Xylosylation and glucuronosylation reactions in rat liver Golgi apparatus and endoplasmic reticulum.

Nuwayhid, Naziha Faiz; Glaser, J H; Johnson, Jo-Anne; Conrad, H. Edward; Hauser, Stephen C.; Hirschberg, Carlos B.

doi:10.1016/s0021-9258(18)69252-x

Cited by 74 publications

(12 citation statements)

References 29 publications

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“…1981b, 1984). Results from these experiments are analogous to what has been observed in the chick sternal chondrocyte system, except there is evidence that xylosylation may not occur to a large extent in the rough endoplasmic reticulum (RER) in this system (Kimura et al, 1984, Nuwayhid et al, 1986. The temporal characteristics of CSPG assembly have also been established in rat chondrosarcoma chondrocytes (Fellini et al, 1984;Mitchell and Hardingham, 1981;Kimura et al, 1981a).…”

supporting

confidence: 74%

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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supporting

confidence: 74%

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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“…The subcellular site for xylosylation of the CSPG core protein, a modification involving O-linkage to serine residues, is unresolved. Some investigators have ascribed this function to the ER (Geetha-Habib et al, 1984;Hoffmann et al, 1984), while others suggest xylosylation occurs in the Golgi complex (Kimura et al, 1984;Nuwayhid et al, 1986). It may be possible that the ER subcompartment of chondrocytes functions in xylosylation.…”

Section: Discussionmentioning

confidence: 99%

“…While we can assign intracellular locations for many processing events, others remain obscure. For example, the subcellular site for xylosylation of the CSPG core protein before glycosaminoglycan chain elongation is not resolved (Geetha-Habib et al, 1984;Hoffmann et al, 1984;Nuwayhid et al, 1986), and it has been proposed that the CSPG core protein and link protein associate before secretion (Kimura et al, 1981;Vertel and Barkman, 1984;Campbell and Schwartz, 1988), but neither an assembly event, nor a site of assembly has been demonstrated.…”

mentioning

confidence: 99%

Precursors of chondroitin sulfate proteoglycan are segregated within a subcompartment of the chondrocyte endoplasmic reticulum.

Vertel

Velasco

LaFrance

et al. 1989

The Journal of Cell Biology

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Abstract. Immunocytochemical methods were used at the levels of light and electron microscopy to examine the intracellular compartments of chondrocytes involved in extracellular matrix biosynthesis. The results of our studies provide morphological evidence for the compartmentalization of secretory proteins in the ER. Precursors of the large chondroitin sulfate proteoglycan (CSPG), the major proteoglycan species produced by chondrocytes, were present in the Goigi complex. In addition, CSPG precursors were localized in specialized regions of the ER. Link protein, a separate gene product which functions to stabilize extracellular aggregates of CSPG monomers with hyaluronic acid, was segregated similarly. In contrast, type II procollagen, another major secretory molecule produced by chondrocytes, was found homogeneously distributed throughout the ER. The CSPG precursor-containing ER compartment exhibits a variable tubulo-vesicular morphology but is invariably recognized as an electronlucent, smooth membrane-bounded region continuous with typical ribosome-studded elements of the rough ER. The observation that this ER structure does not stain with antibodies against resident ER proteins also suggests that the compartment is a specialized region distinct from the main part of the ER. These results support recent studies that consider the ER as a compartmentalized organelle and are discussed in light of the possible implications for proteoglycan biosynthesis and processing.

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“…Although the entire lectican family of CSPGs shares structural similarity, lectican may exist as a variety of isoforms based on the chemical composition of GAG chains. The GAG chain is attached to the core proteins in the endoplasmic reticulum (ER) and Golgi compartment (10)(11)(12)(13). The glycosylation of lectican proteoglycan is initiated by the addition of xylose residue to a serine in the central domain of lecticans.…”

Section: Lectican the Sulfated Proteoglycan In Neuronal Ecmsmentioning

confidence: 99%

“…The glycosylation of lectican proteoglycan is initiated by the addition of xylose residue to a serine in the central domain of lecticans. This reaction is mediated by xylotransferase in ER (10,11,13). Next, two additional galactoses are sequentially added to the xylose in the Golgi compartment prior to the addition of GAG chains (14).…”

Section: Lectican the Sulfated Proteoglycan In Neuronal Ecmsmentioning

confidence: 99%

Extracellular matrixes and neuroinflammation

et al. 2020

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The extracellular matrix is a critical component of every human tissue. ECM not only functions as a structural component but also regulates a variety of cellular processes such as cell migration, differentiation, proliferation, and cell death. In addition, current studies suggest that ECM is critical for the pathophysiology of various human diseases. ECM is composed of diverse components including several proteins and polysaccharide chains such as chondroitin sulfate, heparan sulfate, and hyaluronic acid. Each component of ECM exerts its own functions in cellular and pathophysiological processes. One of the interesting recent findings is that ECM is involved in inflammatory responses in various human tissues. In this review, we summarized the known functions of ECM in neuroinflammation after acute injury and chronic inflammatory diseases of the central nerve systems.

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Xylosylation and glucuronosylation reactions in rat liver Golgi apparatus and endoplasmic reticulum.

Cited by 74 publications

References 29 publications

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

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

Precursors of chondroitin sulfate proteoglycan are segregated within a subcompartment of the chondrocyte endoplasmic reticulum.

Extracellular matrixes and neuroinflammation

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