| Chondroitin Sulfate The Miracle Ingredient In A Calcium Supplement |
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This One Takes |
| Chondroitin Sulfate The Miracle Ingredient In A Calcium Supplement |
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This One Takes |
The reference was:
The word chondrotin comes from the root chondro- which means a word related to cartilage. The full word, chondrotin has a complex chemical definition, but let’s leave it here that when you add some of this material to your "calcium" formula, the matrix becomes more capable of attracting and holding the hunks of calcium.
Chondroitin sulfate (ester) occurs in three forms: A composed of glucuronic acid and sulfated galactosamine, B in which the uronic acid constituent is replaced by L-iduronic acid, and C which differs from chondroitin sulfate B in the position of the sulfate on the galactosamine residue. They are widespread in connective tissues, particularly cartilage. from: Dorland’s Medical Dictionary.
and
chon·dro·i·tin sulfate (kòn-dro¹î-tîn) noun
One of several classes of sulfated glycosaminoglycans that is a major constituent in various connective tissues, especially in the ground substance of blood vessels, bone, and cartilage.
[From chondroitic acid, an acid occurring in cartilage.]
Note that this substance, chondroitin sulfate, is far more expensive as an ingredient than even the very exotic calcium, hydroxy apatite. If you really want a calcium formula which wil reverse osteoporisis, make sure that it contains chondroitin sulfate. Since practically noone, other than research scientists know about this substance, a supplement manufacturer will normally not put it in his formula. It adds greatly to the cost and does not add to its sales appeal!
There are several scientific studies mentioning this substance below.
The effect of bone matrix on young connective tissue cells in culture.
Ainsworth T; Puzic O; Anastassiades T
J Lab Clin Med, 89: 4, 1977 Apr, 781-91
Human and rat decalcified bone matrix preparations were shown to be active in inducing cartilage formation by subcutaneous implantation in the rat. When young rat fibroblastic cells were grown in cultures, which also contained bone matrix preprations in particulate form, the fibroblastic cells underwent a uniform and consistent morphological alteration. These altered cells showed higher rates of synthesis of hyaluronic acid and chondroitin sulfate than the controls and exhibited very active amino-sugar-nucleotide metabolism. It is suggested that this approach to the culture of connective tissue cells will allow a more precise definition of the early steps of connective tissue differentiation.
English
77142783
Bone Matrix [*PH]
Connective Tissue [*CY/*ME]
Glycosaminoglycans [*BI]
Animal
Cartilage
Cells, Cultured
Chondroitin Sulfates [BI]
Human
Hyaluronic Acid [BI]
Morphogenesis
Rats
JOURNAL ARTICLE
0022-2143
UNITED STATES
Newer knowledge of skeletogenesis: macromolecular transitions in the extracellular matrix.
Toole BP; Linsenmayer TF
Clin Orthop, 129, 1977 Nov-Dec, 258-78
Morphogenesis of skeletal tissues is accompanied by dramatic changes in the types and amounts of extracellular macromolecules synthesized. These changes correlate with the morphological and structural characteristics of each tissue type involved in skeletogenesis, viz. mesenchyme, cartilage and bone. At the beginning of skeletogenesis, a hyaluronate-rich extracellular matrix may provide a beneficial milieu for mesenchymal cell migration and proliferation, and prevent precocious differentiation. This matrix also contains type I collagen and possibly a unique sulfated proteoglycan. Cartilage differentiation, during endochondral osteogenesis, involves the removal of hyaluronate and the production of large amounts of type II collagen and a characteristic chondroitin sulfate-proteoglycan. Further complex transitions in arrangement and concentration of proteoglycan occur in the epiphyseal growth plate followed by sudden depletion at the site of initiation of bone formation. In addition, at this site, the type of collagen synthesized reverts from type II back to type I. Bone formation at periosteal sites also involves removal of proteoglycan. The collagen component of both osteoid and bone matrix is type I but the level of hydroxylation of lysine moieties may be significantly higher in osteoid. It is proposed that changes in extracellular matrix composition are important factors in the control of morphogenesis as well as in providing suitable structural properties to the developing skeletal tissues.
