Biomedical subjects

F Rahemtulla

Publications and source records attributed to F Rahemtulla.

At least 19 recordsLinked to original sources

PubMed2001

Immunohistochemical localization of large chondroitin sulphate proteoglycan in porcine gingival epithelia.

In this study, we report the immunohistochemical localization of versican in healthy porcine gingival epithelia. The monoclonal antibody (mAb), 5D5, specifically recognizes core proteins of large chondroitin sulphate proteoglycans such as versican, neurocan and brevican, but not the core protein of aggrecan. Because neurocan and brevican appear to be specific to nervous tissue, the large chondroitin sulphate proteoglycans examined in this study is most likely versican. In the keratinized layer of the attached gingival epithelium, the basal and spinous cell surfaces showed intense staining for mAb 5D5. In the parakeratinized layer of the sulcus epithelium, the localization was restricted to the basal and lower spinous layers. In the junctional epithelium, intense staining was observed in one or two cell layers near the enamel surface. Immunoelectron microscopy revealed high-density depositions of 5D5 immunoreactivity on epithelial cell surfaces. At the enamel surface, 5D5 immunoreactivity was localized to the dental cuticle of the junctional epithelium but was not present in the internal basal lamina. These results suggest that versican, a large chondroitin sulphate proteoglycan, is involved in epithelial differentiation and downgrowth.

Animals↗

PubMed1999

Interleukin (IL)-1 and Porphyromonas gingivalis lipopolysaccharide stimulation of IL-6 production by fibroblasts derived from healthy or periodontally diseased human gingival tissue.

BACKGROUND: Human gingival fibroblasts (HGF) play a key role in tissue repair and destruction. These cells express low levels of interleukin (IL)-6 constitutively and increased levels after stimulation with lipopolysaccharide (LPS) or the cytokines IL-1 and tumor necrosis factor-alpha (TNF-alpha). However, little information is available on IL-6 production by fibroblasts derived from diseased tissue. The present study compared constitutive and induced IL-6 production by human gingival fibroblasts (HGF) derived from healthy and diseased periodontal tissue. We also evaluated whether IL-1 acted in a synergistic manner with LPS in inducing IL-6 production by HGF and whether LPS acted via CD14. METHODS: HGF derived from healthy and diseased tissue and foreskin fibroblasts were grown to confluency, photographed, and counted, and their constitutive IL-6 production was quantitated by ELISA. Healthy and diseased HGF were also pretreated with IL-1alpha, followed by incubation with Porphyromonas gingivalis or Escherichia coli LPS. Culture supernatants were assessed for IL-6 protein by ELISA and cell lysates for mRNA by reverse transcription-polymerase chain reaction (RT-PCR). In order to determine if LPS stimulation was mediated through the LPS receptor, CD14, surface receptors on HGF were assessed by flow cytometry and the total RNA CD14 mRNA was assessed. RESULTS: Higher quantities of IL-6 were produced by the diseased HGF before and after stimulation than by the healthy HGF. Pretreatment with IL-1alpha followed by LPS stimulation of the healthy and diseased HGF cell lines resulted in an additive effect on IL-6 production. Pretreatment with IL-1alpha followed by a second incubation with the same stimulant produced higher amounts of IL-6 than cultures incubated with LPS alone or following IL-1alpha pretreatment. Similar amounts of IL-6 mRNA were present in unstimulated HGF from either diseased or healthy tissue and in those incubated with IL-1alpha only. After incubation with IL-1alpha and LPS, diseased HGF produced slightly more mRNA than healthy HGF. CD14 was not expressed by healthy or diseased HGF even after stimulation with either P. gingivalis or E. coli LPS. CD14 message was also undetectable. CONCLUSIONS: Taken together, these results indicate heterogeneity among gingival fibroblasts and an additive effect of IL-1 and P. gingivalis LPS on IL-6 production by HGF. Furthermore, the LPS effect on HGF was not mediated by CD14.

Cell Count↗

PubMed1998

An immunohistochemical study of the localization of biglycan, decorin and large chondroitin-sulphate proteoglycan in adult rat temporomandibular joint disc.

