cDNA cloning of the basement membrane chondroitin sulfate proteoglycan core protein, bamacan: a five domain structure including coiled-coil motifs.

Research output: Contribution to journalJournal articleResearchpeer-review

Standard

cDNA cloning of the basement membrane chondroitin sulfate proteoglycan core protein, bamacan: a five domain structure including coiled-coil motifs. / Wu, R R; Couchman, J R.

In: Journal of Cell Biology, Vol. 136, No. 2, 1997, p. 433-44.

Research output: Contribution to journalJournal articleResearchpeer-review

Harvard

Wu, RR & Couchman, JR 1997, 'cDNA cloning of the basement membrane chondroitin sulfate proteoglycan core protein, bamacan: a five domain structure including coiled-coil motifs.', Journal of Cell Biology, vol. 136, no. 2, pp. 433-44.

APA

Wu, R. R., & Couchman, J. R. (1997). cDNA cloning of the basement membrane chondroitin sulfate proteoglycan core protein, bamacan: a five domain structure including coiled-coil motifs. Journal of Cell Biology, 136(2), 433-44.

Vancouver

Wu RR, Couchman JR. cDNA cloning of the basement membrane chondroitin sulfate proteoglycan core protein, bamacan: a five domain structure including coiled-coil motifs. Journal of Cell Biology. 1997;136(2):433-44.

Author

Wu, R R ; Couchman, J R. / cDNA cloning of the basement membrane chondroitin sulfate proteoglycan core protein, bamacan: a five domain structure including coiled-coil motifs. In: Journal of Cell Biology. 1997 ; Vol. 136, No. 2. pp. 433-44.

Bibtex

@article{d1ae7fb0597611dd8d9f000ea68e967b,
title = "cDNA cloning of the basement membrane chondroitin sulfate proteoglycan core protein, bamacan: a five domain structure including coiled-coil motifs.",
abstract = "Basement membranes contain several proteoglycans, and those bearing heparan sulfate glycosaminoglycans such as perlecan and agrin usually predominate. Most mammalian basement membranes also contain chondroitin sulfate, and a core protein, bamacan, has been partially characterized. We have now obtained cDNA clones encoding the entire bamacan core protein of Mr = 138 kD, which reveal a five domain, head-rod-tail configuration. The head and tail are potentially globular, while the central large rod probably forms coiled-coil structures, with one large central and several very short interruptions. This molecular architecture is novel for an extracellular matrix molecule, but it resembles that of a group of intracellular proteins, including some proposed to stabilize the mitotic chromosome scaffold. We have previously proposed a similar stabilizing role for bamacan in the basement membrane matrix. The protein sequence has low overall homology, apart from very small NH2- and COOH-terminal motifs. At the junctions between the distal globular domains and the coiled-coil regions lie glycosylation sites, with up to three N-linked oligosaccharides and probably three chondroitin chains. Three other Ser-Gly dipeptides are unfavorable for substitution. Fusion protein antibodies stained basement membranes in a pattern commensurate with bamacan, and they also Western blotted bamacan core protein from rat L2 cell cultures. The antibodies could also specifically immunoprecipitate an in vitro transcription/translation product from a full-length bamacan cDNA. The unusual structure of this proteoglycan is indicative of specific functional roles in basement membrane physiology, commensurate with its distinct expression in development and changes in disease models.",
author = "Wu, {R R} and Couchman, {J R}",
note = "Keywords: Amino Acid Sequence; Animals; Base Sequence; Basement Membrane; Blotting, Northern; COS Cells; Cell Cycle Proteins; Chondroitin Sulfates; Chromosomal Proteins, Non-Histone; Cloning, Molecular; DNA, Complementary; Dipeptides; Glycosylation; Membrane Glycoproteins; Molecular Sequence Data; Molecular Weight; Protein Biosynthesis; Protein Structure, Secondary; Protein Structure, Tertiary; Proteochondroitin Sulfates; Rats; Recombinant Fusion Proteins; Sequence Homology, Amino Acid; Transcription, Genetic; Transfection",
year = "1997",
language = "English",
volume = "136",
pages = "433--44",
journal = "Journal of Cell Biology",
issn = "0021-9525",
publisher = "Rockefeller University Press",
number = "2",

}

RIS

TY - JOUR

T1 - cDNA cloning of the basement membrane chondroitin sulfate proteoglycan core protein, bamacan: a five domain structure including coiled-coil motifs.