English
78125968
Osteogenesis
Animal
Bone Matrix [EM]
Cartilage [CY/EM/PH]
Chemistry
Chick Embryo
Collagen [ME/PH]
Extremities [EM]
Glycosaminoglycans [ME]
Human
Hyaluronic Acid [PH]
Macromolecular Systems
Morphogenesis
Proteoglycans [PH]
Support, U.S. Gov't, P.H.S.
JOURNAL ARTICLE
REVIEW
0009-921X
UNITED STATES
232
The effect of solubilized bone matrix fractions from different mammalian species on glycosaminoglycan synthesis by cultured fibroblasts.
Anastassiades T; Irwin D; Woods A; Robertson W
Comp Biochem Physiol [B], 79: 4, 1984, 623-31
Human and bovine bone matrices were extracted with salt solutions of different composition and the extracts tested for stimulation of incorporation of radioactivity from [3H]glucosamine and [35S]SO4 into the hyaluronic acid and chondroitin sulfate of the cell pellet, the cell surface and the medium fractions of human synovial cells in culture. Stimulatory activity was extracted with a solution of 0.3 M EDTA in 2.5 M NaCl from bovine but not human bone. Subsequent extraction of the residues with 4 M guanidinium hydrochloride yielded activity from both matrices. A major stimulation of incorporation of radioactivity was observed in the cell surface fractions. Human synovial cells constitute a more sensitive assay system for the stimulatory activity than rabbit synovial cells.
English
85100228
Bone Marrow [*PH]
Glycosaminoglycans [*BI]
Synovial Membrane [*ME]
Tissue Extracts [*PD]
Animal
Cattle
Cells, Cultured
Chondroitin Sulfates [BI]
Comparative Study
Fibroblasts [DE/ME]
Glucosamine [ME]
Human
Hyaluronic Acid [BI]
Kinetics
Rats
Solubility
Species Specificity
Sulfates [ME]
Sulfur Radioisotopes [DU]
Support, Non-U.S. Gov't
Tritium [DU]
JOURNAL ARTICLE
0305-0491
ENGLAND
0 (Glycosaminoglycans)
0 (Sulfates)
0 (Sulfur Radioisotopes)
0 (Tissue Extracts)
10028-17-8 (Tritium)
3416-24-8 (Glucosamine)
9004-61-9 (Hyaluronic Acid)
9007-28-7 (Chondroitin Sulfates)
Proteoglycans of developing bone.
Fisher LW; Termine JD; Dejter SW Jr; Whitson SW; Yanagishita M; Kimura JH; Hascall VC; Kleinman HK; Hassell JR; Nilsson; B
J Biol Chem, 258: 10, 1983 May 25, 6588-94
We purified and characterized the bone proteoglycans from fetal calves, growing rats, and human fetuses. The major proteoglycan is part of the mineralized tissue matrix and only 10-20% can be extracted prior to demineralization. This bone proteoglycan is a small glycoconjugate (Mr = 80,000-120,000) containing approximately 20-30% protein and either one or two chondroitin sulfate chains (Mr = 40,000) attached to a relatively monodisperse protein core (Mr = 38,000). "O"-linked and "N"-linked oligosaccharide units are also present. Antibodies directed against the protein core of calf bone proteoglycan do not cross-react with cartilage, skin, corneal, or basement membrane proteoglycans in immunoassays and have minimal cross-reactivity with scleral proteoglycans. Quantitative immunoassays and indirect immunofluorescence were used to show that the molecule is localized to forming bone trabeculae and dentin, but not to any other tissue. Osteoblasts and osteoprogenitor cells adjacent to areas undergoing rapid osteogenesis also contain this small proteoglycan. A second proteoglycan (Mr approximately equal to 1,000,000) was extracted from newly forming bone prior to demineralization. This large proteoglycan, which was isolated from the cartilage-free areas of developing intramembranous bone, has a protein core similar to that of the cartilage aggregating proteoglycan and cross-reacts with antisera raised against these cartilage proteoglycans but not with the small mineral-entrapped proteoglycan. It contains larger (Mr = 40,000) and fewer chondroitin sulfate chains than its cartilage-derived analogue, and is localized to the soft connective tissue mesenchyme lying between growing bone trabeculae. More fully formed compact bone did not contain detectable quantities of this proteoglycan.