To analyse regional variations in extracellular matrix components of adult rat temporomandibular joint discs, immunohistochemical techniques were used to examine the localization of two small dermatan-sulphate proteoglycans, biglycan and decorin, and a large chondroitin-sulphate proteoglycan. Staining for biglycan was intense in the posterior band, although it had a rather weak and even distribution throughout the disc. In contrast, staining for decorin was faint in the intermediate zone and the central part of the posterior band, moderate in the anterior and posterior attachments and most intense in the junction between the anterior band and attachment. The upper surface of the disc stained more intensely than the lower. Similarly, there was intense staining for large chondroitin-sulphate proteoglycan in the peripheral band, but both the anterior and the temporal parts of the posterior attachments were faintly stained. These results demonstrate marked regional differences in the expression of biglycan, decorin and large chondroitin-sulphate proteoglycan in the temporomandibular joint discs of adult rats. These variations probably reflect the different biomechanical environments caused by the complicated articulatory functions of the temporomandibular joint.

Animals↗

PubMed1998

Effect of lipopolysaccharide and inflammatory cytokines on interleukin-6 production by healthy human gingival fibroblasts.

Cytokines are hormone-like proteins which mediate and regulate inflammatory and immune responses. The purpose of this study was to investigate the effect of lipopolysaccharide (LPS) and inflammatory cytokines on regulation of interleukin-6 (IL-6) production by human gingival fibroblasts (HGF). The HGF cell lines used in this study, H-CL and F-CL, were established by the explant technique from healthy gingival tissue. Cultured cells were grown to confluency and incubated with various concentrations of LPS from Escherichia coli or Porphyromonas gingivalis or with the recombinant human cytokine tumor necrosis factor alpha (TNF-alpha), IL-1alpha, or IL-1beta. Culture supernatants were collected at various times and assessed for IL-6 production by enzyme-linked immunosorbent assay. Total RNA was isolated from the harvested cells and used to assess levels of IL-6 mRNA by the RNase protection assay. Both LPS preparations induced IL-6 production (1 to 4 ng of IL-6 per ml) by both HGF cell lines. Although TNF-alpha stimulated IL-6 production by HGF, > 10-fold-larger amounts were induced with IL-1alpha and IL-1beta. Furthermore, the addition of both IL-1alpha and TNF-alpha to cultured cells resulted in approximately 600- to 800-fold-higher levels of IL-6 than seen in control cultures, suggesting that these cytokines synergistically induced IL-6 production by HGF. IL-6 message in cultured cells was upregulated 20-fold by TNF-alpha, 1,000-fold by IL-1alpha and IL-1beta, and 1,400-fold by IL-1alpha plus TNF-alpha. IL-1alpha and TNF-alpha alone upregulate IL-6 production in a dose- and time-dependent fashion. The addition of IL-1alpha and TNF-alpha to cultured HGF cells resulted in a synergistic induction of IL-6 after 8 h of incubation and when greater than 10 pg of this combination per ml was used. Our studies show that inflammatory cytokines are hundreds of times more potent than LPS in stimulating IL-6 production by HGF.

Cell Line↗

PubMed1998

Proteoglycan expression in the rat temporomandibular joint in response to unilateral bite raise.

The vertebrate articular tissue consists of collagen fibers embedded in a ground substance. Collagen resists tensile forces, while proteoglycans in the ground substance provide resilience and resistance to compression. It was hypothesized that unilateral bite raise would induce increasing expression of proteoglycans in TMJ articular tissues. As a test of this hypothesis, six- and nine-week-old Sprague-Dawley rats received unilateral bite-raising appliances bonded to their right upper molars for 4 wks. A group of nine-week-old rats was housed for an additional 4 wks after removal of the appliances they had worn for 4 wks. Proteoglycans that carry abundant chondroitin sulfate and keratan sulfate side-chains, most likely aggrecans, were detected by safranin O in the fibrocartilaginous zone of the condyle in parasagittal sections. A monoclonal antibody against a large chondroitin sulfate proteoglycan related to versican reacted strongly in the surface fibrous layer of the mandibular condyle and moderately in the discs of the treated specimens. Computer quantification for safranin O and anti-versican antibody staining revealed that the average intensities of the treated specimens were significantly higher than those of their corresponding sham-operated controls, and the average intensities of the treatment-reversal specimens had no significant differences from their corresponding sham-operated controls. Thus, unilateral bite raise appeared to have induced an increase in the expression of aggrecan in the condylar cartilage and a proteoglycan related to versican in the TMJ disc and the articular surface of the condyle. The elevated proteoglycan expression is interpreted to suggest that unilateral bite raise leads to an increase in the magnitude of compressive forces in the rat temporomandibular joint.

