Identification and characterization of CPAMD8, a novel member of the complement 3/α2-macroglobulin family with a C-terminal Kazal domain

Genomics

Volumn 83, Issue 6, 2004, Pages 1083-1093

  Li, Zhi Fang ^a   Wu, Xiao Hua ^a   Engvall, Eva ^a  

^a BURNHAM INSTITUTE   (United States)

Author keywords

2 Macroglobulin; Brain; Complement 3; Heparin binding; Innate immunity; Kazal domain; Kidney; Protease activated receptor 4

Indexed keywords

ALPHA 2 MACROGLOBULIN; AMINO ACID; COMPLEMENT COMPONENT C3; COMPLEMENTARY DNA; FOLLISTATIN; HEPARIN; PREGNANCY ASSOCIATED ALPHA2 GLYCOPROTEIN; PROTEINASE ACTIVATED RECEPTOR 4; SERINE PROTEINASE INHIBITOR;

ARTICLE; BRAIN; CARBOXY TERMINAL SEQUENCE; CELL CULTURE; CELL FRACTIONATION; CHROMOSOME 19P; EXON; GENE IDENTIFICATION; GENE MAPPING; GENETIC TRANSCRIPTION; HEART; HUMAN; HUMAN TISSUE; IMMUNOBLOTTING; KIDNEY; LIVER; NUCLEOTIDE SEQUENCE; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DEGRADATION; PROTEIN DOMAIN; REVERSE TRANSCRIPTION POLYMERASE CHAIN REACTION; RNA TRANSLATION; SMALL INTESTINE; TESTIS;

ALPHA-MACROGLOBULINS; AMINO ACID SEQUENCE; CELL MEMBRANE; CHROMOSOMES, HUMAN, PAIR 19; CLONING, MOLECULAR; COMPLEMENT C3; CYTOKINES; EXONS; GENE EXPRESSION PROFILING; HUMANS; MOLECULAR SEQUENCE DATA; PROTEIN PROCESSING, POST-TRANSLATIONAL; PROTEIN SORTING SIGNALS; PROTEIN STRUCTURE, TERTIARY; SEQUENCE ALIGNMENT; SEQUENCE ANALYSIS, DNA; SEQUENCE ANALYSIS, PROTEIN; SEQUENCE HOMOLOGY, AMINO ACID; TRYPSIN INHIBITOR, KAZAL PANCREATIC; UP-REGULATION;

EID: 2642557821     PISSN: 08887543     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ygeno.2003.12.005     Document Type: Article

References (50)