English
83213372
Bone and Bones [AN/*EM]
Bone Development
Proteoglycans [IM/IP/*ME]
Animal
Bone Matrix [AN]
Cartilage [AN]
Cattle
Epitopes [IM]
Human
Immunoassay
Minerals [ME]
Molecular Weight
Oligosaccharides [AN]
Support, Non-U.S. Gov't
JOURNAL ARTICLE
0021-9258
UNITED STATES
0 (Epitopes)
0 (Minerals)
0 (Oligosaccharides)
0 (Proteoglycans)
Scanning electron microscopy studies of collagen, mineral and ground substance in human cortical bone.
Frasca P; Harper RA; Katz JL
Scan Electron Microsc, Pt 3, 1981, 339-46
This paper presents scanning electron microscopy (SEM) observations made on the collagen, mineral and ground substance components comprising human cortical bone, which to a very large extent have been made possible by a sample preparation technique which takes advantage of the fracture propagation behavior inherent to the mature, highly heterogeneous, lamellar cortical bone tissue. By varying the extent to which bone samples are decalcified, it is possible to study certain morphological aspects of all these three main components of bone. Collagen features observable at fairly low magnification (approximately 1000x) include collagen bundle orientations with respect to the long axis of bone or of the osteon samples and collagen bundle morphological interrelationships. Much higher magnifications (approximately 20,000x) reveal spherical structures attached to the collagen fibrils which comprise the fiber bundle. Ground substance, yet to be identified biochemically, was noted in so-called interlamellar regions of osteons and of periosteal and endosteal tissue as well as in resting lines, cement lines and hypercalcified rings. It was observed to contain sulfur and to be trypsin soluble, providing evidence for the presence of a noncollagenous protein and of chondroitin sulfate which may be biochemically related in a protein polysaccharide complex. Such conclusion does not, however, preclude the presence of other ground substance components in this observed material. Large concentrations of mineral were noted in the interlamellar region of osteons and of periosteal and endosteal bone. This mineral does not seem to be directly associated with collagen. This study involves the use of scanning electron microscopy in both the secondary and back-scattered electron detection modes and energy dispersive x-ray microanalysis (XMA).
English
82128969
Bone and Bones [*UL]
Collagen
Bone Matrix [UL]
Calcification, Physiologic
Human
Microscopy, Electron, Scanning
Support, Non-U.S. Gov't
Support, U.S. Gov't, P.H.S.
JOURNAL ARTICLE
0586-5581
UNITED STATES
9007-34-5 (Collagen)
Heparan sulfate is necessary for adhesive interactions between human early hemopoietic progenitor cells and the extracellular matrix of the marrow microenvironment.
Gordon MY; Riley GP; Clarke D
Leukaemia Research Fund Centre, Institute of Cancer Research, London, U.K.
Leukemia, 2: 12, 1988 Dec, 804-9
Human hemopoietic blast colony-forming cells (BI-CFCs) recognize and adhere to the extracellular matrix (ECM) produced by marrow-derived stromal cells in vitro. We have investigated the requirements for this interaction by testing the capacity of BI-CFCs to adhere to ECM components under a variety of conditions. Binding was prevented completely by prior treatment of stromal ECM with nitrous acid, in large part by treatment with heparitinase or hyaluronidase, and slightly by treatment with chondroitinases. Whereas heparan sulfate isolated from marrow stromal cultures effectively blocked binding, heparan sulfate from bovine kidney did not. Chondroitin sulfate and hyaluronic acid did not have any effect in this test. In contrast, collagen was not sufficient for the interaction because dishes coated with collagen type I or IV did not act as adhesive surfaces for BI-CFCs. Ligands for integrin receptors (e.g., fibronectin) did not participate in BI-CFC binding because the synthetic pentapeptide glycine-arginine-glycine-asparagine-serine did not compete with stroma in binding BI-CFCs. These findings indicate that heparan sulfate in the bone marrow microenvironment is necessary for BI-CFC binding to ECM and may contribute to localizing hemopoietic stem cells in hemopoietic tissue.
