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J Bocquet

Publications and source records attributed to J Bocquet.

At least 19 recordsLinked to original sources
PubMed2001

Biochemical characterization of integral membrane heparan sulfate proteoglycans in Sertoli cells from immature rat testis.

(35)S-Radiolabeled cultured Sertoli cells from immature rat testis were extracted with detergent and the different proteoheparan sulfate (HSPG) forms of the extract were discriminated and quantified on the basis of their high anionic charge, hydrodynamic size, lipophilic properties, susceptibility to trypsin and phosphatidylinositol phospholipase C (PI-PLC). Trypsin released 50% of total cellular HSPG corresponding to 80% of total hydrophobic HSPG. Trypsin-accessible HSPG were presumed to be integral membrane species. Trypsin-resistant HSPG, probably intracellular, distributed into non-lipophilic (37.5%) and lipophilic (12.5%) populations. Biochemical analysis of PG copurified with plasma membrane confirmed the existence of hydrophobic HSPG integrated into this structure. Among hydrophobic HSPG accessible to trypsin, 35% were PI-PLC released and radiolabeled by [(3)H]inositol indicating that about one third of integral membrane HSPG were intercalated into the plasma membrane through a phosphatidylinositol anchor (glypican type). PI-PLC-resistant forms represented HSPG inserted into the membrane through a hydrophobic segment of the core protein (syndecan type). No lipophilic PG was present in other cell compartments (culture medium, cell periphery, extracellular matrix). (125)I-Iodinated hydrophobic HSPG were deglycanated and submitted to SDS-polyacrylamide gel electrophoresis. In the glypican family, a core protein (64--65 kDa) was detected, whereas in the syndecan family, bands of 60 and 68 kDa were observed which may correspond to self-association of different core proteins. In Sertoli cell, specific functional attributes of different integral membrane HSPG forms remain to be investigated.

Animals↗
PubMed2000

Expression of glypican-1, syndecan-1 and syndecan-4 mRNAs protein kinase C-regulated in rat immature Sertoli cells by semi-quantitative RT-PCR analysis.

In seminiferous tubules, Sertoli cells provide structural and nutritional support for the developing germinal cells. Cell to cell signalization and cell adhesion require proteoglycans expressed at the cell membrane. A preliminary biochemical and structural approach indicated that cell surface proteoglycans are mostly heparan sulfate (HSPG) in immature rat Sertoli cells. The present study focused on the qualitative and quantitative expression of three membrane HSPG, syndecan-1, syndecan-4 and glypican-1 in Sertoli cells of 20-day-old rat. A semi-quantitative multiplex RT-PCR strategy was developed to appreciate the effect of PKC activation on the mRNA expression of the three HSPG. Our data show that the syndecan-1 and glypican-1 mRNA expression is increased by the phorbol myristate acetate (PMA) suggesting a regulation of their expression by the phosphatidyl inositol pathway, as previously hypothesized (Fagen et al., Biochim. Biophys. Acta, 1472 (1999) 250-261). In addition, a physiological effector of the PKC as ATP gave similar effects. Thus, this over-expression could be related with paracrine factors secreted by germ cells.

Adenosine Triphosphate↗
PubMed2000

In Vitro Synthesis of Proteoglycans and Collagen in Primary Cultures of Mantle Cells from the Nacreous Mollusk, Haliotis tuberculata: A New Model for Study of Molluscan Extracellular Matrix.

