Gene expression of the chondroitin sulfate proteoglycan core protein PG19.

Bourdon, M A; Shiga, M; Ruoslahti, E

doi:10.1128/mcb.7.1.33

Cited by 29 publications

(30 citation statements)

References 22 publications

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“…USA 83 (1986) 7687 prepro form and processed into the mature core protein of 329 amino acids. Interestingly, the core protein of a rat yolk sac tumor proteoglycan core protein, although otherwise entirely different (9), is also synthesized in a prepro form (33). The mature core protein of PG40 has a molecular weight of 36,319, which is in good agreement with the value of 38,000 determined by NaDodSO4/polyacrylamide gel electrophoresis for the nonglycosylated core protein obtained from tunicamycin-treated fibroblasts (7).…”

Section: Resultssupporting

confidence: 68%

“…Moreover, the 12 amino acid sequence that surrounds the substituted serine within the carboxyl terminus of the propeptide and the amino terminus of the mature core protein in PG40 (residues -3 through 9 in Fig. 2) is 50% homologous to a 12 amino acid stretch within the propeptide of the rat yolk sac tumor proteoglycan (33). It is possible that some structural features in the sequences flanking the Ser-Gly dipeptide or located close to such a sequence can serve as a recognition signal for the attachment of the glycosaminoglycan side chain to the serine residues.…”

Section: Resultsmentioning

confidence: 99%

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Primary structure of an extracellular matrix proteoglycan core protein deduced from cloned cDNA.

Krusius¹,

Ruoslahti²

1986

Proc. Natl. Acad. Sci. U.S.A.

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492

261

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The core protein of a small chondroitin/dermatan sulfate proteoglycan expressed by human fibroblasts and present in extracellular matrices in association with collagen has been cloned from a Xgtll fibroblast cDNA library. cDNA clones were isolated by use of antibodies specific for the intact proteoglycan and antibodies against a peptide synthesized on the basis of the amino-terminal sequence of the core protein. A 1.8-kilobase cDNA was found to code for a prepro core protein composed of a signal peptide, a propeptide, and a mature core protein of 329 amino acids. The amino-terminal amino acid sequence deduced from the cDNA sequence was identical to that previously obtained by protein sequencing. The core protein contains three Ser-Gly dipeptide sequences, of which one is substituted with glycosaminoglycan. A protein data base homology search established the core protein sequence is a unique sequence distinct from published amino acid sequences. RNA blot hybridizations, performed using the cloned cDNA as a probe, revealed two related transcripts of 1.6 and 1.9 kilobases in RNA from both human fibroblast and placental tissue. Hybridization of genomic DNA restriction fragments suggested that there is one gene for the core protein of this proteoglycan and possibly one other closely related gene. Availability of the cloned cDNA for the proteoglycan now makes it possible to apply methods of molecular biology to study the collagen-binding and cell attachment-inhibiting properties of this proteoglycan.Proteoglycans are abundant molecules in extracellular matrices, in basement membranes, and at cell surfaces (1, 2). They exist in many different forms, some of which are tissueor cell-type specific (1, 2). The structural relationships and functional properties of proteoglycans are poorly understood. This is mostly due to a lack of detailed structural information about the core proteins which primarily determine the specific properties of a proteoglycan.A small chondroitin/dermatan sulfate proteoglycan, or group of proteoglycans, is of particular interest due to its abundance and functional properties. This proteoglycan is the major sulfated product of fibroblasts and is abundant in the extracellular matrices of connective tissues (2). It binds to type I collagen, affecting fibril formation (3,4), and inhibits the cell attachment-promoting activity of collagen and fibronectin by binding to these molecules near their cell-binding site (5). At least the binding to collagen appears to be mediated by the core protein, since treatment of the proteoglycan with chondroitinase, which removes most of the glycosaminoglycan, does not eliminate the binding to collagen (ref. 4 and unpublished results).This proteoglycan has a core protein of Mr 38,000 and usually carries one glycosaminoglycan chain (2, 6, 7). It is not known whether the core protein is a single protein or whether it might consist of a family of closely related molecules. Recent work on bovine cartilage proteoglycans suggests that at least two core protein species...

