scholarly journals An Immunohistochemical Study of the Rabbit Suprapatella, a Sesamoid Fibrocartilage in the Quadriceps Tendon Containing Aggrecan

2002 ◽  
Vol 50 (7) ◽  
pp. 955-960 ◽  
Author(s):  
T. Tischer ◽  
S. Milz ◽  
M. Maier ◽  
M. Schieker ◽  
M. Benjamin

The rabbit suprapatella is a sesamoid fibrocartilage in the deep surface of the tendon of vastus intermedius and an integral part of the knee joint. We report the presence of a variety of proteoglycans (aggrecan and versican), glycosaminoglycans (chondroitin 4 and 6 sulfate, dermatan sulfate, keratan sulfate) and glycoproteins (tenascin) in its extracellular matrix and the intermediate filament vimentin in the fibrocartilage cells. The most significant finding is the presence of aggrecan in the extracellular matrix, along with its associated link protein and several of its integral glycosaminoglycans. Aggrecan probably enables the suprapatella to withstand compression. Although it can be assumed that aggrecan metabolites detected in synovial fluid from some human joints are predominantly associated with articular hyaline cartilage, the presence of aggrecan in the rabbit suprapatella means that this cannot be assumed for all animal knee joints. We conclude that it is important for orthopedic researchers who use animal models for arthritis research to check for the presence of a suprapatella when joint fluid analyses are interpreted.

2020 ◽  
pp. 002215542094640 ◽  
Author(s):  
Sylvain D. Vallet ◽  
Olivier Clerc ◽  
Sylvie Ricard-Blum

The six mammalian glycosaminoglycans (GAGs), chondroitin sulfate, dermatan sulfate, heparin, heparan sulfate, hyaluronan, and keratan sulfate, are linear polysaccharides. Except for hyaluronan, they are sulfated to various extent, and covalently attached to proteins to form proteoglycans. GAGs interact with growth factors, morphogens, chemokines, extracellular matrix proteins and their bioactive fragments, receptors, lipoproteins, and pathogens. These interactions mediate their functions, from embryonic development to extracellular matrix assembly and regulation of cell signaling in various physiological and pathological contexts such as angiogenesis, cancer, neurodegenerative diseases, and infections. We give an overview of GAG–protein interactions (i.e., specificity and chemical features of GAG- and protein-binding sequences), and review the available GAG–protein interaction networks. We also provide the first comprehensive draft of the GAG interactome composed of 832 biomolecules (827 proteins and five GAGs) and 932 protein–GAG interactions. This network is a scaffold, which in the future should integrate structures of GAG–protein complexes, quantitative data of the abundance of GAGs in tissues to build tissue-specific interactomes, and GAG interactions with metal ions such as calcium, which plays a major role in the assembly of the extracellular matrix and its interactions with cells. This contextualized interactome will be useful to identify druggable GAG–protein interactions for therapeutic purpose:


1994 ◽  
Vol 42 (4) ◽  
pp. 513-522 ◽  
Author(s):  
A Asari ◽  
S Miyauchi ◽  
S Kuriyama ◽  
A Machida ◽  
K Kohno ◽  
...  

To demonstrate localization of hyaluronic acid (HA) in articular cartilage of the human femur, biotinylated HA-binding region, which specifically binds HA molecules, was applied to the tissue. In sections fixed by 2% paraformaldehyde-2% glutaraldehyde, HA staining was detected in lamina splendens and chondrocytes in the middle zone. By pretreatment with trypsin, intense HA staining appeared in the extracellular matrix of the deep zone and weak staining in the superficial and middle zones. Moreover, pre-treatment with chondroitinase ABC (CHase ABC) intensely enhanced the stainability for HA in the superficial and middle zones and weakly in the deeper zone. Combined pre-treatment of trypsin with CHase ABC abolished intra- and extracellular staining for HA in all zones. By microbiochemical study, the concentrations of HA and dermatan sulfate were high in the middle zone, whereas those of chondroitin sulfate and keratan sulfate were high in the deep zone. These results suggest that HA is abundantly synthesized in and secreted from the chondrocytes, particularly in the middle zone, whereas it is largely masked by proteoglycan constituents in the extracellular matrix.