English
89069663
Antigens, Surface [*PH]
Bone Marrow [*CY]
Cell Adhesion [*DE]
Extracellular Matrix [DE/*PH]
Glycosaminoglycans [*PH]
Hematopoietic Stem Cells [DE/*PH]
Heparitin Sulfate [*PH]
Binding, Competitive
Cells, Cultured
Human
Oligopeptides [ME]
Protein Binding
Support, Non-U.S. Gov't
JOURNAL ARTICLE
0887-6924
UNITED STATES
0 (Antigens, Surface)
0 (Cell Adhesion Molecules)
0 (Glycosaminoglycans)
0 (Oligopeptides)
9050-30-0 (Heparitin Sulfate)
96426-21-0 (glycyl-arginyl-glycyl-aspartyl-serine)
Extracellular matrix alterations during endochondral ossification in humans.
Horton WA; Machado MM
Department of Pediatrics, University of Texas Medical School, Houston.
J Orthop Res, 6: 6, 1988, 793-803
Immunohistochemical methods were employed to examine alterations in the cartilage extracellular matrix constituents associated with endochondral ossification in humans. The distributions of chondroitin 4- and 6-sulfate and keratan sulfate proteoglycan (PG) determinants, cartilage PG link protein, collagen types I and II, and fibronectin were determined in iliac crest growth-plate specimens using the avidin-biotin-horseradish peroxidase system. Collagen type II was distributed throughout the growth plate, providing a framework within which chondrocytes divided and formed clusters of differentiating (hypertrophic) cells. The septa between these clusters and their subchondral extensions into underlying bone trabeculae were rich in PG, PG link protein, and collagen type II and resembled the extracellular matrix of reserve cartilage. The territorial matrix associated with the differentiating cells within the clusters contained reduced amounts of collagen type II, PG link protein, and possibly cartilage PG. Collagen type I and fibronectin were detected within the cytoplasm of the maturing and degenerating cells, and fibronectin localized intensely to the pericellular matrix envelopes of these cells. These alterations presumably facilitate the degradation of the matrix associated with the cell clusters by invading vascular tissue, while the septa, which retain the characteristics of more typical cartilage matrix, are not degraded and firmly anchor the cartilage to the subchondral bone.
English
89011134
Extracellular Matrix [ME/*PH/UL]
Growth Plate [CY/ME/*PH]
Osteogenesis
Adolescence
Child
Child, Preschool
Collagen [CL/ME]
Fibronectins [ME]
Human
Immunohistochemistry
Proteins [ME]
Proteoglycans [ME]
Staining
Support, Non-U.S. Gov't
Support, U.S. Gov't, P.H.S.
Tissue Distribution
JOURNAL ARTICLE
0736-0266
UNITED STATES
0 (link proteins)
0 (Fibronectins)
0 (Proteoglycans)
9007-34-5 (Collagen)
Structural characterization of human alveolar bone proteoglycans.
Waddington RJ; Embery G
Department of Basic Dental Science, Dental School, University of Wales College of Medicine, Heath Park, Cardiff, U.K.
Arch Oral Biol, 36: 12, 1991, 859-66
Proteoglycans were extracted from EDTA-demineralized human alveolar bone under dissociative conditions using 4 M guanidinium chloride in the presence of protease inhibitors. The extract was further purified by anion-exchange chromatography on DEAE-Sephacel, using a step-wise salt gradient. The proteoglycan-rich fraction was analysed for carbohydrate, protein and amino acid composition and molecular size by SDS-PAGE. Glycosaminoglycan content was determined by cellulose acetate electrophoresis after proteolysis. The sulphate isomers of the glycosaminoglycans were confirmed by Fourier-transformed infra-red spectroscopy. Two chondroitin sulphate-proteoglycan species were identified with molecular weights of 79 and 55-65 kDa, respectively. The core proteins had molecular weights of 49 kDa for both proteoglycans, with the amino acid content rich in glycine, leucine, glutamate and aspartate. The chondroitin sulphate chains were mainly as the 4-sulphate isomer forms although low but detectable amounts of 6-sulphate isomer were also present.