Aggrecans↗

PubMed1998

Proteoglycans at the bone-implant interface.

The widespread success of clinical implantology stems from bone's ability to form rigid, load-bearing connections to titanium and certain bioactive coatings. Adhesive biomolecules in the extracellular matrix are presumably responsible for much of the strength and stability of these junctures. Histochemical and spectroscopic analyses of retrievals have been supplemented by studies of osteoblastic cells cultured on implant materials and of the adsorption of biomolecules to titanium powder. These data have often been interpreted to suggest that proteoglycans permeate a thin, collagen-free zone at the most intimate contact points with implant surfaces. This conclusion has important implications for the development of surface modifications to enhance osseointegration. The evidence for proteoglycans at the interface, however, is somewhat less than compelling due to the lack of specificity of certain histochemical techniques and to possible sectioning artifacts. With this caveat in mind, we have devised a working model to explain certain observations of implant interfaces in light of the known physical and biological properties of bone proteoglycans. This model proposes that titanium surfaces accelerate osseointegration by causing the rapid degradation of a hyaluronan meshwork formed as part of the wound-healing response. It further suggests that the adhesive strength of the thin, collagen-free zone is provided by a bilayer of decorin proteoglycans held in tight association by their overlapping glycosaminoglycan chains.

Animals↗

PubMed1997

Light and electron microscopical immunohistochemical localization of large proteoglycans in human tooth germs at the bell stage.

The immunohistochemical localization of large hyaluronate-binding proteoglycans has been studied in human tooth germs at the bell stage using a monoclonal antibody, 5D5, which is derived from bovine sclera and specifically recognizes the core protein of large proteoglycans, such as versican, neurocan and brevican, but not that of aggrecan. In the early bell stage before predentine secretion, when the enamel organs consisted of the inner and outer enamel epithelia, stratum intermedium and stellate reticulum, the enamel organs were not stained by 5D5, but the dental papillae and follicles stained strongly. Concomitant with the secretion of predentine, dentine and subsequent enamel matrix, strong 5D5 immunostaining distributed over the entire cell surfaces of secretory ameloblasts was observed. The forming enamel matrix showed strong staining. While most of the inner and outer enamel epithelia and stratum intermedium lacked staining, the cervical loop region and stellate reticulum showed weak staining. Although the forming dentine and odontoblasts appeared to lack 5D5 affinity, the predentine, dental papilla and dental follicle demonstrated moderate to strong reactivity. At the ultrastructural level, specific immunoreaction by immunogold particle deposition was clearly detected over the basal lamina of presecretory ameloblasts, secretion granules of secretory ameloblasts and the forming enamel matrix. These results indicate that a marked increase in the large proteoglycan associated with secretory ameloblasts may correlate with cell differentiation and enamel matrix biosynthesis.

Humans↗

PubMed1997

Quantification of human myeloperoxidase in oral fluids.

Peroxidase activity in human whole saliva is derived from salivary peroxidase and myeloperoxidase. Present spectrophotometric assays are relatively non-specific and influenced by ions present in salivary secretions, resulting in an over and/or underestimation of peroxidase activities. Specific polyclonal or monoclonal antibodies would greatly simplify the identification of salivary peroxidase and myeloperoxidase in human saliva and determine the relative contribution of each enzyme to the total peroxidase activity in human saliva. In the present study, a highly purified preparation of myeloperoxidase was used to raise polyclonal antibodies against the antigen. The antibodies were purified and extensively characterized in terms of their ability to interact with the antigen, with other mammalian peroxidases, and with other proteins present in salivary fluids. The antibodies recognized only myeloperoxidase and did not cross-react with any of the substances tested, showing that these antibodies can be used to detect and differentiate myeloperoxidase from other peroxidases in saliva. We have also developed and tested a sandwich ELISA which can be used in a clinical setting to quantify myeloperoxidase in whole saliva and gingival crevicular fluid.

Antibodies↗

PubMed1996

Cloning and sequence analysis of the human salivary peroxidase-encoding cDNA.

A cDNA (hSPO) encoding human salivary peroxidase (hSPO) was isolated and its nucleotide (nt) sequence determined. The coding sequence resembles those of other mammalian peroxidases and contains a 3' untranslated region of 538 nt. In a rabbit reticulocyte lysate transcription/translation system, the cDNA produces a major protein of approx. 67 kDa, which corresponds to the calculated molecular weight of unglycosylated hSPO.