1992 ◽  
Vol 40 (2) ◽  
pp. 275-282 ◽  
Author(s):  
S Byers ◽  
B Caterson ◽  
J J Hopwood ◽  
B K Foster

Monoclonal antibodies were used in this study to immunolocate glycosaminoglycans throughout the human growth plate. Chondroitin-4-sulfate, chondroitin-6-sulfate, and keratan sulfate were observed in the extracellular matrix of all zones of the growth plate and persisted into the cartilage trabeculae of newly formed metaphyseal bone. Also present in the extracellular matrix was an oversulfated chondroitin/dermatan sulfate glycosaminoglycan which appeared to be specific to the proliferative and hypertrophic zones of the growth plate. As with the other extracellular matrix molecules, this epitope persisted into the cartilage trabeculae of the metaphyseal bone. Zonal differences between the extracellular and pericellular or lacunae matrix were also observed. The hypertrophic chondrocytes appeared to synthesize chondroitin sulfate chains containing a non-reducing terminal 6-sulfated disaccharide, which were located in areas immediately adjacent to the cells. This epitope was not found to any significant extent in the other zones. The pericellular region around hypertrophic chondrocytes also contained a keratan sulfate epitope which was also observed in the resting zone but not in the proliferative zone. These cell-associated glycosaminoglycans were not found in the cartilage trabeculae of metaphyseal bone, indicating their removal as the terminal hypertrophic chondrocytes and their lacunae are removed by invading blood vessels. These changes in matrix glycosaminoglycan content, both in the different zones and within zones, indicate constant subtle alterations in chondrocyte metabolic products as they proceed through their life cycle of proliferation, maturation, and hypertrophy.


2021 ◽  
Vol 22 (11) ◽  
pp. 5708
Author(s):  
Kazadi N. Mutoji ◽  
Mingxia Sun ◽  
Garrett Elliott ◽  
Isabel Y. Moreno ◽  
Clare Hughes ◽  
...  

Corneal transparency relies on the precise arrangement and orientation of collagen fibrils, made of mostly Type I and V collagen fibrils and proteoglycans (PGs). PGs are essential for correct collagen fibrillogenesis and maintaining corneal homeostasis. We investigated the spatial and temporal distribution of glycosaminoglycans (GAGs) and PGs after a chemical injury. The chemical composition of chondroitin sulfate (CS)/dermatan sulfate (DS) and heparan sulfate (HS) were characterized in mouse corneas 5 and 14 days after alkali burn (AB), and compared to uninjured corneas. The expression profile and corneal distribution of CS/DSPGs and keratan sulfate (KS) PGs were also analyzed. We found a significant overall increase in CS after AB, with an increase in sulfated forms of CS and a decrease in lesser sulfated forms of CS. Expression of the CSPGs biglycan and versican was increased after AB, while decorin expression was decreased. We also found an increase in KS expression 14 days after AB, with an increase in lumican and mimecan expression, and a decrease in keratocan expression. No significant changes in HS composition were noted after AB. Taken together, our study reveals significant changes in the composition of the extracellular matrix following a corneal chemical injury.


2020 ◽  
Vol 79 (Suppl 1) ◽  
pp. 793.3-793
Author(s):  
M. A. Mortada ◽  
Y. A. Amer

Background:Calcific tendonitis is most commonly seen around shoulder joint. Few cases of quadriceps calcific tendonitis (QCT) of were reported. Routine use of ultrasonography in diagnosis of knee osteoarthritis has resulted in detection of many cases of QCT.Up to the best of our knowledge, this is the first study to detect impact of QCT in knee osteoarthritis by ultrasonography.Objectives:To compare pain, function, and clinical and radiological findings among primary KOA patients with or without ultrasonography-detected QCT.Methods:A prospective, observational study study was conducted on 214 patients with knee OA in the period between february 2019 to july 2019. Ultrasonography of knee joints was done according to EULAR guidelines. Quadriceps calcific tendonitis is defined as hyperechoic mass within the quadriceps tendon with posterior shadowing. The patients were categorized into two groups according to the presence or absence of QCT.Radiological grades of Kellgren–Lawrence were recorded. Pain and functional status was assessed by visual analog scale (VAS), Health Assessment Questionnaire-II (HAQ-II), and Western Ontario and McMaster Universities Osteoarthritis Index (WOMAC)Results:QCT were detected in 25 (11.6%) patients. Most cases of QCT were detected in vastus lateralis 18 (72%), then in vastus intermedius 5 (20%) and only 2 cases were detected in vastus medialis.QCT were detected mainly in advanced stages of knee OA; 22 cases of QCT were found in patients with grade 4 KOA.The presence of QCT was statistically significant related (P< 0.05*) with age, VAS, HAQ-II, WOMAC subscales, synovitis and effusion.Conclusion:Quadriceps calcific tendonitis is not rare. Ultrasonography can detect QCT in many cases with advanced knee OA. QCT is associated with increased pain and dysfunction in knee OAReferences:NoneDisclosure of Interests:None declared


2016 ◽  
Vol 157 (25) ◽  
pp. 995-999
Author(s):  
Gréta Varkoly ◽  
János Bencze ◽  
Tibor Hortobágyi ◽  
László Módis