English
92117879
Alveolar Process [*CH]
Proteoglycans [*AN/CH]
Aspartic Acid [AN]
Bone Matrix [CH]
Chondroitin Sulfates [AN]
Chromatography, Ion Exchange
Electrophoresis, Cellulose Acetate
Electrophoresis, Polyacrylamide Gel
Fourier Analysis
Glutamates [AN]
Glycine [AN]
Glycosaminoglycans [AN]
Hexosamines [AN]
Hexoses [AN]
Human
Leucine [AN]
Molecular Weight
Sodium Dodecyl Sulfate
Spectrophotometry, Infrared
Uronic Acids [AN]
JOURNAL ARTICLE
0003-9969
ENGLAND
0 (Glutamates)
0 (Glycosaminoglycans)
0 (Hexosamines)
0 (Hexoses)
0 (Proteoglycans)
0 (Uronic Acids)
151-21-3 (Sodium Dodecyl Sulfate)
56-40-6 (Glycine)
56-84-8 (Aspartic Acid)
56-86-0 (Glutamic Acid)
7005-03-0 (Leucine)
9007-28-7 (Chondroitin Sulfates)
The clones of osteoarthritic cartilage.
Mitchell N; Lee ER; Shepard N
Division of Orthopaedics, McGill University Shriners Hospital for Crippled Children, Montreal, Quebec, Canada.
J Bone Joint Surg [Br], 74: 1, 1992 Jan, 33-8
We studied the early cartilage changes in osteoarthritis, examining the most normal appearing articular cartilage from the hips of 17 patients. Normal appearing cartilage from five patients treated for fractures was used as control material. Two different types of clone were found. The first had increased staining for proteoglycan and was thought to have been engaged in the synthesis of matrix. The other type was associated with a severe deficiency of proteoglycan, matrix streaks and evidence of degradation and phagocytosis of matrix components. Immunohistochemistry demonstrated large amounts of chondroitin 4 and 6 sulphate about the synthetic-type clones, and little or no reactivity about the degenerative clones which lay more superficially and were associated with matrix destruction. Clones appeared to be engaged in either matrix synthesis or its destruction. The disease process of osteoarthritis appeared to begin at the surface of the articular cartilage.
English
92121209
Cartilage, Articular [ME/*UL]
Osteoarthritis, Hip [ME/*PA]
Aged
Antibodies, Monoclonal
Chondroitin Sulfates [ME]
Clone Cells [ME/UL]
Extracellular Matrix [ME/UL]
Femur Head
Human
Immunohistochemistry
Microscopy, Electron
Middle Age
Proteoglycans [ME]
Support, Non-U.S. Gov't
JOURNAL ARTICLE
0301-620X
ENGLAND
0 (Antibodies, Monoclonal)
0 (Proteoglycans)
9007-28-7 (Chondroitin Sulfates)
Age-related changes in hyaluronan, proteoglycan, collagen, and osteonectin synthesis by human bone cells.
Fedarko NS; Vetter UK; Weinstein S; Robey PG
National Institute of Dental Research, National Institutes of Health, Bethesda, Maryland 20892.
J Cell Physiol, 151: 2, 1992 May, 215-27
Human bone cells grown in culture, representative of a preosteoblastic stage of maturation, produce an extracellular matrix composed of collagen, several noncollagenous glycoproteins, hyaluronan, and four distinct proteoglycans (PGs). The influence of donor age on the levels of expression of these molecules in vitro has not been well characterized. In this study, human bone cells derived from sources ranging from fetal to 60-year-old donors were grown in culture, radiolabeled for 24 h, and the amount of incorporation of [35S]sulfate into PGs, [3H]glucosamine into hyaluronan, [3H]leucine/proline into osteonectin, and [3H]proline into collagen was determined. Cell proliferation was most rapid in fetal-derived bone cells and decreased with increasing age. Total protein and PG synthesis also decreased with increasing age, falling to 1/3 and 1/4, respectively, of fetal levels after age 30. A large chondroitin sulfate PG (Mr approximately 600,000 Da) was the major fetal PG and its levels were highly correlated with cellular proliferation. [3H]Collagen and [35S]decorin levels increased with the increasing age of the donor, reached a maximum in puberty-derived cells, and decreased to 1/3 maximal levels after age 20. The heparan sulfate PG (Mr approximately 400,000 Da) exhibited steady-state levels regardless of donor age. [3H]Osteonectin and [35S]biglycan levels were high in fetal-derived cells and in cells derived from pubescent donors. The percentage of collagen and four proteoglycans associated with the cell layer pool changed with donor age. All fetal-derived PG core proteins possessed more N- and O-linked oligosaccharides than newborn or adult derived PGs.