AU - Wu, R R

AU - Couchman, J R

N1 - Keywords: Amino Acid Sequence; Animals; Base Sequence; Basement Membrane; Blotting, Northern; COS Cells; Cell Cycle Proteins; Chondroitin Sulfates; Chromosomal Proteins, Non-Histone; Cloning, Molecular; DNA, Complementary; Dipeptides; Glycosylation; Membrane Glycoproteins; Molecular Sequence Data; Molecular Weight; Protein Biosynthesis; Protein Structure, Secondary; Protein Structure, Tertiary; Proteochondroitin Sulfates; Rats; Recombinant Fusion Proteins; Sequence Homology, Amino Acid; Transcription, Genetic; Transfection

PY - 1997

Y1 - 1997

N2 - Basement membranes contain several proteoglycans, and those bearing heparan sulfate glycosaminoglycans such as perlecan and agrin usually predominate. Most mammalian basement membranes also contain chondroitin sulfate, and a core protein, bamacan, has been partially characterized. We have now obtained cDNA clones encoding the entire bamacan core protein of Mr = 138 kD, which reveal a five domain, head-rod-tail configuration. The head and tail are potentially globular, while the central large rod probably forms coiled-coil structures, with one large central and several very short interruptions. This molecular architecture is novel for an extracellular matrix molecule, but it resembles that of a group of intracellular proteins, including some proposed to stabilize the mitotic chromosome scaffold. We have previously proposed a similar stabilizing role for bamacan in the basement membrane matrix. The protein sequence has low overall homology, apart from very small NH2- and COOH-terminal motifs. At the junctions between the distal globular domains and the coiled-coil regions lie glycosylation sites, with up to three N-linked oligosaccharides and probably three chondroitin chains. Three other Ser-Gly dipeptides are unfavorable for substitution. Fusion protein antibodies stained basement membranes in a pattern commensurate with bamacan, and they also Western blotted bamacan core protein from rat L2 cell cultures. The antibodies could also specifically immunoprecipitate an in vitro transcription/translation product from a full-length bamacan cDNA. The unusual structure of this proteoglycan is indicative of specific functional roles in basement membrane physiology, commensurate with its distinct expression in development and changes in disease models.

AB - Basement membranes contain several proteoglycans, and those bearing heparan sulfate glycosaminoglycans such as perlecan and agrin usually predominate. Most mammalian basement membranes also contain chondroitin sulfate, and a core protein, bamacan, has been partially characterized. We have now obtained cDNA clones encoding the entire bamacan core protein of Mr = 138 kD, which reveal a five domain, head-rod-tail configuration. The head and tail are potentially globular, while the central large rod probably forms coiled-coil structures, with one large central and several very short interruptions. This molecular architecture is novel for an extracellular matrix molecule, but it resembles that of a group of intracellular proteins, including some proposed to stabilize the mitotic chromosome scaffold. We have previously proposed a similar stabilizing role for bamacan in the basement membrane matrix. The protein sequence has low overall homology, apart from very small NH2- and COOH-terminal motifs. At the junctions between the distal globular domains and the coiled-coil regions lie glycosylation sites, with up to three N-linked oligosaccharides and probably three chondroitin chains. Three other Ser-Gly dipeptides are unfavorable for substitution. Fusion protein antibodies stained basement membranes in a pattern commensurate with bamacan, and they also Western blotted bamacan core protein from rat L2 cell cultures. The antibodies could also specifically immunoprecipitate an in vitro transcription/translation product from a full-length bamacan cDNA. The unusual structure of this proteoglycan is indicative of specific functional roles in basement membrane physiology, commensurate with its distinct expression in development and changes in disease models.

M3 - Journal article

VL - 136

SP - 433

EP - 444

JO - Journal of Cell Biology

JF - Journal of Cell Biology

SN - 0021-9525

IS - 2

ER -

ID: 5165035