1. Sottrup-Jensen L. α2-Macroglobulin and related thiol ester plasma proteins. Putnam F.W. The Plasma Proteins: Structure, Function and Genetic Control. 1987;191-291 Academic Press, Orlando
2. 2-Macroglobulin: an evolutionarily conserved arm of the innate immune system. Dev. Comp. Immunol. 23:1999;375-390
3. Volanakis J.E. The role of complement in innate and adaptive immunity. Curr. Top. Microbiol. Immunol. 266:2002;41-56
4. Barnum S.R., Fey G., Tack B.F. Biosynthesis and genetics of C3. Lambris J.D. The Third Complement Component. 1990;23-43 Springer-Verlag, Berlin
5. Studd J.W., Blainey J.D., Bailey D.E. A study of serum protein changes in late pregnancy and identification of the pregnancy zone protein using antigen antibody crossed immunoelectrophoresis. J. Obstet. Gynaecol. Br. Commun. 77:1970;42-51
6. 2M-macroglobulin. Immunol. Rev. 166:1998;15-26
7. Lin M., et al. Cell surface antigen CD109 is a novel member of the alpha (2) macroglobulin/C3, C4, C5 family of thioester-containing proteins. Blood. 99:2002;1683-1691
8. Senger D.R., Hynes R.O. C3 component of complement secreted by established cell lines. Cell. 15:1978;375-384
9. Van Leuven F., Cassiman J.J., Van den Berghe H. Human pregnancy zone protein and alpha 2-macroglobulin: high-affinity binding of complexes to the same receptor on fibroblasts and characterization by monoclonal antibodies. J. Biol. Chem. 261:1986;16622-16625
10. Sottrup-Jensen L., Gliemann J., Van Leuven F. Domain structure of human alpha 2-macroglobulin: characterization of a receptor-binding domain obtained by digestion with papain. FEBS Lett. 205:1986;20-24
11. Crookston K.P., Webb D.J., Wolf B.B., Gonias S.L. Classification of alpha 2-macroglobulin-cytokine interactions based on affinity of noncovalent association in solution under apparent equilibrium conditions. J. Biol. Chem. 269:1994;1533-1540
12. Gonias S.L., LaMarre J., Crookston K.P. Alpha 2-macroglobulin and the alpha 2-macroglobulin receptor/LRP: a growth regulatory axis. Ann. N.Y. Acad. Sci. 737:1994;273-290
13. Liu Q., et al. Identification of the high affinity binding site in transforming growth factor-beta involved in complex formation with alpha 2-macroglobulin: implications regarding the molecular mechanisms of complex formation between alpha 2-macroglobulin and growth factors, cytokines, and hormones. J. Biol. Chem. 276:2001;46212-46218
14. Arandjelovic S., Freed T.A., Gonias S.L. Growth factor-binding sequence in human alpha(2)-macroglobulin targets the receptor-binding site in transforming growth factor-beta. Biochemistry. 42:2003;6121-6127
15. Gonias S.L., et al. Identical or overlapping sequences in the primary structure of human alpha(2)-macroglobulin are responsible for the binding of nerve growth factor-beta, platelet-derived growth factor-BB, and transforming growth factor-beta. J. Biol. Chem. 275:2000;5826-5831
16. Mettenburg J.M. Distinct binding sites in the structure of α2M mediate the interaction with beta-amyloid peptide and growth factors. J. Biol. Chem. 277:2002;13345-13388
17. Blacker D., Wilcox M.A., Laird N.M. Alpha-2 macroglobulin is genetically associated with Alzheimer disease. Nat. Genet. 19:1998;357-360
18. Gunnarsson M., Stigbrand T., Jensen P.E. Aberrant forms of alpha(2)-macroglobulin purified from patients with multiple sclerosis. Clin. Chim. Acta. 295:2000;27-40
19. Sarcione E.J., Biddle W.C. Elevated serum pregnancy zone protein levels in HIV-1-infected men. AIDS. 15:2001;2467-2469
20. Beckman L., von Schoultz B., Stigbrand T. "Pregnancy zone" protein in sera from patients with prostatic cancer treated with oestrogens. Urol. Res. 1:1973;67-69
21. Sutherland D.R., et al. Identification of a cell-surface antigen associated with activated T lymphoblasts and activated platelets. Blood. 77:1991;84-93
22. + cells enriched in hematopoietic stem and progenitor cells. Exp. Hematol. 27:1999;1282-1294
23. Joni D., et al. Post-translational proteolytic processing of procollagen C-terminal proteinase enhancer releases a metalloproteinase inhibitor. J. Biol. Chem. 275:2000;1384-1390
24. Banyai L., Patthy L. The NTR module: domains of netrins, secreted frizzled related proteins, and type I procollagen C-proteinase enhancer protein are homologous with tissue inhibitors of metalloproteases. Protein Sci. 8:1999;1636-1642
