The Specificity of a Mouse Monoclonal Antibody to Human Aorta Proteoglycans

Baker, John; Walker, Terri C.; Morrison, Kelly; Neame, Peter J.; Christner, James E.

doi:10.1016/s0934-8832(89)80026-5

Cited by 11 publications

(2 citation statements)

References 31 publications

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“…27 A preparation of proteoglycans from human aorta was obtained by a previously outlined procedure. 28 The aortic proteoglycans were further fractionated by gel chromatography on Sepharose CL-2B to give a partial separation of chondroitin sulfate and dermatan sulfate proteoglycans (see Figure 2 and Table 1 …”

Section: Methodsmentioning

confidence: 99%

Specificity of the low density lipoprotein-glycosaminoglycan interaction.

Sambandam

Baker

Christner

et al. 1991

Arterioscler Thromb

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There is ample documentation of the binding of chondroitin sulfate/dermatan sulfate proteoglycans to low density lipoprotein (LDL) both in vivo and in vitro. The interaction of these two species may be an early and important step in atberogenesis. Therefore, there is interest in defining the features of both molecules that are critical for then-interaction. We employed a recently described competitive microassay that measures initial binding of proteogtycan to immobilized LDL. We confirmed the work of others that it is the apolipoprotein B component and, at least in part, a heparin-binding domain of LDL that are responsible for binding chondroitin sulfate/dermatan sulfate proteoglycans. The principal thrust of our study was concerned with the effects of a gtyeosaminoglycan's degree of sulfation on the binding to LDL. Initial experiments comparing dermatan sulfate and chondroitin sulfate proteoglycans indicated that the former was more efficient at binding LDL than the latter and that oversulfation, rather than chain length or iduronate content, was the preeminent feature involved. Additional binding studies with dermatan sulfate, chemically sulfated chondroitin-4-sulfate, and naturally occurring oversulfated chondroitin sulfates indicated that the degree of sulfation, not the position of sulfation, determined affinity for LDL. These results suggest that studies should be undertaken to determine whether oversulfated segments of glycosaminoglycans are especially involved in associations with LDL, leading to lipid accumulation, in the artery wall. (Arteriosclerosis and TTirombosis 1991;ll:561-568)

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Section: Methodsmentioning

confidence: 99%

Specificity of the low density lipoprotein-glycosaminoglycan interaction.

Sambandam

Baker

Christner

et al. 1991

Arterioscler Thromb

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“…MAb 4-C-4 detects a sialyl fucosyl-KS proteoglycan containing highly sulfated KS on embryonic carcinoma cells ( Fukuma et al 2003 ). Monoclonal antibody, 6D2/B5, recognizes a fucosyl-KS epitope in cartilage proteoglycans and also detects fucoidan ( Baker et al 1989 ). A novel anti-KS antibody 3D12/H7 identifies KS chains interspersed within the CS rich region of the aggrecan core protein in articular cartilage and to a significantly lesser extent in tracheal cartilage aggrecan and corneal extracts ( Fischer et al 1996 ).…”

Section: Introductionmentioning

confidence: 99%

Keratan sulfate, a complex glycosaminoglycan with unique functional capability

2018

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From an evolutionary perspective keratan sulfate (KS) is the newest glycosaminoglycan (GAG) but the least understood. KS is a sophisticated molecule with a diverse structure, and unique functional roles continue to be uncovered for this GAG. The cornea is the richest tissue source of KS in the human body but the central and peripheral nervous systems also contain significant levels of KS and a diverse range of KS-proteoglycans with essential functional roles. KS also displays important cell regulatory properties in epithelial and mesenchymal tissues and in bone and in tumor development of diagnostic and prognostic utility. Corneal KS-I displays variable degrees of sulfation along the KS chain ranging from non-sulfated polylactosamine, mono-sulfated and disulfated disaccharide regions. Skeletal KS-II is almost completely sulfated consisting of disulfated disaccharides interrupted by occasional mono-sulfated N-acetyllactosamine residues. KS-III also contains highly sulfated KS disaccharides but differs from KS-I and KS-II through 2-O-mannose linkage to serine or threonine core protein residues on proteoglycans such as phosphacan and abakan in brain tissue. Historically, the major emphasis on the biology of KS has focused on its sulfated regions for good reason. The sulfation motifs on KS convey important molecular recognition information and direct cell behavior through a number of interactive proteins. Emerging evidence also suggest functional roles for the poly-N-acetyllactosamine regions of KS requiring further investigation. Thus further research is warranted to better understand the complexities of KS.

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Keratan Sulphate in the Tumour Environment

Hayes

Melrose

2020

Advances in Experimental Medicine and Biology

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Keratan sulphate (KS) is a bioactive glycosaminoglycan (GAG) of some complexity composed of the repeat disaccharide D-galactose 1→4 glycosidically linked to N-acetyl glucosamine. During the biosynthesis of KS a family of glycosyl transferase and sulphotransferase enzymes act sequentially and in a co-ordinated fashion to add D-galactose (D-Gal) then N-acetyl glucosamine (GlcNAc) to an GlcNAc acceptor residue at the reducing terminus of a nascent KS chain to effect chain elongation. D-Gal and GlcNAc can both undergo sulphation at C6 but this occurs more frequently on GlcNAc than D-Gal. Sulphation along the developing KS chain is not uniform and contains regions of variable length where no sulphation occurs, regions which are monosulphated mainly on GlcNAc and further regions of high sulphation where both of the repeat disaccharides are sulphated. Each of these respective regions in the KS chain can be of variable length leading to KS complexity in terms of chain length and charge localization along the KS chain. Like other GAGs it is these variably sulphated regions in KS which define its interactive properties with ligands such as growth factors, morphogens and cytokines and which determine the functional properties of tissues containing KS. Further adding to KS complexity is the identification of three different linkage structures in KS to Asparagine (N-linked) or to Threonine or Serine residues (O-linked) in proteoglycan core proteins which has allowed the categorization of KS into 3 types, namely KS-I (corneal KS, Nlinked), KS-II (skeletal KS, O-linked) or KS-III (brain KS, O-linked). KS-I to III are also subject to variable addition of L-fucose and sialic acid groups. Furthermore, the GlcNAc residues of some members of the mucin-like glycoprotein family can also act as acceptor molecules for the addition of D-Gal and GlcNAc residues which can also be sulphated leading to small low sulphation glycoforms of KS. These differ from the more heavily sulphated KS chains found on proteoglycans. Like other GAGs, KS has evolved molecular recognition and information transfer properties over hundreds of millions of years of vertebrate and invertebrate evolution which equips them with cell mediatory properties in normal cellular processes and in aberrant pathological situations such as in tumourogenesis. Two KS-proteoglycans in particular, podocalyxcin and lumican are cell membrane, intracellular or stromal tissue associated components with roles in the promotion or regulation of tumour development, mucin-like KS-glycoproteins may also contribute to tumourogenesis. A greater understanding of the biology of KS may allow better methodology to be developed to more effectively combat tumourogenic processes.

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The Specificity of a Mouse Monoclonal Antibody to Human Aorta Proteoglycans

Cited by 11 publications

References 31 publications

Specificity of the low density lipoprotein-glycosaminoglycan interaction.

Specificity of the low density lipoprotein-glycosaminoglycan interaction.

Keratan sulfate, a complex glycosaminoglycan with unique functional capability

Keratan Sulphate in the Tumour Environment

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