Amino Acid Sequence↗

PubMed1996

Effect of in vitro passage of healthy human gingival fibroblasts on cellular morphology and cytokine expression.

Cytokines have been implicated in the regulation of antibody and inflammatory responses, but their role in periodontal diseases has not been elucidated. In the present study, cytokine production by human gingival fibroblasts (HGF) following in vitro passage was assessed in order to determine the basal levels of cytokine message and protein and to determine if the cellular morphology and the profile of cytokines produced differed with passage. The HGF cell line F-CL was established by explantation from non-inflamed gingival tissue, and cells from passages 1-10 were studied. The number of cells was determined in confluent cultures and cell morphology was examined by light microscopy. Fibroblasts from confluent cultures were examined for cytokine mRNA by reverse transcription-polymerase chain reaction and culture supernatants were assessed for cytokines by enzyme-linked immunosorbent assay. The morphology of F-CL fibroblasts in passages 1-4 was normal, while fibroblasts in passages 5-10 were larger. In general, the number of cells decreased from early to late passage. Fibroblasts from passages 1-10 contained message for interleukin-1 beta, -6 and -8, but not for interleukin-1 alpha or tumour necrosis factor-alpha. Interleukin-6 was detected in culture supernatants of F-CL fibroblasts by the enzyme immunoassay and its level decreased with increasing passage.

Cell Culture Techniques↗

PubMed1996

Chemical characterization and quantification of proteoglycans in human post-burn hypertrophic and mature scars.

1. Samples of normal skin from four patients, post-burn hypertrophic scar from five patients and post-burn mature scar from six patients were analysed for hydroxyproline, water and uronic acid and extracted with guanidinium chloride to yield the proteoglycan pool. A large chondroitin sulphate proteoglycan and biglycan were purified from one hypertrophic scar biopsy and decorin from a normal skin biopsy, by ion-exchange chromatography, gel-filtration and hydrophobic interaction chromatography. These purified proteoglycans were used in an inhibition ELISA assay to estimate the quantities of each in the tissue samples. 2. Samples of post-burn hypertrophic scar had on average 30% less hydroxyproline, 12% more water and 2.4 times as much uronic acid as normal skin. These differences were all statistically significant, whereas the small differences between mature scars and normal skin were not. The content of decorin in hypertrophic scars was only 25% of that in normal skin whereas the large chondroitin sulphate proteoglycan and biglycan were each about 6-fold higher. The mature scars had slightly elevated levels of large chondroitin sulphate proteoglycan and biglycan and a reduced content of decorin compared with normal skin but these differences were not statistically significant. 3. The results suggest that aberrant proteoglycan metabolism is a significant factor contributing to the altered physical properties of hypertrophic scars and that maturation of post-burn scars is dependent on a return of the relative proportions and concentrations of proteoglycans to those characteristic of normal dermis.

Burns↗

PubMed1995

Immunohistochemical localization of the proteoglycans decorin, biglycan and versican and transforming growth factor-beta in human post-burn hypertrophic and mature scars.

The distributions of the small proteoglycans, decorin and biglycan and the large proteoglycan, versican, in normal skin and post-burn hypertrophic and mature scars, were compared using monoclonal and polyclonal antibodies to the core proteins. Biglycan and versican were virtually undetectable in normal dermis but readily seen in hypertrophic scars. Staining for decorin was strong throughout the dermis in normal skin but restricted to the deep dermis and a narrow zone under the epidermis in hypertrophic scar--areas which did not stain for versican. Decorin was absent or reduced in the nodules in these specimens. In mature post-burn scars, staining for all three proteoglycans demonstrated an intensity that was intermediate between that in normal dermis and that in the nodules of the hypertrophic scars. Transforming growth factor-beta was present in the nodules of hypertrophic scars but the deep dermis of these specimens stained most intensely for this cytokine which was also found in the dermis of mature scars but was not detectable in normal dermis. The apparent co-distribution of decorin and transforming growth factor-beta suggests that this proteoglycan may play an active role in the resolution of the scars. Changes in proteoglycan type and distribution could possibly account, at least in part, for the derangement of collagen and the altered physical properties of hypertrophic scar tissue.

Adult↗

PubMed1993

Versican, a hyaluronate-binding proteoglycan of embryonal precartilaginous mesenchyma, is mainly expressed postnatally in rat brain.