English
92242314
Aging [*ME]
Bone and Bones [CY/*ME]
Bone Development
Extracellular Matrix Proteins [*ME]
Cell Division
Cells, Cultured
Collagen [ME]
Homeostasis
Human
Hyaluronic Acid [ME]
Osteonectin [ME]
Proteoglycans [CH/ME]
Statistics
Support, Non-U.S. Gov't
JOURNAL ARTICLE
0021-9541
UNITED STATES
0 (Extracellular Matrix Proteins)
0 (Osteonectin)
0 (Proteoglycans)
9004-61-9 (Hyaluronic Acid)
9007-34-5 (Collagen)
Transformation of fetal secondary cartilage into embryonic bone in organ cultures of human mandibular condyles.
Ben-Ami Y; von der Mark K; Franzen A; de Bernard B; Lunazzi GC; Silbermann M
Laboratory for Musculoskeletal Research, Rappaport Family Institute for Research in the Medical Sciences, Faculty of Medicine, Technion-Israel Institute of Technology, Haifa.
Cell Tissue Res, 271: 2, 1993 Feb, 317-22
Mandibular condyles of human fetuses, 14-21 weeks in utero, were kept in an organ culture system for up to 60 days. After 6 days in culture, the cartilage of the mandibular condyle appeared to have maintained its inherent structural characteristics, including all its various layers: chondroprogenitor, chondroblastic, and hypertrophic. After 12 days in culture, no chondroblasts could be seen; instead, the entire cartilage was occupied by hypertrophic chondrocytes. At the same time, the mesenchymal cells in the vicinity of the chondroprogenitor zone differentiated into osteoblast-like cells that produced type I collagen. The progenitor cells were still actively incorporating 3H-thymidine. The newly formed osteoid-like tissue lacked both metachromatic reactivity and a response to antibodies against chondroitin sulfate. Instead, the tissue reacted positively for osteocalcin (bone gla-protein). The process of new bone formation further progressed and, by the 20th day in culture, the new bone reacted positively for type I collagen, osteonectin, and to a lesser extent for chondroitin sulfate. The osteoid also underwent mineralization as revealed by both the von Kóssa stain and vital staining with tetracycline. The above feature appeared even more intense in 40-day-old cultures. After 60 days, the newly formed bone contained osteoblasts and osteocytes, whereas the extracellular matrix revealed a high degree of matrix polarization. The results of the present study recapitulate findings reported for organ cultures of mice mandibular condyles. However, the in vitro process of de novo bone formation in human specimens requires a 6-fold longer culture time than that needed for mice condyles.
English
93201582
Bone and Bones [CY/*EM]
Cartilage [CY/*EM]
Mandibular Condyle [CY/*EM]
Osteogenesis
Animal
Biological Markers
Cell Differentiation
Comparative Study
Female
Gestational Age
Human
Male
Mice [EM]
Organ Culture
Osteoblasts [CY/ME]
Species Specificity
Stem Cells [CY]
Time Factors
JOURNAL ARTICLE
0302-766X
GERMANY
0 (Biological Markers)
Histogenesis and possible mechanism of chondroid changes in mixed tumour of the skin: immunohistochemical evaluation of bone morphogenetic protein, glycosaminoglycans, keratin, vimentin and neuronal markers.
Mori M; Shrestha P; Sakamoto F; Yang LJ; Qin C; Tsujimura T
Department of Oral and Maxillofacial Surgery, Asahi University School of Dentistry, Gifu, Japan.
