Proteoglycans of Wharton’s jelly

Gogiel, Tomasz; Bańkowski, Edward; Jaworski, Stefan

doi:10.1016/s1357-2725(03)00128-6

Cited by 44 publications

(34 citation statements)

References 22 publications

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“…20,[31][32][33][34] The distribution of ECM proteins in Wharton's jelly has been examined using immunofluorescent imaging, demonstrating that collagen types I, II, and VI are homogeneously distributed throughout the entire layer of Wharton's jelly, enmeshed with fibrils of collagen type III and type IV, as well as laminin and heparan sulfate proteoglycans. 32 Collagen has been found to be the major matrix protein in Wharton's jelly, with the total content of collagen reported to be approximately 550 mg=g, or approximately 50% of the dry weight of defatted Wharton's jelly.…”

Section: Discussionmentioning

confidence: 99%

“…Significant amounts of sulfated GAGs have also been found in Wharton's jelly, forming predominantly chondroitin sulfate and dermatan sulfate proteoglycans, including decorin, biglycan, and versican. 31,34 These proteoglycans affect the matrix network organization of collagen fibrils and contribute to cell-cell and cell-ECM interactions. For example, decorin and biglycan co-regulate the diameter and organization of collagen fibrils, whereas versican can assist with the growth and proliferation of cells, destabilizing their adhesion to the ECM.…”

Section: Discussionmentioning

confidence: 99%

“…For example, decorin and biglycan co-regulate the diameter and organization of collagen fibrils, whereas versican can assist with the growth and proliferation of cells, destabilizing their adhesion to the ECM. 31,34 These proteoglycans also form a reservoir for binding a variety of growth factors, such as FGF, TGF-b1, PDGF, and EGF, to regulate cellular proliferation, differentiation, and homeostasis of other ECM proteins in the vocal fold lamina propria. 16,20 Together with HA, these proteoglycans likely contributed to the observed optimal viscoelastic properties of the acellular HUV construct and the recellularized scaffold as well.…”

Section: Discussionmentioning

confidence: 99%

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The Human Umbilical Vein with Wharton's Jelly as an Allogeneic, Acellular Construct for Vocal Fold Restoration

Chan

Rodriguez²,

McFetridge³

2009

Tissue Engineering Part A

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This study investigated the potential of the decellularized human umbilical vein (HUV) as an allogeneic, acellular extracellular matrix (ECM) scaffold for engineering the vocal fold lamina propria in vitro. HUV specimens with Wharton's jelly on the abluminal surface were uniformly dissected from native umbilical cords using an automated procedure and subjected to a novel saline-based decellularization treatment for removal of potentially antigenic epitopes. Human vocal fold fibroblasts from primary culture were seeded onto the resulting acellular constructs and cultured for 21 days. The structures of decellularized and fibroblast-repopulated HUV constructs and the attachment, proliferation, and infiltration of fibroblasts were examined with light microscopy and scanning electron microscopy. Changes in the relative densities of collagen in the constructs associated with decellularization and recellularization were quantified using digital image analysis. In addition, fibroblasts infiltrating the scaffolds were released by cell recovery and quantified by counting. Viscoelastic properties of the scaffolds were measured using a linear, simple-shear rheometer at phonatory frequencies. Results showed that an acellular ECM construct with an intact three-dimensional structure of Wharton's jelly was fabricated. Vocal fold fibroblasts readily attached on the abluminal surface of the construct with high viability, with significant cellular infiltration up to approximately 600 mm deep into the construct. A significant increase in collagen expression was observed with recellularization. The elastic modulus and dynamic viscosity of the fibroblast-repopulated scaffolds were comparable to those of the human vocal fold lamina propria. These findings supported the potential of the construct as a possible surgical allograft for vocal fold restoration and reconstruction.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

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The Human Umbilical Vein with Wharton's Jelly as an Allogeneic, Acellular Construct for Vocal Fold Restoration

Chan

Rodriguez²,

McFetridge³

2009

Tissue Engineering Part A

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“…epithelial (Figure 8a), endothelial, and smooth muscle (results not shown). There was also significant staining throughout Wharton's jelly (Figure 8a), the highly hydrated matrix composed of many types of collagens and GAGs [41].…”

Section: Light-and Electron-microscopic Localization Of Type XV Collamentioning

confidence: 99%

The molecular structure of human tissue type XV presents a unique conformation among the collagens