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Section: Resultssupporting

confidence: 68%

Section: Resultsmentioning

confidence: 99%

Primary structure of an extracellular matrix proteoglycan core protein deduced from cloned cDNA.

Krusius¹,

Ruoslahti²

1986

Proc. Natl. Acad. Sci. U.S.A.

Self Cite

492

261

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show abstract

“…The GAG chains are clustered closely within this region, conferring a unique structure on this proteoglycan. The human serglycin proteoglycan carries chondroitin sulfate chains in most hematopoietic cells (1)(2)(3)(4), whereas mucosal mast cell serglycin carries chondroitin sulfate or heparin (5). The length and number of chondroitin sulfate GAG chains vary in a cellspecific fashion among these different cells.…”

mentioning

confidence: 99%

DNase I Hypersensitivity Patterns of the Serglycin Proteoglycan Gene in Resting and Phorbol 12-Myristate 13-Acetate-stimulated Human Erythroleukemia (HEL), CHRF 288-11, and HL-60 Cells Compared with Neutrophils and Human Umbilical Vein Endothelial Cells

Castronuevo

Thornton

McCarthy

et al. 2003

Journal of Biological Chemistry

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“…Since the acceptor assay potentially measures both recognition by the enzyme and acceptor activity, we also examined several of the inactive peptides as competitors for xylosyltransferase in peptide acceptor assays. We are particularly interested in a peptide derived from the PG19 propeptide (21) that is homologous with the 12-amino acid homology region in the core proteins. This sequence is probably not substituted with a glycosaminoglycan, since the serine is followed by an asparagine residue, not a glycine, and since peptides corresponding to this sequence were inactive as acceptors in the xylosyltransferase assay (Table 1, peptides 10 and 11).…”

mentioning

confidence: 99%

Identification and synthesis of a recognition signal for the attachment of glycosaminoglycans to proteins.

Bourdon¹,

Krusius²,

Campbell³

et al. 1987

Proc. Natl. Acad. Sci. U.S.A.

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229

136

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Comparison of the amino acid sequences of three different proteoglycan core proteins reveals a 12-amino acid sequence that is about 50% homologous among these proteoglycans. In each of the proteoglycans, this sequence surrounds the serine-glycine dipeptide in which the serine is known or presumed to be substituted with a chondroitin/dermatan sulfate glycosaminoglycan chain. Peptides containing this sequence from two proteoglycans were examined for their ability to serve as acceptors for xylosyltransferase, the enzyme that begins the assembly of glycosaminoglycan chains.Those peptides corresponding to amino acid sequences known to contain glycosaminoglycan-substituted serine residues in the protein were efficient xylosyltransferase acceptors, whereas peptides from sequences with no glycosaminoglycan-substituted serine residues were not. Amino acid substitutions at four critical sites in the acceptor peptides showed that single substitutions could completely abolish acceptor activity or greatly reduce it. The results suggest that the proteoglycan recognition consensus sequence for the attachment of glycosaminoglycans to core proteins consists of acidic amino acids closely followed by the tetrapeptide Ser-Gly-Xaa.Gly, where Xaa is any amino acid. The signal appears to be contained in the primary sequence information. In this regard it resembles a number of other signals for protein processing and intracellular routing.

show abstract

Gene expression of the chondroitin sulfate proteoglycan core protein PG19.

Cited by 29 publications

References 22 publications

Primary structure of an extracellular matrix proteoglycan core protein deduced from cloned cDNA.

Primary structure of an extracellular matrix proteoglycan core protein deduced from cloned cDNA.

DNase I Hypersensitivity Patterns of the Serglycin Proteoglycan Gene in Resting and Phorbol 12-Myristate 13-Acetate-stimulated Human Erythroleukemia (HEL), CHRF 288-11, and HL-60 Cells Compared with Neutrophils and Human Umbilical Vein Endothelial Cells

Identification and synthesis of a recognition signal for the attachment of glycosaminoglycans to proteins.

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