25. Samonte I.E., Sato A., Mayer W.E., Shintani S., Klein J. Linkage relationships of genes coding for alpha2-macroglobulin, C3 and C4 in the zebrafish: implications for the evolution of the complement and MHC systems. Scand. J. Immunol. 56:2002;344-352
26. Nakao M., Mutsuro J., Nakahara M., Kato Y., Yano T. Expansion of genes encoding complement components in bony fish: biological implications of the complement diversity. Dev. Comp. Immunol. 27:2003;749-762
27. Saito A., Sinohara H. Murinoglobulin, a novel protease inhibitor from murine plasma: isolation, characterization, and comparison with murine alpha-macroglobulin and human alpha-2-macroglobulin. J. Biol. Chem. 260:1985;775-781
28. Overbergh L., Hilliker C., Lorent K., Van Leuven F., Van den Berghe H. Identification of four genes coding for isoforms of murinoglobulin, the monomeric mouse alpha 2-macroglobulin: characterization of the exons coding for the bait region. Genomics. 22:1994;530-539
29. Lagueux M., Perrodou E., Levashina E.A., Capovilla M., Hoffmann J.A. Constant expression of a TEP protein in Toll and JAK gain-of-function mutant. Proc. Natl. Acad. Sci. USA. 97:2000;11427-11432
30. Levashina E.A., et al. Conserved role of a complement-like protein in phagocytosis revealed by dsDNA knockout in cultured cells of the mosquito, Anopheles gambiae. Cell. 104:2001;709-718
31. Sunyer J.O., Zarkadis I.K., Lambris J.D. Complement diversity: a mechanism for generating immune diversity. Immunol. Today. 19:1998;520-522
32. Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O. Prediction of the coding sequences of unidentified human genes: XVII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 7:2000;143-150
33. Roskoski R. Jr. Protein prenylation: a pivotal posttranslational process. Biochem. Biophys. Res. Commun. 303:2003;1-7
34. Lewin B. Gene VI. 1997;Oxford Univ. Press, Oxford
35. Yu C.Y. Genetics of human complement component C4 and evolution the central MHC. Front. Biosci. 6:2001;D904-D913
36. Abi-Rached L., Gilles A., Shiina T., Pontarotti P., Inoko H. Evidence of en bloc duplication in vertebrate genomes. Nat. Genet. 31:2002;100-105
37. 2-macroglobulin expression is due to activation of NF-κB. J. Immunol. 167:2001;1469-1481
38. Higuchi M., et al. Expression of the alpha 2-macroglobulin-encoding gene in rat brain and cultured astrocytes. Gene. 141:1994;155-162
39. Barnum S.R., Jones J.L., Benveniste E.N. Interleukin-1 and tumor necrosis factor-mediated regulation of C3 gene expression in human astroglioma cells. Glia. 7:1993;225-236
40. 2-macroglobulin in a human glial cell line. Mol. Brain Res. 105:2002;108-114
41. Kazal L.A., Spicer D.S., Brahinski R.A. Isolation of a bovine pancreatic secretory trypsin inhibitor-anticoagulant protein from the pancreas. J. Am. Chem. Soc. 70:1948;3034-3040
42. Greene L.J., Bartelt D.C. The structure of the bovine pancreatic secretory trypsin inhibitor-Kazal's inhibitor: II. The order of the tryptic peptides. J. Biol. Chem. 244:1969;2646-2657
43. Hoheneaster E., Maurer P., Timpl R. Crystal structure of a pair of follistatin-like and EF-hand calcium-binding domains in BM-40. EMBO J. 16:1997;3778-3786
44. Chneyer A., et al. Follostatin-related protein (FSRP): a new member of the follistatin gene family. Mol. Cell. Endocrinol. 180:2001;33-38
45. Hill J.J., Qiu Y., Hewick R.M., Wolfman N.M. Regulation of myostatin in vivo by growth and differentiation factor-associated serum protein-1: a novel protein with protease inhibitor and follistatin domains. Mol. Endocrinol. 17:2003;1144-1154
46. Innis C.A., Hyvonen M. Crystal structures of the heparan sulphate-binding domain of follistatin: insights into ligand binding. J. Biol. Chem. 278:2003;39969-39977
47. Burge C., Karlin S. Prediction of complete gene structures in human genomic DNA. J. Mol. Biol. 268:1997;78-94
48. Sambrook J., Fritsch E.F., Maniatis T. Molecular Cloning: A Laboratory Manual. 1989;Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
49. Yang R.B., et al. Identification of a novel family of cell-surface proteins expressed in human vascular endothelium. J. Biol. Chem. 277:2002;46364-46373
50. Holmes E., Engvall E. Determination of integrins on cells by cell adhesion to antibodies. Anal. Biochem. 214:1993;100-105