Myers

Amenta

Dion

et al. 2007

Biochemical Journal

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Establishing the structure of the non-fibrillar collagens has provided a unique perspective to understanding their specialized functions in the extracellular matrix. These proteins exhibit very diverse conformations and supramolecular assemblies. Type XV collagen is a large macromolecule distinguished by a highly interrupted collagenous domain and many utilized sites of attachment for CS (chondroitin sulfate) and HS (heparan sulfate) glycosaminoglycan chains. It is present in most basement membrane zones of human tissues, where it is found closely associated with large collagen fibrils. To determine the molecular shape and organization of type XV, the protein was purified from human umbilical cords by salt extraction, and by ion-exchange and antibody-affinity chromatography. The representation of type XV in one of its most abundant tissue sources is estimated at only (1-2) × 10 −4 % of dry weight. The molecules examined by transmission electron microscopy after rotary shadowing were visualized in multiple forms. Relatively few type XV monomers appeared elongated and kinked; most molecules were found in a knot/figure-of-eight/pretzel configuration not previously described for a collagen. Collective measurements of these populations revealed an average length of 193 + − 16 nm. At the N-terminal end, identified by C-terminal antibody binding, were three 7.7 nm-diameter spheres, corresponding to TSPN-1 (Nterminal module of thrombospondin-1) modules, and attached to the collagen backbone by a short linker. The type XV monomers show the ability to self-assemble into higher-order structures. Some were arranged in complex clusters, but simpler oligomers, which may represent intermediates, were observed in a cruciform pattern with intermolecular binding sites that probably originate in the interruption sequences. The morphology of type XV is thus the antithesis of the fibrillar collagens, and the shape attains the required flexibility to form the spectrum of interconnecting links between banded fibrils at the basement membrane/interstitial border. These type XV structures may act as a biological 'spring' to stabilize and enhance resilience to compressive and expansive forces, and the multimers, in particular, with selective complements of many localized CS and HS chains, may be instrumental in spatial and temporal recruitment of modulators in growth, development and pathological processes.

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“…Since Wharton's jelly contains a low number of cells and very high amounts of ECM components, it may be concluded that the scanty cells are strongly stimulated to produce large amounts of collagen [1] , hyaluronate [5] and sulphated proteoglycans [6] . It is well known that the biosynthesis of ECM components is enhanced by several PGFs -mainly insulin-like growth factor [7] , fibroblast growth factor [8] and transforming growth factor-␤ [9] .…”

Section: Introductionmentioning

confidence: 99%

Altered Sphingolipid Composition in Wharton’s Jelly of Pre-Eclamptic Newborns

Romanowicz

Bańkowski²

2010

Pathobiology

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Objectives: Wharton’s jelly is a myxomatous substance surrounding the umbilical cord (UC) vessels to protect them against extension, bending, twisting and compression. Pre-eclampsia (hypertension, oedema, proteinuria) is the most common pregnancy-associated pathological syndrome. It is accompanied by significant alterations in UC composition. Here we describe the sphingolipids of Wharton’s jelly from 10 newborns delivered by healthy mothers and from 10 babies of pre-eclamptic mothers. Methods: Thin-layer chromatography, solid-phase extraction and high-performance liquid chromatography were employed. Results: Control tissues were abundant in sphingomyelins (Sms) and ceramides (Cers), whereas the amounts of sphingoid bases were distinctly lower. Pre-eclampsia is associated with a significant increase in Sms, Cers, sphingosine, sphinganine, 4-OH-sphinganine, sphingosine 1-phosphate and glycosylated sphingosine. Furthermore, a decrease in sphinganine 1-phosphate was found. Stearate (C_18:₀) is the dominating fatty acid in Sms and Cers of control tissue. In contrast, pre-eclamptic material contained the highest amount of laurate (C_12:₀) in Sms and myristoleate (C_14:₁) in Cers. Conclusions: Sphingolipids and some sphingoid bases are bioactive molecules which contribute to the regulation of signal transduction pathways, protein sorting and mediation of cell-to-cell interactions and recognition. The alteration in sphingolipid content may modify the metabolism of Wharton’s jelly, resulting in remodelling of its composition.

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Proteoglycans of Wharton’s jelly

Cited by 44 publications

References 22 publications

The Human Umbilical Vein with Wharton's Jelly as an Allogeneic, Acellular Construct for Vocal Fold Restoration

The Human Umbilical Vein with Wharton's Jelly as an Allogeneic, Acellular Construct for Vocal Fold Restoration

The molecular structure of human tissue type XV presents a unique conformation among the collagens

Altered Sphingolipid Composition in Wharton’s Jelly of Pre-Eclamptic Newborns

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