Arch Dermatol Res, 286: 5, 1994, 285-92
The distribution of immunoreactivity of bone morphogenetic protein (BMP), the glycosaminoglycans chondroitin 4-sulphate (C4SPG), chondroitin 6-sulphate (C6SPG), dermatan sulphate (DSPG) and keratan sulphate proteoglycans (KSPG), cytokeratin (K8.12), vimentin, glial fibrillary acidic protein (GFAP), actin, desmin, S-100 protein and neuron-specific enolase (NSE) in mixed tumour of the skin was investigated using immunohistochemical methods using monoclonal (MoAb) and polyclonal antibodies (PoAb). A strong BMP immunoreactivity was found characteristically in outer tumour cells of tubuloductal structures and modified myoepithelial cells. Modified myoepithelial cells and chondroidally changed cells showed positive immunoreactivity for C4SPG, C6SPG and DSPG; and KSPG was more pronounced in the modified myoepithelial cells. Vimentin, S-100 protein, GFAP and NSE, but not actin and desmin, were distribute in the outer tumour cells and modified myoepithelial cells in chondroidally changed tissue. Two factors show that chondrogenesis in mixed tumour of the skin is associated with the modified myoepithelial cells through the activity of BMP and biosynthesis of glycosaminoglycans as matrix substance. First, outer or basal tumour cells in mixed tumour of the skin is characterized by the presence of positive immunoreactivity for BMP, KSPG, vimentin, cytokeratin K8.12, S-100 protein, GFAP and NSE, and second, there is a matrix of chondroidally changed tissue containing the reaction products of C4SPG, C6SPG, DSPF and KSPG.
English
94338179
Adenoma, Sweat Gland [*ME]
Glycosaminoglycans [*ME]
Keratin [*ME]
Proteins [*ME]
Sweat Gland Neoplasms [*ME]
Vimentin [*ME]
Actins [ME]
Chondroitin Sulfates [ME]
Dermatan Sulfate [ME]
Desmin [ME]
Glial Fibrillary Acidic Protein [ME]
Human
Keratan Sulfate [ME]
Nerve Tissue Protein S 100 [ME]
Phosphopyruvate Hydratase [ME]
Proteochondroitin Sulfates [ME]
Support, Non-U.S. Gov't
JOURNAL ARTICLE
0340-3696
GERMANY
EC 4.2.1.11 (Phosphopyruvate Hydratase)
0 (bone morphogenetic protein)
0 (keratan sulfate proteoglycan)
0 (Actins)
0 (Desmin)
0 (Glial Fibrillary Acidic Protein)
0 (Glycosaminoglycans)
0 (Nerve Tissue Protein S 100)
0 (Proteins)
0 (Proteochondroitin Sulfates)
0 (Vimentin)
24967-94-0 (Dermatan Sulfate)
68238-35-7 (Keratin)
9007-28-7 (Chondroitin Sulfates)
9056-36-4 (Keratan Sulfate)
Cartilage and bone metabolism in rheumatoid arthritis. Differences between rapid and slow progression of disease identified by serum markers of cartilage metabolism.
Månsson B; Carey D; Alini M; Ionescu M; Rosenberg LC; Poole AR; Heinegård D; Saxne T
Department of Rheumatology, Lund University, Sweden.
J Clin Invest, 95: 3, 1995 Mar, 1071-7
Serum concentrations of specific cartilage and bone molecules reflecting tissue turnover were measured in two well-defined patient groups with early rheumatoid arthritis with distinctly different disease outcome to see if early differences in their levels are prognostic of the rate of joint destruction. Compared with a matched normal population, increased concentrations of cartilage oligomeric matrix protein (COMP) were found in all patients who developed rapid hip joint destruction. In contrast, levels of a putative marker of cartilage aggrecan synthesis, the chondroitin sulfate epitope 846, were increased only in patients with slow joint destruction. Levels of bone sialoprotein (BSP) were increased in both groups, as were levels of the C-propeptide of type II procollagen (CPII), a marker of collagen II synthesis. The increased concentrations of the 846 epitope in patients with slow joint destruction suggest increased aggrecan synthesis. The low levels of the 846 epitope in patients with rapid joint destruction, concomitant with elevated levels of CPII, suggest a selective increase in collagen synthesis. The elevated BSP levels indicate an increased bone turnover in both groups. Thus elevated serum levels of COMP may indicate an unfavorable prognosis for rapid joint destruction, whereas elevated 846 epitope indicates a more favorable prognosis.
