity of the ABO locus [20].
 

Anatomical context of ALKBH1

 

Associations of ALKBH1 with chemical compounds

  • Strikingly, ABH causes significant enhancement of nonadrenergic, noncholinergic nerve-mediated relaxation of penile corpus cavernosum smooth muscle, suggesting that arginase inhibition sustains L-arginine concentrations for NO synthase activity [23].
  • ABH binds as the tetrahedral boronate anion, with one hydroxyl oxygen symmetrically bridging the binuclear manganese cluster and a second hydroxyl oxygen coordinating to Mn2+A [23].
  • The crystal structure of the complex between the binuclear manganese metalloenzyme arginase and the boronic acid analog of L-arginine, 2(S)-amino-6-boronohexanoic acid (ABH), has been determined at 1.7 A resolution from a crystal perfectly twinned by hemihedry [23].
  • These include isozyme profile, morphology with light and scanning electron microscopes, karyotype, growth rate, DNA content by flow cytometry, presence of cell surface ABH isoantigens, tumorigenicity in nude mice, lactic acid dehydrogenase isozymes, and colony formation in soft agar [24].
  • Human vascular endothelial cells have at their surface the same lactosamine-ended precursor and sialylated chains as pigs, but instead of terminal alpha Gal they express the fucosylated polymorphic ABH histo-blood group epitopes [25].
 

Analytical, diagnostic and therapeutic context of ALKBH1

  • The combination of A9 pattern and ABH blood group antigen expression in tumor tissue was the variable most strongly associated with duration of disease-free survival, even after adjustment for the traditional prognostic factors of tumor site, stage, and TNM classification [26].
  • Using indirect immunofluorescence (IFL) on viable human thyroid cultures, it has been shown that, although adult follicular cells do not express blood group ABH antigens in vivo, they invariably reexpress the corresponding antigens on the cell surface when cultured in monolayers, even for very short periods [10].
  • We studied ABH expression in 166 group A apheresis platelet donors by flow cytometry, Western blotting, and thin layer chromatography relative to donor age, sex, A1/A2 subgroup, and Lewis phenotype [27].
  • Platelets express ABH antigens, which can adversely effect platelet transfusion recovery and survival in ABH-incompatible recipients [27].
  • In contrast, ABH antigens were not detected by immunofluorescence on normal peripheral lymphocytes [28].

