Subcellular localization of the synthesis and glycosylation of chondroitin sulfate proteoglycan core protein.

Geetha-Habib, M; Campbell, Steven C.; Schwartz, Nancy B.

doi:10.1016/s0021-9258(17)39872-1

Cited by 64 publications

(19 citation statements)

References 38 publications

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“…Regulating the elaboration of both chondroitin sulfate and heparan sulfate chains on the same core protein is a significant problem because the initial four saccharides are identical. The synthesis of both types of chains is initiated by a xylosyltransferase that resides in either the endoplasmic reticulum or the Golgi region (for review see Farquhar, 1985) and by three Golgilocalized glycosyltransferases (Geetha-Habib et al, 1984). Specific chain elongation subsequently involves the sequential action of an N-acetylgalactosaminyltransferase and a glucuronosyltransferase for chondroitin sulfate, and an N-acetylglucosaminyltransferase and a glucuronosyltransferase for heparan sulfate.…”

Section: Putative Attachment Sites For Heparan Sulfate and Chondroitin Sulfatementioning

confidence: 99%

Molecular cloning of syndecan, an integral membrane proteoglycan.

Saunders

Jalkanen

O'Farrell

et al. 1989

The Journal of Cell Biology

477

251

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Abstract. We describe cDNA clones for a cell surface proteoglycan that bears both heparan sulfate and chondroitin sulfate and that links the cytoskeleton to the interstitial matrix. The eDNA encodes a unique core protein of 32,868 D that contains several structural features consistent with its role as a glycosaminoglycan-containing matrix anchor. The sequence shows discrete cytoplasmic, transmembrane, and NH2-terminal extracellular domains, indicating that the molecule is a type I integral membrane protein. The cytoplasmic domain is small and similar in size but not in sequence to that of the/~-chain of various integrins. The extracellular domain contains a single dibasic sequence adjacent to the extracellular face of the transmembrane domain, potentially serving as the proteasesusceptible site involved in release of this domain from the cell surface. The extracellular domain contains two distinct types of putative glycosaminoglycan attachment sites; one type shows sequence characteristics of the sites previously described for chondroitin sulfate attachment (Bourdon, M. A., T. Krusius, S. Campbell, N. B. Schwartz, and E. Ruoslahti. 1987. Proc. Natl. Acad. Sci. USA. 84:3194-3198), but the other type has newly identified sequence characteristics that potentially correspond to heparan sulfate attachment sites. The single N-linked sugar recognition sequence is within the putative chondroitin sulfate attachment sequence, suggesting asparagine glycosylation as a mechanism for regulating chondroitin sulfate chain addition. Both 5' and 3' regions of this eDNA have sequences substantially identical to analogous regions of the human insulin receptor eDNA: a 99-bp region spanning the 5' untranslated and initial coding sequences is 67 % identical and a 35-bp region in the 3' untranslated region is 81% identical in sequence. mRNA expression is tissue specific; various epithelial tissues show the same two sizes of mRNA (2.6 and 3.4 kb); in the same relative abundance (3:1), the cerebrum shows a single 4.5-kb mRNA. This core protein eDNA describes a new class of molecule, an integral membrane proteoglycan, that we propose to name syndecan (from the Greek syndein, to bind together).

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Section: Putative Attachment Sites For Heparan Sulfate and Chondroitin Sulfatementioning

confidence: 99%

Molecular cloning of syndecan, an integral membrane proteoglycan.

Saunders

Jalkanen

O'Farrell

et al. 1989

The Journal of Cell Biology

477

251

View full text Add to dashboard Cite

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“…Cultures of chick sternal chondrocytes were established from 14 d embryos according to previously described procedures (Geetha-Habib et al, 1984;Cahn et al, 1967) with a few important modifications. Briefly, cells were plated at an initial density of 2.5 × 105/60 nun Falcon Primaria culture dish in F12 medium supplemented with 10% FCS and 50 Ixg/ml gentamycin.…”

Section: Cell Culturementioning

confidence: 99%

“…Membranes were then collected by centrifugation in a type 65 rotor at 40,000 rpm for I h at 4°C, and pellets were resuspended in an appropriate buffer for further analysis. Our previous work using this protocol (Geetha-Habib et al, 1984) demonstrated that the 10-1 fraction (top interface from the gradient containing 10,000 g pellet material) was highly enriched in golgi-derived membranes, while the 100-3 fraction (bottom interface from the gradient containing 100,000 g pellet material) was enriched in RERderived membranes.…”

Section: Subcellular Fractionationmentioning

confidence: 99%

Kinetics of intracellular processing of chondroitin sulfate proteoglycan core protein and other matrix components.

Campbell

Schwartz

1988

The Journal of Cell Biology

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Abstract. Pulse-chase labeling techniques are used in conjunction with subcellular fractionation and quantitative immunoprecipitation to define the kinetics of intracellular translocation and secretion of proteoglycan core protein, along with link protein and type II collagen. In embryonic chick chondrocytes the core protein is processed very rapidly, exhibiting a t,~ in both the rough endoplasmic reticulum and golgi region of less than 10 min. Link protein appears to be processed as rapidly as the core protein, but the kinetics of type II collagen secretion is 3-4 times slower. These results are consistent with possible segregation and coordinate intracellular processing of link protein and core protein, macromolecules which are known to associate extracellularly. In contrast, rat chondrosarcoma chondrocytes translocated and secreted the core protein much more slowly (t,~ = 40 min) than the chick cells, perhaps due to the significantly reduced levels of galactosyltransferase I observed in the transformed chondrocytes.

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“…Like all proteoglycans (PGs), the biosynthesis of the perlecan core protein occurs in the rough endoplasmic reticulum (RER), and it is then transported to the Golgi apparatus where post-translational addition of glycosaminoglycan (GAG) chains occurs [ 10 , 11 , 12 ]. Perlecan is then exported out of the Golgi in vesicles to the extracellular environment or it is translocated to the nucleus or perinuclear regions.…”

Section: Introductionmentioning

confidence: 99%

What Are the Potential Roles of Nuclear Perlecan and Other Heparan Sulphate Proteoglycans in the Normal and Malignant Phenotype

Hayes

Melrose

2021

IJMS

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The recent discovery of nuclear and perinuclear perlecan in annulus fibrosus and nucleus pulposus cells and its known matrix stabilizing properties in tissues introduces the possibility that perlecan may also have intracellular stabilizing or regulatory roles through interactions with nuclear envelope or cytoskeletal proteins or roles in nucleosomal-chromatin organization that may regulate transcriptional factors and modulate gene expression. The nucleus is a mechano-sensor organelle, and sophisticated dynamic mechanoresponsive cytoskeletal and nuclear envelope components support and protect the nucleus, allowing it to perceive and respond to mechano-stimulation. This review speculates on the potential roles of perlecan in the nucleus based on what is already known about nuclear heparan sulphate proteoglycans. Perlecan is frequently found in the nuclei of tumour cells; however, its specific role in these diseased tissues is largely unknown. The aim of this review is to highlight probable roles for this intriguing interactive regulatory proteoglycan in the nucleus of normal and malignant cell types.

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Subcellular localization of the synthesis and glycosylation of chondroitin sulfate proteoglycan core protein.

Cited by 64 publications

References 38 publications

Molecular cloning of syndecan, an integral membrane proteoglycan.

Molecular cloning of syndecan, an integral membrane proteoglycan.

Kinetics of intracellular processing of chondroitin sulfate proteoglycan core protein and other matrix components.

What Are the Potential Roles of Nuclear Perlecan and Other Heparan Sulphate Proteoglycans in the Normal and Malignant Phenotype

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