Structure and functions of Glycosaminoglycans: a short review (with some personal scientific contributions)

Auteurs

  • Alberto Calatroni <strong>Accademia Peloritana dei Pericolanti, University of Messina, Italy </strong>

DOI :

https://doi.org/10.6092/1828-6550/APMB.108.2.2020.SD1

Mots-clés :

Glycosaminoglycans, Proteoglycans, Extracellular Matrix, Mucopolysaccharidoses, human plasma

Résumé

Abstract
This present article wishes to underline the strong contribution to both structure and functions of living bodies of a group of acidic polysaccharides, the Glycosaminoglycans (GAGs), usually covalently linked to proteins to give Proteoglycans (PGs): GAGs and PGs are structural components of connective tissues and of tissue extracellular matrix, also present on cell membrane surface and in secretory granules. Their basic structure is very simple: a linear repeat of disaccharide units, each composed of uronic acid and hexosamine moieties. However, except unsulphated high molecular weight Hyaluronan, they show very high structural heterogeneity, due to the chemical nature of both uronic acid and aminosugar components, the degree of monosaccharide sulphation, the distribution of O- and N-sulphate groups, the length of the chain and its copolymeric degree, the nature of interacting protein in PGs. So they are able to interact with a large variety of molecular structures, including matrix proteins, growth factors, cytokines and chemokines, and enzymes. Many functions in connective tissues are known GAG-depending. Many others in the body are expected. In this short review, to each one of the selected topics, GAGs synthesis, distribution, catabolism and related inborn errors, PGs functions, some personal scientific contributions will be recalled.

Références

Castellani, A.A., Calatroni, A., Righetti, P.G. (1967). UDP-xylose formation in cartilage. Ital J Biochem, 16: 5-11.


Calatroni, A, Donnelly, P.V., Di Ferrante, N. (1969). The glycosaminoglycans of human plasma. J Clin Invest, 48(2): 332-343. doi: 10.1172/JCl105989.


Pomin, V.H., Mulloy, B. (2018). Glycosaminoglycans and proteoglycans. Pharmaceuticals,11,27. doi:10.3390/ph11010027.

Paganini, C., Costantini, R., Superti-Furga, A., Rossi, A. (2019). Bone and connective tissue disorders caused by defects in glycosaminoglycan biosynthesis: a panoramic view. FEBS 286(15), doi.org/10.1111/febs.14984

Caterson, B. (2012) Fell-Muir Lecture: chondroitin sulphate glycosaminoglycans: fun for some and confusion for others. Int J Exp Path, 93(1): 1-10. doi: 10.1111/j.1365-2613.2011.00807.x.

Caon, I., Parnigoni, A., Viola, M., Karousou, E., Passi, A., Vigetti, D. (2020). Cell energy metabolism and Hyaluronan synthesis. J Histochem Cytochem. 22155420929772. doi: 10.1369/0022155420929772

Calatroni, A., Di Ferrante, N. (1968). Oversulfated dermatan sulfate extracted from Hurler spleen. Anal Biochem, 25(1): 370-378. doi: 10.1016/0003-2697(68)90111-5.

Coutinho, M.F., Lacerda, L., Alves, S. (2012). Glycosaminoglycan storage disorders: a review. Biochem Res Int ID 471325. doi: 10.1155/2012/471325.

Filocamo, M., Tomanin, R., Bertola, F., Morrone, A. (2018). Biochemical and molecular analysis in mucopolysaccharidoses: what a paediatrician must know. Ital J Paediat, 44: 129. doi: org/10.1186/s13052-018-0553-2.

Fecarotta, S., Tarallo, A., Damiano, C., Minopoli, N., Parenti, G. (2020). Pathogenesis of Mucopolysaccharidoses, an update. Int J Mol Sci 21: 2515. doi:10.3390/ijms21072515

Calatroni, A. (1972). Test for mucopolysaccharidoses: simple method for quantitative estimation of urinary glycosaminoglycans. Clin Chem, 18(3): 266-269. doi: org/10.1093/clinchem/18.3.266.

Tira, M.E., Calatroni, A., Balduini, C., Torri, G., Moretti, R., Casu, B. (1979). Structure of urinary glycosaminoglycans. Chemical and 1H-NMR characterization of heparan sulphates and dermatan sulphates from mucopolysaccharidoses type II, III and VI. Persp Inher Metabol Dis, 2, 165-183.

Calatroni, A., Pallavicini, G., Castellani, A.A. (1974). Aminosugar-containing low molecular weight acidic compounds present in urine of normal children and of patients affected by mucopolysaccharidoses type II, III or IV. Ital J Biochem, 23(3): 183-201.

Fraldi, A.,Serafini, M, Sorrentino N.C., Gentner, B., Aiuti, A., Bernardo M.E. (2018). Gene therapy for mucopolysaccharidoses:in vivo and ex vivo approaches. It J Pediat 44, 130. doi.org/10.1186/s13052-018-0565-y.

Calatroni, A., Di Ferrante, N. (1969). The glycosaminoglycans of human term placenta. Carbohydr Res, 10: 535-548.

Ferlazzo, A.M., Vinci, R., Panzera, M., Ferlazzo, A., Calatroni, A. (1991). Glycosaminoglycan concentration in horse plasma and serum. Differences with other animal species and identification of affecting factors. Comp Biochem Physiol, 100B(4): 745-751. doi: 10.1016/0305-049(91)90284-k.

Calatroni, A., Vinci, R., Ferlazzo, A.M. (1992). Characteristics of the interactions between acid glycosaminoglycans and proteins in normal human plasma as revealed by the behavior of the protein-polysaccharide complexes in ultrafiltration and chromatographic procedures. Clin Chim Acta, 206(3):167-180. doi: 10.1016/0009-8981(92)90086-6.