The localization of versican, a large hyaluronate-binding fibroblast proteoglycan, was studied in rat prenatal and postnatal development. In adult rat white matter and cerebellum, the distribution of versican was identical to that previously reported for brain-specific glial hyaluronate-binding protein (GHAP). Versican was also found in gray matter where it formed characteristic coats around large neurons. It was also found in peripheral tissues, namely, kidney medulla, myotendinous junctions, and endoneurial and endomysial sheaths. In rat embryo the most notable finding was the presence of large amounts of versican immunoreactive material in precartilaginous mesenchyma. In embryonal CNS, versican was mainly confined to the marginal zone on the surface of the cerebral hemispheres. Versican expression mainly occurred postnatally in brain and spinal cord. In spinal cord white matter, versican immunoreactivity was already present in 3-day-old rats and preceded the appearance of GHAP, which was first detected on day 13 after the onset of myelination. Versican expression was markedly delayed in gray matter. The characteristic perineuronal coats were first observed on day 21 in the cerebral cortex. It is concluded that, with the exception of hyaluronate, brain extracellular matrix (ECM) is mainly produced postnatally and that the ECM protein produced by brain cells, most likely astrocytes, is similar to that produced by precartilaginous mesenchyma.

Animals↗

PubMed1993

Colocalization of tenascin with versican, a hyaluronate-binding chondroitin sulfate proteoglycan.

Rabbit antisera against tenascin, a large extracellular matrix protein, in conjunction with monoclonal antibodies of mouse origin against versican, a large hyaluronate-binding proteoglycan, were used to make a comparative study of the distribution of the two antigens in the same cryostat sections by double immunofluorescence. In the central nervous system, tenascin was invariably associated with versican, but the reverse was not true, in that versican was also found where tenascin was not detectable, particularly in gray matter. There were major species differences in the distribution of tenascin in the central nervous system. In the cow, tenascin was found in cerebral and spinal cord white matter and in the granule cell layer of the cerebellum. In the human brain, tenascin was found in cerebral white matter but not in the cerebellum. In the rat, tenascin was mainly confined to brain periventricular layer and spinal cord white matter. During the development of the cerebellum of the rat, the tenascin immunoreactivity decreased, and a lower molecular weight band appeared (J1-160/180/restrictin?) and persisted throughout adulthood. Tenascin expression was a relatively late event in the development of the rat central nervous system, immunoreactivity being first observed after birth. In the rat embryo, tenascin was found to co-localize with versican in precartilaginous mesenchyme and in connective tissue underlying epithelia. The colocalization of versican with tenascin suggests that versican may be the tenascin (cytotactin)-associated proteoglycan reported in the literature.

Animals↗

PubMed1993

Immunohistochemical localization of proteoglycans in human periodontium.

Proteoglycans (PGs) are extracellular and cell surface-associated macromolecules that regulate cell adhesion, cell growth, matrix formation, and bind growth factors. In this work we studied the distribution of core proteins of four PGs (decorin, biglycan, a large molecular weight PG, and CD44) in human gingiva and periodontal ligament by immunohistochemical staining of frozen tissue sections with specific antibodies. Decorin, a major PG of this tissue, was localized on collagen fiber bundles in the gingival and periodontal connective tissues. Staining for decorin was most intense at the subepithelial region. Biglycan was a minor PG component of the human periodontium, showing some accumulation in connective tissue under the oral epithelium. At the immunohistochemical level, biglycan appeared to form fine filament-like structures on extracellular matrix fibers. Localization of large molecular weight PG differed from that of decorin and biglycan. It was concentrated in deep connective tissue areas of the gingiva and in the periodontal ligament, and was only weakly present at the subepithelial region. CD44 was mainly concentrated in cell-cell contact areas of basal and spinous layers of oral epithelium. In the connective tissue of gingiva and periodontal ligament, CD44 was localized on fibroblast cell surfaces. Connective tissue area under the junctional epithelium contained relatively small amounts of PGs. The results indicate that different parts of human periodontium contain a typical variety of PGs, suggesting a specific function for each PG species in the location at which they accumulate.

Adolescent↗

PubMed1993

Extracellular matrix in regenerating rat sciatic nerve: a comparative study on the localization of laminin, hyaluronic acid, and chondroitin sulfate proteoglycans, including versican.

