Abstract
Tetranectin is a plasminogen-binding tetrameric protein originally isolated from plasma. Expression of tetranectin appears ubiquitous, although particularly high expression is noted in the stroma of malignant tumors and during mineralization. To dissect the molecular basis of tetranectin gene regulation, mouse tetranectin cDNA was cloned from a 16-day-old mouse embryo library. Sequence analysis revealed a 992-bp cDNA with an open reading frame of 606 bp, which is identical in length to the human tetranectin cDNA. The deduced amino acid sequence showed high homology to the human cDNA with 76% identity and 87% similarity at the amino acid level. Sequence comparisons between mouse and human tetranectin and some C-type lectins confirmed a complete conservation in the position of six cysteines as well as numerous other amino acid residues, indicating an essential structure for potential function(s) of tetranectin. The sequence analysis revealed a difference in both sequence and size of the noncoding regions between mouse and human cDNAs. Northern analysis of the various tissues from mouse, rat, and cow showed the major transcript(s) to be approximately 1 kb, which is similar in size to that observed in human. Although additional minor bands of 1.5 and 3.3 kb were found in Northern blots, RT-PCR (reverse transcription polymerase chain reaction) analysis failed to provide evidence that these minor bands are products of the tetranectin gene. Finally, the genetic map location for this gene, Tna, was determined to be on distal mouse Chromosome (Chr) 9 by analysis of two sets of multilocus crosses.
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References
Adamson, M.C., Silver, J., Kozak, C.A. (1991). The mouse homolog of the gibbon ape leukemia virus receptor: genetic mapping and a possible receptor function in rodents. Virology 183, 778–781.
Berglund, L., Petersen, T.E., (1992). The gene structure of tetranectin, a plasminogen binding protein. FEBS Lett. 31, 15–19.
Chen, L.H., Bissell, M.J. (1987). Transferrin mRNA level in the mouse mammary gland is regulated by pregnancy and extracellular matrix. J. Biol. Chem. 262, 17247–17250.
Christensen, L., Clemmensen, I. (1989). Tetranectin immunoreactivity in normal human tissues: an immunohistochemical study of exocrine epithelia mesenchyme. Histochemistry 92, 29–35.
Christensen, L., Clemmensen, I. (1991). Differences in tetranectin immunoreactivity between benign and malignant breast tissue. Histochemistry 95, 427–433.
Clemmensen, I. (1989). Interaction of tetranectin with sulfated polysaccharides and trypan blue. Scand. J. Clin. Lab. Invest. 49, 719–725.
Clemmensen, I., Chr. Petersen, L., Kluft, C. (1986). Purification and characterization of a novel, oligomeric, plasminogen kringle 4 binding protein from human plasma: tetranectin. Eur. J. Biochem. 156, 327–333.
Danciger, M., Kozak, C.A., Farber, D.B. (1989). The gene for the alphasubunit of retinal rod transducin on mouse chromosome 9. Genomics 4, 215–217.
Drickamer, K. (1988). Two distinct classes of carbohydrate-recognition domains in animal lectins. J. Biol. Chem. 263, 9557–9560.
Friedman, J.M., Schneider, B.S., Barton, D.E., Francke, U. (1989). Level of expression and chromosome mapping of the mouse cholecystokinin gene: implications for murine models of genetic obsity. Genomics 5, 463–469.
Fuhlendorff, J., Clemmensen, I., Magnusson, S. (1987). The primary structure of a kringle 4 binding protein: tetranectin. Structure homology with asialoprotein receptors and a proteoglycan core protein. Biochemistry 26, 6257–6264.
Green, E.L. (1981). Linkage, recombination and mapping In Genetics and Probability in Animal Breeding Experiments, ? eds. (New York: Macmillan), p. 77.
Ibaraki, K., Termine, J.D., Whitson, S.W., Young, M.F. (1992). Bone matrix mRNA expression in differentiating fetal bovine osteoblasts. J. Bone Min. Res. 7, 743–754.
Imai, K., Kingsley, D.M., (1994) Mouse Chromosome 9. Mamm. Genome 5, S139-S153.
Jensen, B.A., Clemmensen, I. (1988). Plasma tetranectin is reduced in cancer and related to metastasia. Cancer 62. 869–872.
Kluft, C., Los, P., Clemmensen, I. (1989) Calcium-dependent binding of tetranectin to fibrin. Thrombosis Res. 55, 233–238.
Kozak, C.A., Peyser, M., Krall, M., Mariano, T.M., Kumar, C.S., Pestka, S., Mock, B.A. (1990). Molecular genetic markers spanning mouse chromosome 10. Genomics 8, 519–524.
Naeme, P.J., Young, C.N., Treep, J.T. (1992). Primary structure of a protein isolated from reef shark (Carcharhinus springeri) cartilage that is similar to the mammalian C-type lectin homolog, tetranectin. Protein Sci. 1, 161–168.
Sambrook, J., Fritsch, E.E., Maniatis, T. (1989). Molecular Cloning: A Laboratory Manual, 2nd ed. (Cold Spring Harbor, N.Y.: Cold Spring Harbor Laboratory Press).
Sorensen, C.B., Berglund, L., Petersen, T.E. (1995). Cloning of a cDNA encoding murine tetranectin. Gene 23, 243–245.
Wewer, U.M., Albrechtsen, R. (1992). Tetranectin, a plasminogen kringle 4-binding protein: cloning and gene expression pattern in human colon cancer. Lab. Invest. 67, 253–262.
Wewer, U.M., Ibaraki, K., Schjørring, P., Durkin, M.E., Young, M.F., Albrechtsen, R. (1994). A potential rule for tetranectin in mineralization during osteogenesis. J. Cell Biol. 127, 1767–1775.
Young, M.F., Ibaraki, K., Kerr, J., Lyu, M.S., Kozak, C.A. (1994). Murine bone sialoprotein (BSP): cDNA cloning, mRNA expression, and genetic mapping. Mamm. Genome 5, 108–111.
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Ibaraki, K., Kozak, C.A., Wewer, U.M. et al. Mouse tetranectin: cDNA sequence, tissue-specific expression, and chromosomal mapping. Mammalian Genome 6, 693–696 (1995). https://doi.org/10.1007/BF00354289
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DOI: https://doi.org/10.1007/BF00354289