The cornea is the first refractive element of the eye. The transparency of the cornea results from the regularly arranged collagen fibrils, forming lamellar structure and the leucin rich proteoglycans, which make interactions between the fibrils. The adult cornea consists mainly of fibril-forming collagens. The cornea has less amount of fibril associated and non-fibrillar collagens. The main proteoglycans of the cornea are keratan-sulfate proteoglycans and it also contains dermatan-sulfate proteoglycans. Disorders of the proteoglycan synthesis lead to the disruption of the unique pattern and result in thicker collagen fibrils. The abnormal structure of the extracellular matrix can generate corneal disorders and the loss of corneal transparency. Furthermore, proteoglycans and collagens have an important role in wound healing. In injury the keratocytes produce higher amounts of collagens and proteoglycans mediated by growth factors. Depending on the ratio of the cells and growth factors the extracellular matrix returns to normal or corneal scar tissue develops. Orv. Hetil., 2016, 157(25), 995–999.


2020 ◽  
Vol 79 (Suppl 1) ◽  
pp. 110.1-110
Author(s):  
S. Nysom Christiansen ◽  
F. C. Müller ◽  
M. Ǿstergaard ◽  
O. Slot ◽  
J. Møllenbach Møller ◽  
...  

Background:Dual energy CT (DECT) has diagnostic potential in gout patients. DECT can automatically colour-code presumed urate deposits based on radiodensity (Hounsfield Units, HU) and DECT ratio (difference in attenuation between high and low kV series) of lesions. However, other materials may imitate properties of urate deposits, most importantly calcium-containing material, dense tendons and artefacts, which may lead to misinterpretations. The characteristics of DECT lesions in gout patients have not yet been systematically investigated.Objectives:To evaluate the properties and locations of colour-coded DECT lesions in gout patients.Methods:DECT were performed in patients with suspected gout. Patients were separated into gout and non-gout patients based on joint fluid microscopy findings. DECT of the hands, knees and feet were performed using default gout settings and colour-coded lesions were registered. Only location-relevant lesions were analysed (e.g. nail bed artefacts excluded). Mean density (mean of HU at 80 kV and Sn150 kV), mean DECT ratio, size and location of each lesion was determined.Subgroup analysis was performed post-hoc evaluating potential differences in properties and locations of lesions. Lesions were separated into groups according to properties (Figure 1, grey box): 1)Size—to separate artefacts characterised by small volume (possible artefacts). 2)DECT ratios—to separate calcium-containing material characterised by high DECT ratio (possible calcium-containing material). 3)Density—to separate dense tendons characterised by low DECT ratio and low HU values (possible dense tendons). Lesion fulfilling all urate characteristics (large volume, low DECT ratio, high density) were labelleddefinite urate deposits. Finally, for non-gout patients, properties ofnon-gout urate-imitation lesions(properties asdefinite urate deposits) were analysed.Results:In total, 3918 lesions (all lesions) were registered in gout patients (n=23), with mean DECT ratio 1.06 (SD 0.13), median density 160.6 HU and median size 6 voxels (Figure 1, blue box). Lesions were seen in all analysed joints, most frequently MTP1 joints (medial side), knee joints and midtarsal joints (Figure 2a). Tendon affections were also common, especially in the knee tendons (patella and quadriceps), malleolus-related tendons (e.g. peroneus and tibialis posterior) and the Achilles tendons (Figure 2a).Subgroup analyses showed thatdefinite urate deposits(figure 2b) were found at the same locations asall lesionin gout patients (figure 2a), with the four most common sites being MTP1 joints, midtarsal joints, and quadriceps and patella tendons (Figure 2b).Possible dense tendonlesions had a mean HU value of 156.5 HU—markedly higher than expected for dense tendons (<100HU)—and lesion-locations were similar todefinite urate deposits(data not shown), indicating that they primarily consisted of true urate deposits. In contrast,possible calcium-containing materialandnon-gout urate-imitating lesionshad distinctly different properties (ratios 1.33 and 1.20, respectively) (Figure 1, yellow and orange box). Furthermore, the locations of these lesions were different fromdefinite urate depositssince they were primarily found in a few weight-bearing joints (knee, midtarsal and talocrural including malleolus regions) and tendons (Achilles and quadriceps), whereas no lesions were found in either MTP1 joints or patella tendons (figure 2c).Conclusion:DECT color-coded lesions in gout patients are heterogeneous in properties and locations. Subgroup analyses found that locations such as MTP1 joints and patella tendons were characterised by almost only showingdefinite urate deposits. A sole focus on these regions in the evaluation of gout patients may therefore improve specificity of DECT scans.Disclosure of Interests:Sara Nysom Christiansen Speakers bureau: SNC has received speaker fees from Bristol Myers Squibb (BMS) and General Electric (GE)., Felix C Müller Employee of: Siemens Healthineers., Mikkel Ǿstergaard Grant/research support from: AbbVie, Bristol-Myers Squibb, Celgene, Merck, and Novartis, Consultant of: AbbVie, Bristol-Myers Squibb, Boehringer Ingelheim, Celgene, Eli Lilly, Hospira, Janssen, Merck, Novartis, Novo Nordisk, Orion, Pfizer, Regeneron, Roche, Sandoz, Sanofi, and UCB, Speakers bureau: AbbVie, Bristol-Myers Squibb, Boehringer Ingelheim, Celgene, Eli Lilly, Hospira, Janssen, Merck, Novartis, Novo Nordisk, Orion, Pfizer, Regeneron, Roche, Sandoz, Sanofi, and UCB, Ole Slot: None declared, Jakob Møllenbach Møller: None declared, Henrik F Børgesen: None declared, Kasper K Gosvig: None declared, Lene Terslev Speakers bureau: LT declares speakers fees from Roche, MSD, BMS, Pfizer, AbbVie, Novartis, and Janssen.


