Polynucleotides that encode the human proteoglycan peptide core

Details Polynucleotides that encode the human proteoglycan peptide core Polynucleotides that encode the human proteoglycan peptide core

1991-01-18

1992-12-15

Wax, Robert A.

Chemistry: molecular biology and microbiology

Micro-organism, tissue cell culture or enzyme using process...

Recombinant dna technique included in method of making a...

435 701, 4353201, 4352401, 4352402, 4352523, 43525233, 536 27, 935 66, 935 70, 935 72, C12P 2102, C12N 121, C12N 510, C07H 2104

Patent

active

051716747

DESCRIPTION:

BRIEF SUMMARY
FIELD OF THE INVENTION

The present invention is directed to the purification of human secretory granule proteoglycan and production of the peptide core thereof by recombinant DNA technology. It is also directed to the production of antibodies against human secretory granule proteoglycan.


BRIEF DESCRIPTION OF THE BACKGROUND ART

Secretory granule proteoglycans comprise one of several families of mammalian proteoglycans, all of which are highly acidic macromolecules possessing at least one sulfated, glycosaminoglycan chain covalently bound to a peptide core. Tantravahi, R. V., et al., Proc. Natl. Acad. Sci. USA 83:9207 (1986). Various proteoglycan families have been proposed in the human based on differential reactivity to panels of monoclonal antibodies, differential peptide mapping after proteolytic treatment, different sizes after translation, and, in some cases, different amino acid sequences. They are further differentiated by their eventual location in the cell (e.g., intracellular, extracellular, and/or pericellular matrix) and by the nature of the carbohydrate residues attached to their peptide cores. For instance, proteoglycans that are localized to extracellular matrices appear to belong to a family that is distinct from the subfamily of more hydrophobic proteoglycans intercalated into the plasma membrane. Tantravahi, R. V., et al., supra.
Although there are at least 12 distinct proteins in the human that exist as proteoglycan peptide cores, the complete primary structure and/or chromosomal location of only a few of these proteoglycans are presently known and no gene has been isolated that encodes the complete peptide core of any proteoglycan.
A cDNA that encodes the dermatan sulfate proteoglycan peptide core that resides in the extracellular matrix around fibroblasts has been cloned from a human embryonic fibroblast cell line. Krusius, T., and Krusius, T., Proc. Natl. Acad. Sci., USA 83:7683 (1986). Its nucleotide sequence predicts a peptide core of 40,000 M.sub.r with three potential glycosaminoglycan initiation sites and three potential sites for N-linked oligosaccharides.
Cell surface glycoproteins may also exist as proteoglycans. For example, the transferrin receptor and the invariant chain of the class II antigens have been reported to be proteoglycans on the plasma membrane of human skin fibroblasts and human lymphoid tissues, respectively. Giacoletto, K. S., et al., J. Exp. Med. 164:1422 (1986). The deduced amino acid sequence of the cDNAs that encode the transferrin receptor and the invariant protein have revealed serineglycine glycosaminoglycan initiation sites. Another proteoglycan which contains chondroitin sulfate glycosaminoglycans has been described on the surfaces of human melanoma cells. Bumol, T. F., and Ricefeld, R. A., Proc. Natl. Acad. Sci. USA 79:1245-1249 (1982). The gene that encodes its more than 240,000 M.sub.r peptide core is predicted to reside on chromosome 15. Rettig, W. J., et al., Science 231:1281 (1986).
The first clear evidence for the existence of proteoglycans stored within the granules of a cell was obtained from studies of the rat skin mast cell. However, it has become increasingly apparent that a number of cells which participate in immune and inflammatory responses, including mucosal mast cells, basophils, eosinophils, neutrophils, macrophages, platelets, and natural killer cells, also contain proteoglycans in their granules. The presence of a family of proteoglycans that resides inside cells rather than on the plasma membrane or in the extracellular matrix suggests that these molecules may be important in the functions of such cells for tumor surveillance and host defense against bacterial, viral, fungal, and parasitic pathogens. Stevens, R. L., "Intracellular Proteoglycans in Cells of the Immune System," In: Biology of Proteoglycans (1987), herein incorporated by reference, reviews the evidence for the localization of the proteoglycans of mast cells, basophils, and natural killer cells within the secretory granule, the unique structural features of these

REFERENCES:
Tantravahi, R. V. et al., Proc. Natl. Acad. Sci. USA 83:9207-9210 (1986).
Giacoletto, K. S. et al., J. Exp. Med. 164:1422-1439 (1986).
Bourdon, M. A. et al., Proc. Natl. Acad. Sci. USA 82:1321-1325 (1985).
Stevens, R. L. et al., The Journal of Biological Chemistry 260:14194-14200 (1985).
Avraham, S. et al., Proc. Natl. Acad. Sci. USA 86:3763-3767 (1989).
Bourdon, M. A. et al., Molecular and Cellular Biology 7:33-40 (1987).
Luikart, S. D. et al., Chemical Abstracts 103:647 Abstract No. 212337K (1985).
Tantravahi, R. V. et al., Fed. Proc. 45:626, Abstract No. 2740 (1986).
Hassell, J. R. et al., Ann. Rev. Biochem. 55:539-567 (1986).
Bourdon, M. A. et al., "Identification from cDNA of the Precursor Form of a Chondroitin Sulfate Proteuglycan Core Protein" J. Biol. Chem. 261:12534-12537 (1986).
Berger S. L. et al. (ed) Methods in Enzymology 152 (1987) Academic Press.
Stevens, R. L. et al., "Isolation and Characterization of a cDNA that encodes the peptide core of the secvectory granule proteoglycan of human promyelocytic leukemia HL-60 cells"]J. Biol. Chem. 263:7287-7291 (1988).
Krusius, T. et al., "Primary structure of an extracellular matrix poteoglycan core protein deduced from cloned cDNA", Proc. Nat. Acad. Sci. 83:7683-7687 (1986).
Alliel, P. M. et al., "Complete Amino Acid Sequence of a human platelet proteoglycan" FEBS Lett. 236:123-126 (Aug. 1988).

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