Muraca, U., Vinci, R., Ferlazzo, A.M., Muraca, G., Calatroni, A. (1992).Factors affecting glycosaminoglycan concentration in normal human plasma. Ital J Biochem, 41(3), 159-169.

Calatroni, A., Avenoso, A., Ferlazzo, A.M., Lindner, A., Campo, G.M. (2008). Transient increase with strenous exercise of plasma levels of glycosaminoglycans in human and horses. Conn Tissue Res, 49: 416-425. doi: org/10.1080/03008200802324949.

Calabrò, L., Musolino, C., Spatari, G., Vinci, R., Calatroni, A. (1998). Increased concentration of circulating acid glycosaminoglycans in chronic lymphocytic leukaemia and essential thrombocythaemia. Clin Chim Acta, 269 (2): 185-199. doi: 10.1016/s0009-8981(97)00200-3

Campo, S., Campo, G.M., Avenoso, A., D’Ascola, A., Musolino, C., Calabro’, L., Bellomo, G., Quartarone, E., Calatroni, A. (2006). Lymphocytes from patients with early stage of B-cell chronic lymphocytic leukaemia and long survival synthesize decorin. Biochemie, 88(12): 1933-39. doi: 10.1016/j.biochi.2006.07.010.

Sainio A.O., Jarvelainen, H.T. (2018). Decorin-mediated oncosuppression – a potential future adjuvant therapy for human epithelial cancers. doi.org/10.1111/bph.14180.

Campo, G.M., Campo, S., Ferlazzo, A.M., Calatroni, A. (2001). Improved HPLC method to estimate aminosugars and its application to glycosaminoglycan determination in plasma and serum. J Chromatogr B, 765(2): 151-160. doi: 10.1016/s0378-4347(01)00427-3.

Chen, S., Birk, D.E. (2013). The regulatory roles of small leucine-rich proteoglycans in extracellular assembly. FEBS J., 280(10): 2120-2137. doi: 10.1111/febs.12136.

Schafer, L., Iozzo, R.V. (2008). Biological functions of the small leucine-rich proteoglycans: from genetics to signal transduction. J Biol Chem, 283: 21305-21309. doi: 10.1074/jbc.R800020200

Scott, J.E. (2008). Cartilage is held together by elastic glycan strings. Physiological and pathological implications. Biorheology, 45(3-4): 209-17. doi10.3233/BIR-2008-0477

Sarrazin, S., Lamanna, W.C., Esko, J.D. (2011). Heparan sulfate proteoglycans. Cold Spring Harb Perspect Biol, 3:a004952. doi: 10.1101/cshperspect.a004952

Korpetinou, A., Skandalis, S.S., Labropoulou, V.T., Smirlaki, G., Noulas, A., Karamanos, N., Theocharis, A.D. (2014). Serglycin: at the crossroad of inflammation and malignancy. Front Oncol, 3:327. doi: 10.3389/fonc.2013.00327

Gondelaud, F., Ricard-Blum, S. (2019). Structure and interactions of syndecans. FEBS J 286(15) 2994-3007. doi: 10.1111/febs.14828

Afratis, N.A., Nikitovic, D., Multhaupt, H., Theocharis, A.D., Couchman, J.R., Karamanos, N. (2017). Syndecans-key regulators of cell signaling and biological functions. FEBS J., 284(1): 27-41. doi 10.1111/febs. 13940

Gopal, S. (2020) Syndecans in inflammation at a glance. Front Immunol, 11: 227. doi: 10.3389/fimmu.2020.00227

Montalbano, M., Georgiadis, G., Masterson, A.L., McGuire, J.T., Prajapati. J., Shirafkan, A., Rastellini, C., Cicalese, L. (2017). Biology and function of glypican-3 as a candidate for early cancerous transformation of hepatocytes in hepatocellular carcinoma (Review). Oncol Rep, 37(3): 1291-1300. doi.org/10.3892/or.2017.5387

Senbanjo, L.T., Chellaiah, M.A. (2017). CD44: a multifunctional cell surface adhesion receptor is a regulator of progression and metastasis of cancer cells. Cell Develop Biol, 5:18 doi: 10.3389/fcell.2017.00018

Campo, G.M., Avenoso, A., Campo, S., Nastasi, G., Traina, P., D’Ascola, A., Calatroni, A. (2008). Chondroitin-4-sulphate reduced oxidative injury in cerulei-induced pancreatitis in mice. The involvement of NF-kB trans location and apoptosis activation. Exp Biol Med, 233: 741-752. doi: 10.3181/0711-RM-318.

Campo, G.M., Avenoso, A., Nastasi, G., Micali, A., Prestipino, V., Vaccaro, M., D’Ascola, A., Calatroni, A., Campo, S. (2011). Hyaluronan reduces inflammation in experimental arthritis by modulating TLR-2 and TLR-4 cartilage expression. Biochim Biophys Acta, 1812 (9): 1170-1181 doi: 10.1016/bbadis.2011.06006.

Avenoso, A., D’Ascola, A., Scuruchi, M., Mandraffino, G., Calatroni, A., Saitta, A., Campo, S., Campo, G.M. (2018) Hyaluronan in the experimental injury of the cartilage: biochemical action and protective effects. Inflamm Res 67: 5-20. doi:10.1007/s00011-017-1084-9.

Scuruchi, M., D’Ascola, A, Avenoso, A., Mandraffino, G., Campo, S., Campo, G.M. (2019) Serglycin as part of IL-1beta induced inflammation in human chondrocytes. Arch Biochem Biophys 669: 80-86. doi: 10.1016/j.abb.2019.05.021.

Téléchargements

Publiée

2020-12-22

Numéro

Rubrique

SCHOLARLY DIALOGS