Using a glial hyaluronate-binding protein as a probe, monoclonal antibodies against versican and ABC digested chondroitin sulfate proteoglycans, and polyclonal antibodies against laminin, we localized these extracellular matrix (ECM) components in the endoneurium of the adult rat sciatic nerve. During Wallerian degeneration caused by nerve crushing, the staining pattern of these ECM elements changed dramatically. In the first stages and up to 5 days after injury, the tubular endoneurial structures remained the same as in control nerves. Ten days after crush, the bands of Büngner formed by proliferating Schwann cells in the distal stump of crushed nerves stained diffusely for hyaluronate, laminin, and chondroitin sulfate. Regenerating axons were demonstrated in this location by double-labeling experiments with neurofilament antibodies. Conversely, staining with antibodies against versican, a hyaluronate binding proteoglycan, was reduced and the bands of Büngner were not stained. After 30 days the endoneurial tubes made their reappearance and, as in normal nerve, they stained for hyaluronate, laminin, versican, and chondroitin sulfate. It is concluded that proliferating Schwann cells in peripheral nerve undergoing Wallerian degeneration are capable of producing several endoneurial ECM constituents, versican being a notable exception.

Animals↗

PubMed1992

Isolation of a large aggregating proteoglycan from human brain.

A large proteoglycan (365 kDa), identified with monoclonal antibodies raised against chondroitin sulfate, was isolated from human brain. The isolation required anion-exchange chromatography followed by gel filtration through a Sephacryl S-500 column. The proteoglycan bound specifically to [3H]hyaluronate (HA). The binding was not reduced by high salt concentrations (up to 4 M) and was inhibited at low pH (< 4.0). The binding was inhibited by the octamer and decamer (but not the hexamer) oligosaccharides of HA. Limited proteolysis of the proteoglycan gave rise to a relatively stable polypeptide (80 kDa). The amino-terminal sequence of the 80-kDa polypeptide was identical to the cDNA-derived amino-terminal sequence of versican, a large human fibroblast proteoglycan. A monoclonal antibody raised against bovine proteoglycans and recognizing the versican core protein reacted by immunoblotting with the proteoglycan isolated from human brain. The antibody was used to localize the proteoglycan in acetone-fixed cryostat sections of bovine spinal cord. The localization of the proteoglycan in the central nervous system was identical to that previously reported for glial hyaluronate-binding protein (GHAP), a 60-kDa glycoprotein of the brain extracellular matrix (ECM). However, a major difference was observed with respect to the sensitivity of the two antigens to hyaluronidase. As previously reported, GHAP was released from the tissue by hyaluronidase digestion, whereas the proteoglycan persisted under these conditions. We conclude that the protein-hyaluronate aggregates in brain ECM contain both GHAP and versican, that GHAP is only retained in the ECM by its interaction with hyaluronate, and that the proteoglycan is anchored in some other manner and probably connects cell surfaces with the ECM since it was not released by hyaluronidase digestion.

Amino Acid Sequence↗

PubMed1992

A biochemical analysis of human periodontal tissue proteoglycans.

Proteoglycans synthesized by periodontal (gingival, periodontal ligament, dental follicle) fibroblasts were analysed by SDS/polyacrylamide and agarose gel electrophoresis after being labelled with radioactive sulphate. Medium, cell membrane and extracellular matrix fractions were analysed separately. Samples were treated with chondroitinase AC, chondroitinase ABC, heparitinase or a combination of chondroitinase ABC and heparitinase before electrophoretic separation of proteoglycans. Antibodies to versican and decorin were used to identify these molecules by Western immunoblots. For steady-state metabolic radiolabelling of fibroblasts, medium and cell membrane fractions contained about equal proportions of radiolabelled proteoglycans (about 43%), whereas less radioactivity (about 14%) was found in proteoglycans of the matrix fraction. Periodontal fibroblasts produce six major proteoglycans: versican, a high-molecular-mass chondroitin sulphate proteoglycan (CSPG); decorin, a dermatan sulphate proteoglycan (DSPG); a membrane-associated heparan sulphate proteoglycan (HSPG); two medium- or matrix-associated HSPGs; and a 91 kDa membrane-associated CSPG. Variation in decorin molecular size was observed in mass cultures of fibroblasts. Similar polydispersity in molecular size of decorin was seen in several clones established from one mass culture.

Cell Fractionation↗