2018 ◽  
Vol 475 (15) ◽  
pp. 2511-2545 ◽  
Author(s):  
Anthony J. Hayes ◽  
James Melrose

The aim of the present study was to examine the roles of l-fucose and the glycosaminoglycans (GAGs) keratan sulfate (KS) and chondroitin sulfate/dermatan sulfate (CS/DS) with selected functional molecules in neural tissues. Cell surface glycans and GAGs have evolved over millions of years to become cellular mediators which regulate fundamental aspects of cellular survival. The glycocalyx, which surrounds all cells, actuates responses to growth factors, cytokines and morphogens at the cellular boundary, silencing or activating downstream signaling pathways and gene expression. In this review, we have focused on interactions mediated by l-fucose, KS and CS/DS in the central and peripheral nervous systems. Fucose makes critical contributions in the area of molecular recognition and information transfer in the blood group substances, cytotoxic immunoglobulins, cell fate-mediated Notch-1 interactions, regulation of selectin-mediated neutrophil extravasation in innate immunity and CD-34-mediated new blood vessel development, and the targeting of neuroprogenitor cells to damaged neural tissue. Fucosylated glycoproteins regulate delivery of synaptic neurotransmitters and neural function. Neural KS proteoglycans (PGs) were examined in terms of cellular regulation and their interactive properties with neuroregulatory molecules. The paradoxical properties of CS/DS isomers decorating matrix and transmembrane PGs and the positive and negative regulatory cues they provide to neurons are also discussed.


Blood ◽  
1988 ◽  
Vol 72 (3) ◽  
pp. 903-912 ◽  
Author(s):  
BR Tomasini ◽  
DF Mosher

Abstract A difference in recognition of the adhesive glycoprotein vitronectin (also called S-protein, serum spreading factor, and epibolin) by monoclonal antibody 8E6 (Hayman EG, et al, Proc Natl Acad Sci USA 80:4003, 1983) was investigated using a competitive enzyme- immunosorbent assay and immunoaffinity chromatography. Recognition of vitronectin in serum was approximately 50-fold greater than recognition of vitronectin in plasma. Recognition of vitronectin incubated with heparin, thrombin-antithrombin III complex, or heparin and thrombin- antithrombin III complex together was 2.5-, 7-, or 32-fold greater, respectively, than recognition of vitronectin alone. Thrombin or antithrombin III by itself did not induce the antigenic change. Factor Xa-antithrombin III was less effective than thrombin-antithrombin III in induction of the change. Dextran sulfate and fucoidan were more potent than heparin in induction of the antigenic change, whereas dermatan sulfate, hyaluronic acid, heparan sulfate, chondroitin sulfate, or keratan sulfate were less effective. Immunoblotting analysis of serum and of vitronectin incubated with thrombin and antithrombin III demonstrated the presence of complexes composed of vitronectin and thrombin-antithrombin III that could only be dissociated with reducing agent. N-ethylmaleimide completely blocked the formation of the presumably disulfide-bonded complexes and partially blocked the antigenic change. Both non-disulfide-bonded and disulfide-bonded vitronectin bound to antibody-Sepharose from a mixture of vitronectin and thrombin-antithrombin III. Treatment of vitronectin with 8 mol/L urea resulted in enhanced recognition by the monoclonal antibody. Thus, the 8E6 antibody reacts with an epitope that is preferentially expressed by noncovalently and covalently linked vitronectin/thrombin-antithrombin III complexes and by urea-treated vitronectin. The change in vitronectin induced by thrombin-antithrombin III, therefore, is a physiological correlate of urea treatment and of adsorption of vitronectin onto tissue culture plastic (as is done in cell adhesion assays). The change may be important for expression of vitronectin activity.


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