Evidence for the transfer of mannose to the extension peptides of procollagen within the cisternae of the rough endoplasmic reticulum

Anttinen, Henrik; Oikarinen, Aarne; Ryhänen, Lasse; Kivirikko, Kari I.

doi:10.1016/0014-5793(78)80337-8

Cited by 12 publications

(2 citation statements)

References 27 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Furthermore, asparagine-linked oligosaccharides may be present in the propeptide extensions (14). These oligosaccharides are synthesized on a dolichol lipid intermediate in the RER membrane and transferred intact to the proα chain (15).…”

Section: Collagen Biosynthesismentioning

confidence: 99%

Collagens and proteoglycans of the corneal extracellular matrix

Michelacci

2003

Braz J Med Biol Res

197

136

View full text Add to dashboard Cite

The cornea is a curved and transparent structure that provides the initial focusing of a light image into the eye. It consists of a central stroma that constitutes 90% of the corneal depth, covered anteriorly with epithelium and posteriorly with endothelium. Its transparency is the result of the regular spacing of collagen fibers with remarkably uniform diameter and interfibrillar space. Corneal collagen is composed of heterotypic fibrils consisting of type I and type V collagen molecules. The cornea also contains unusually high amounts of type VI collagen, which form microfibrillar structures, FACIT collagens (XII and XIV), and other nonfibrillar collagens (XIII and XVIII). FACIT collagens and other molecules, such as leucine-rich repeat proteoglycans, play important roles in modifying the structure and function of collagen fibrils. Proteoglycans are macromolecules composed of a protein core with covalently linked glycosaminoglycan side chains. Four leucine-rich repeat proteoglycans are present in the extracellular matrix of corneal stroma: decorin, lumican, mimecan and keratocan. The first is a dermatan sulfate proteoglycan, and the other three are keratan sulfate proteoglycans. Experimental evidence indicates that the keratan sulfate proteoglycans are involved in the regulation of collagen fibril diameter, and dermatan sulfate proteoglycan participates in the control of interfibrillar spacing and in the lamellar adhesion properties of corneal collagens. Heparan sulfate proteoglycans are minor components of the cornea, and are synthesized mainly by epithelial cells. The effect of injuries on proteoglycan synthesis is discussed.

show abstract

Section: Collagen Biosynthesismentioning

confidence: 99%

Collagens and proteoglycans of the corneal extracellular matrix

Michelacci

2003

Braz J Med Biol Res

197

136

View full text Add to dashboard Cite

show abstract

“…The presence of N-glycan on collagen has been observed in the C-terminal propeptide domain [134][135][136][137][138][139][140][141][142]. These studies also revealed that glycan is a high mannose oligosaccharide containing two N-acetylglucosamine (GlcNAc) and six to nine mannose residues.…”

Section: N-glycanmentioning

confidence: 90%

Glycosylation Modulates the Structure and Functions of Collagen: A Review

Tvaroška

2024

Molecules

View full text Add to dashboard Cite

Collagens are fundamental constituents of the extracellular matrix and are the most abundant proteins in mammals. Collagens belong to the family of fibrous or fiber-forming proteins that self-assemble into fibrils that define their mechanical properties and biological functions. Up to now, 28 members of the collagen superfamily have been recognized. Collagen biosynthesis occurs in the endoplasmic reticulum, where specific post-translational modification—glycosylation—is also carried out. The glycosylation of collagens is very specific and adds β-d-galactopyranose and β-d-Glcp-(1→2)-d-Galp disaccharide through β-O-linkage to hydroxylysine. Several glycosyltransferases, namely COLGALT1, COLGALT2, LH3, and PGGHG glucosidase, were associated the with glycosylation of collagens, and recently, the crystal structure of LH3 has been solved. Although not fully understood, it is clear that the glycosylation of collagens influences collagen secretion and the alignment of collagen fibrils. A growing body of evidence also associates the glycosylation of collagen with its functions and various human diseases. Recent progress in understanding collagen glycosylation allows for the exploitation of its therapeutic potential and the discovery of new agents. This review will discuss the relevant contributions to understanding the glycosylation of collagens. Then, glycosyltransferases involved in collagen glycosylation, their structure, and catalytic mechanism will be surveyed. Furthermore, the involvement of glycosylation in collagen functions and collagen glycosylation-related diseases will be discussed.

show abstract

Secretory Organelles: I The Endomembrane System

Dillon

1981

Ultrastructure, Macromolecules, and Evolution

View full text Add to dashboard Cite

Evidence for the transfer of mannose to the extension peptides of procollagen within the cisternae of the rough endoplasmic reticulum

Cited by 12 publications

References 27 publications

Collagens and proteoglycans of the corneal extracellular matrix

Collagens and proteoglycans of the corneal extracellular matrix

Glycosylation Modulates the Structure and Functions of Collagen: A Review

Secretory Organelles: I The Endomembrane System

Contact Info

Product

Resources

About