In Mollusca, the mantle produces an organic matrix that mineralizes in time to make shell. Primary mantle cell cultures from the nacreous gastropod Haliotis tuberculata have been established as useful experimental model to investigate in vitro synthesis of both proteoglycans/glycosaminoglycans (PGs/GAGs) and collagen. First, we tested different enzymatic digestion procedures to find the method that gives the highest percentage of viable and adherent cultured cells. Enzymatic digestion with 0.1% pronase plus 0.1% collagenase was routinely used. Six days after the initiation of culture, about 80% of cells were viable, among which 20% were adherent as quantified by the MTT reduction assay. In addition, the protein synthesis estimated by [(3)H]leucine incorporation remained constant during this period. For the first time, we demonstrated a de novo synthesis of PGs/GAGs and collagen in primary cultures of mantle cells. After 48 hours of labeling, among the [(3)H]-d-glucosamine macromolecules synthesized, [(3)H]PGs/GAGs represented 43%, divided into 45% heparan sulfate, 37% chondroitin/dermatan sulfate, and 6% hyaluronic acid. Early elution on anion-exchange chromatography of these PGs/GAGs indicated that most of them appeared as undersulfated GAG molecules. De novo synthesis of collagen represents 4.52% +/- 0.84% (SD) with respect to the total protein synthesis. Such a model will facilitate studies on the synthesis of PGs/GAGs and collagen as components of the extracellular matrix and its regulation in Mollusca. Both PGs/GAGs and collagen participate in molecular events that regulate cell adhesion, migration, and proliferation. Further studies with this type of in vitro model should provide knowledge about novel aspects of molluscan cell signaling, in relation to extracellular matrix components.

Journal Article↗
PubMed1999

Activation of protein kinase C increases proteoglycan synthesis in immature rat Sertoli cells.

In order to determine the signal transduction pathways involved in the regulation of proteoglycan (PG) synthesis in immature rat Sertoli cells (SC), we have examined the effect of the tumor promoter phorbol ester PMA (phorbol myristate acetate) on [35S]sulfate and [3H]glucosamine incorporation into PG molecules neosynthesized by cultured rat SC. PMA induced a dose- and time-dependent stimulation of labeled cell-associated PG as determined by quantitative solid phase assay. The overall effect of PMA resulted from enhancement of both glycosylation and catabolism of cell PG, this latter effect leading to a drastic decrease of their residence time in the membrane. Besides these quantitative effects, activation of protein kinase C by PMA induced qualitative changes as reflected by increase in relative proportion of heparan sulfate PG (HSPG) in cell membrane PG. In light of our previous results suggesting an inverse relationship between PG synthesis and FSH responsiveness in immature rat Sertoli cells, the PMA-induced upregulation of cell membrane PG, and particularly HSPG, could constitute one mechanism involved in the repression of FSH-stimulated steroidogenesis induced by PKC activation.

Animals↗
PubMed1999

Activation of protein kinase C pathway by phorbol ester results in a proteoglycan synthesis increase in peritubular cells from immature rat testis.

In cultured peritubular cells (PT) from rat testis, protein kinase C (PKC) was activated by phorbol 12-myristate 13-acetate (PMA). PMA enhanced the synthesis of proteoglycans (PG) and to a lesser extent their catabolism; the stimulation of the synthesis appeared to be due to an increase in PG protein moiety production and, at the same time, to an increase in the glycanation process as revealed by the use of an exogenous acceptor, p-nitrophenyl-beta-d-xyloside. In the presence of PMA, the molecular weight of neosynthesized PG and the length of their constitutive glycosaminoglycan chains were not modified. Moreover, the distribution of proteochondroitin sulfate and proteoheparan sulfate in medium and in cell layer remained unchanged. However, PMA reduced the sulfation level of chondroitin sulfate and heparan sulfate chains, suggesting that PKC activation resulted in an independent modulation of the sugar chain formation and of the sulfate residue transfer. PMA effect on the synthesis of hyaluronan was also determined: PMA dramatically enhanced its production by PT cells.

Animals↗
PubMed1999

Inhibition of transmembrane calcium influx induces decrease in proteoglycan synthesis in immature rat Sertoli cells.