References

  1. Human susceptibility and resistance to Norwalk virus infection. Lindesmith, L., Moe, C., Marionneau, S., Ruvoen, N., Jiang, X., Lindblad, L., Stewart, P., LePendu, J., Baric, R. Nat. Med. (2003) [Pubmed]
  2. Neoexpression of ABH and Lewis blood group antigens in human hepatocellular carcinomas. Okada, Y., Arima, T., Togawa, K., Nagashima, H., Jinno, K., Moriwaki, S., Kunitomo, T., Thurin, J., Koprowski, H. J. Natl. Cancer Inst. (1987) [Pubmed]
  3. Degradation of blood group antigens in human colon ecosystems. I. In vitro production of ABH blood group-degrading enzymes by enteric bacteria. Hoskins, L.C., Boulding, E.T. J. Clin. Invest. (1976) [Pubmed]
  4. Mucin degradation in human colon ecosystems. Isolation and properties of fecal strains that degrade ABH blood group antigens and oligosaccharides from mucin glycoproteins. Hoskins, L.C., Agustines, M., McKee, W.B., Boulding, E.T., Kriaris, M., Niedermeyer, G. J. Clin. Invest. (1985) [Pubmed]
  5. Blood group-related antigens in human urothelium: enhanced expression of precursor, LeX, and LeY determinants in urothelial carcinoma. Cordon-Cardo, C., Reuter, V.E., Lloyd, K.O., Sheinfeld, J., Fair, W.R., Old, L.J., Melamed, M.R. Cancer Res. (1988) [Pubmed]
  6. Glycolipid core structure switching from globo- to lacto- and ganglio-series during retinoic acid-induced differentiation of TERA-2-derived human embryonal carcinoma cells. Fenderson, B.A., Andrews, P.W., Nudelman, E., Clausen, H., Hakomori, S. Dev. Biol. (1987) [Pubmed]
  7. The expression of ABH and Y blood group antigens in benign and malignant breast tissue: the preservation of the H and Y antigens in malignant epithelium. Vowden, P., Lowe, A.D., Lennox, E.S., Bleehen, N.M. Br. J. Cancer (1986) [Pubmed]
  8. Human red cell aquaporin CHIP. I. Molecular characterization of ABH and Colton blood group antigens. Smith, B.L., Preston, G.M., Spring, F.A., Anstee, D.J., Agre, P. J. Clin. Invest. (1994) [Pubmed]
  9. Binding of uropathogenic Escherichia coli R45 to glycolipids extracted from vaginal epithelial cells is dependent on histo-blood group secretor status. Stapleton, A., Nudelman, E., Clausen, H., Hakomori, S., Stamm, W.E. J. Clin. Invest. (1992) [Pubmed]
  10. Reexpression of blood group ABH antigens on the surface of human thyroid cells in culture. Khoury, E.L. J. Cell Biol. (1982) [Pubmed]
  11. Crystal structure of human arginase I at 1.29-A resolution and exploration of inhibition in the immune response. Di Costanzo, L., Sabio, G., Mora, A., Rodriguez, P.C., Ochoa, A.C., Centeno, F., Christianson, D.W. Proc. Natl. Acad. Sci. U.S.A. (2005) [Pubmed]
  12. Loss of blood group ABO-related antigen expression in urothelium from patients with chronic cystitis. Orntoft, T.F., Hvid, H., Clausen, H., Hakomori, S., Dabelsteen, E. Lab. Invest. (1989) [Pubmed]
  13. Correlation of expression of binding sites for synthetic blood group A-, B- and H-trisaccharides and for sarcolectin with survival of patients with bronchial carcinoma. Kayser, K., Bovin, N.V., Korchagina, E.Y., Zeilinger, C., Zeng, F.Y., Gabius, H.J. Eur. J. Cancer (1994) [Pubmed]
  14. Genetics and linkage relationships of the C3 polymorphism: discovery of C3-Se linkage and assignment of LES-C3-DM-Se-PEPD-Lu synteny to chromosome 19. Eiberg, H., Mohr, J., Nielsen, L.S., Simonsen, N. Clin. Genet. (1983) [Pubmed]
  15. Semiquantitative immunohistochemical studies of blood group antigen A, B, H, Le(a), Le(b) structures and Ii backbone chains in the normal human cervix and in cervical adenocarcinoma. Griffin, N.R., Wells, M. Histochem. J. (1993) [Pubmed]
  16. Distribution of alkB genes within n-alkane-degrading bacteria. Vomberg, A., Klinner, U. J. Appl. Microbiol. (2000) [Pubmed]
  17. Molecular cloning and functional analysis of a human cDNA encoding an Escherichia coli AlkB homolog, a protein involved in DNA alkylation damage repair. Wei, Y.F., Carter, K.C., Wang, R.P., Shell, B.K. Nucleic Acids Res. (1996) [Pubmed]
  18. H-deficient blood groups ( Bombay) of Reunion Island. Gerard, G., Vitrac, D., Le Pendu, J., Muller, A., Oriol, R. Am. J. Hum. Genet. (1982) [Pubmed]
  19. Immunohistologic expression of blood-group antigens in normal human gastrointestinal tract and colonic carcinoma. Cordon-Cardo, C., Lloyd, K.O., Sakamoto, J., McGroarty, M.E., Old, L.J., Melamed, M.R. Int. J. Cancer (1986) [Pubmed]
  20. Loss of ABH antigen expression in bladder cancer is not caused by loss of heterozygosity of the ABO locus. Meldgaard, P., Johnson, P.H., Langkilde, N.C., Wolf, H., Orntoft, T.F. Int. J. Cancer (1995) [Pubmed]
  21. Biochemical evidence that secretor gene, Se, is a structural gene encoding a specific fucosyltransferase. Kumazaki, T., Yoshida, A. Proc. Natl. Acad. Sci. U.S.A. (1984) [Pubmed]
  22. Insights into the expression of ABH and Lewis antigens through human bone marrow transplantation. Oriol, R., Le Pendu, J., Sparkes, R.S., Sparkes, M.C., Crist, M., Gale, R.P., Terasaki, P.I., Bernoco, M. Am. J. Hum. Genet. (1981) [Pubmed]
  23. Arginase-boronic acid complex highlights a physiological role in erectile function. Cox, J.D., Kim, N.N., Traish, A.M., Christianson, D.W. Nat. Struct. Biol. (1999) [Pubmed]
  24. Establishment and characterization of four human bladder tumor cell lines and sublines with different degrees of malignancy. Lin, C.W., Lin, J.C., Prout, G.R. Cancer Res. (1985) [Pubmed]
  25. Oligosaccharides and discordant xenotransplantation. Cooper, D.K., Koren, E., Oriol, R. Immunol. Rev. (1994) [Pubmed]
  26. Altered antigen expression predicts outcome in squamous cell carcinoma of the head and neck. Wolf, G.T., Carey, T.E., Schmaltz, S.P., McClatchey, K.D., Poore, J., Glaser, L., Hayashida, D.J., Hsu, S. J. Natl. Cancer Inst. (1990) [Pubmed]
  27. Determinants of ABH expression on human blood platelets. Cooling, L.L., Kelly, K., Barton, J., Hwang, D., Koerner, T.A., Olson, J.D. Blood (2005) [Pubmed]
  28. Expression of ABH and X (Lex) antigens on platelets and lymphocytes. Mollicone, R., Caillard, T., Le Pendu, J., François, A., Sansonetti, N., Villarroya, H., Oriol, R. Blood (1988) [Pubmed]
 
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