English
95190001
Arthritis, Rheumatoid [*ME/RA]
Bone and Bones [*ME]
Cartilage [IM/*ME]
Adult
Aged
Calcium-Binding Proteins [BL]
Chondroitin Sulfates [IM/ME]
Collagen [BL]
Epitopes
Female
Human
Hyaluronic Acid [BL]
Male
Membrane Glycoproteins [BL]
Middle Age
Proteoglycans [BL/IM]
Radioimmunoassay
Sialoglycoproteins [BL]
Support, Non-U.S. Gov't
Support, U.S. Gov't, P.H.S.
JOURNAL ARTICLE
0021-9738
UNITED STATES
0 (aggrecan)
0 (bone sialoprotein)
0 (cartilage oligomeric matrix protein)
0 (chondrocalcin)
0 (Calcium-Binding Proteins)
0 (Epitopes)
0 (Membrane Glycoproteins)
0 (Proteoglycans)
0 (Sialoglycoproteins)
9004-61-9 (Hyaluronic Acid)
9007-28-7 (Chondroitin Sulfates)
9007-34-5 (Collagen)
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SUBSCRIBE: The Wednesday Letter is a free electronic monthly newsletter written and published by Karl Loren. You can view more than 50 back issues of this publication by clicking here. The Wednesday Letter subscription list is maintained on a secure server, no name is ever given or sold to anyone, and it is never used except for this Newsletter. It is automatically published on the Tuesday night just before the first Wednesday of every month. You can subscribe to this free monthly electronic letter by entering your eMail address and name below. You will then automatically receive a request for confirmation, sent to whatever address you have entered. If you do NOT receive this confirmation request, then you will not be subscribed. There may have been an error with your address and you should resubmit. The letter is never sent twice to the same address -- so you do not have to worry about a duplicate subscription. When you receive this confirmation request you must reply to it, or your subscription will not become active. No one can subscribe your name, and address, without you being notified, and if you get an unwanted notice of subscription you only need to DO NOTHING and the subscription will NOT be active.
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Personal Message: When you send a personal message to Karl Loren, you will receive a personal reply as per his instructions. Karl pledges that every personal message will get a personal answer. When you provide your mail address, we will send you free information including our free catalog and a cassette tape lecture by Karl Loren about heart disease, no charge, by mail, even if outside the US. You can select particular information you would like to receive, along with the free cassette tape and catalog.
You can reach Vibrant Life in many ways, including by mail to Vibrant Life, 2808 N. Naomi St., Burbank, CA 91504. Within the US and Canada, use the toll free number: (800) 523-4521, the local number: (818) 558-1799, the FAX: (818) 558-7299, eMail to kimberly@oralchelation.com or any one of the hundreds of message forms throughout the 50 web sites. Vibrant Life normally ships the same day we get an order. There are message forms on each of the 100,000+ pages on this and other sites where you can communicate with Vibrant Life. Check out our companion site, at: http://www.oralchelation.net where Karl's 2000 page book is published. Karl Loren is the author and webmaster for this BOOK, as well as for another web site about ORAL CHELATION. His personal philosophical articles are at PHILOSOPHY.
Copyright © May 20, 2008 6:23 AM by Karl Loren on behalf of Vibrant Life, ALL RIGHTS RESERVED. Permission is granted for non-commercial downloading, copying, distribution or redistribution on two conditions: One, that some form of copyright notice is included in every copy distributed or copied, showing the copyright belonging to Vibrant Life, Burbank, CA, at www.oralchelation.com . The second condition is that the material is not to be used for any purpose contrary to the purposes and objectives of this site. This permission does not extend to materials on this site which are copyrighted by others.