Beyond increased cAMP synthesis, calcium influx has been involved in signal transduction triggered by the gonadotropin follicle-stimulating hormone (FSH), the main regulator of Sertoli cells functions. In order to delineate a possible involvement of calcium in the regulation of proteoglycan synthesis, we have examined the effect of low-voltage-activated calcium channel blocker verapamil on both [(35)S]-sulfate and [(3)H]-glucosamine incorporation into proteoglycan molecules neosynthesized by cultured Sertoli cells from 20-day-old rats. Verapamil induced a dose- and time-dependent decrease in labeling of both secreted and cell-associated proteoglycans, as determined by quantitative solid-phase assay. This effect was mimicked by the addition of the calcium chelator EGTA, suggesting that verapamil effect resulted from the inhibition of transmembrane calcium influx. The decrease in apparent proteoglycan synthesis appeared to be attributable primarily to a lowering of the glycanation process, as shown by experiments using an exogenous acceptor for glycosaminoglycan synthesis. Moreover, verapamil induced a decrease in relative proportion of heparan sulfate proteoglycans in the cell layer. Pulse-chase kinetics demonstrated that verapamil also altered proteoglycan catabolism, leading to glycosaminoglycan retention in the cell layer and inhibiting the proteoglycan desulfation step. We conclude that intracellular calcium is essential to maintain Sertoli cell proteoglycan expression and could thus be involved in the repression of Sertoli cell cAMP-dependent syntheses such as estradiol production.

Animals↗
PubMed1999

Drug-induced alterations in rat peritubular cell cytoskeleton result in proteoglycan synthesis modifications. Comparison with some intracellular signaling pathways.

The influence of phorbol myristate acetate (PMA), dibutyryl cAMP and insulin-like growth factor (IGF-1) as well as cytoskeletal disrupting drugs on morphological changes has been studied in peritubular cells isolated from immature rat testis. Morphological studies were combined with immunofluorescence investigations of cytoskeletal elements and their rearrangements by various agents. The results were correlated with modulation of proteoglycan synthesis. Peritubular cells exposed to dibutyryl cAMP or cytochalasin D were transformed from flattened, fibroblast-like into neuronal-like morphology. In such cells, destruction of actin filaments was accompanied with a 50% decrease in cell-associated proteoglycan synthesis as well as with oversulfation of total proteoglycans. On the contrary, peritubular cell shape has been slightly altered after addition of PMA, IGF-1, vinblastine or colchicine. After these treatments, destruction or rearrangement of cytoskeletal elements was observed; cell-layer proteoglycan synthesis remained either unchanged or increased while total proteoglycans were always undersulfated. IGF-1, PMA and dibutyryl cAMP modified the peritubular cell morphology, cytoskeletal organization and proteoglycan production; the cytoskeleton disrupting drugs such as vinblastine, colchicine and cytochalasin D mimicked some of these effects. These observations suggest that alterations in proteoglycan biosynthesis, after activation of tyrosine kinase, protein kinase C and protein kinase A pathways might be mediated, at least in part, by the disorganization of the cytoskeleton structure.

Actin Cytoskeleton↗
PubMed1998

Regulation of proteoglycan and hyaluronan synthesis by elevated level of intracellular cyclic adenosine monophosphate in peritubular cells from immature rat testis.

The effects of an increase in intracellular cAMP concentration on proteoglycan (PG) synthesis by peritubular (PT) cells from immature rat testis were investigated. In the presence of dBcAMP for 72 h, the [3H]-hexosamine incorporation in secreted PG and in cell-associated PG was reduced, whereas [35S]-sulfate radioactivity was enhanced in secreted PG and not affected in cell-associated PG. Cholera toxin and IBMX, known to generate high intracellular cAMP levels, induced similar changes. Cyclic AMP did not alter PG protein moiety synthesis but enhanced PG turnover. Cholera toxin and dBcAMP profoundly modified PG characteristics: (1) Apparent molecular weight of PG was increased. (2) This was due to an increase in glycosaminoglycans (heparan sulfate (HS) and chondroitin sulfate (CS)) length. (3) The number of glycosaminoglycan chains was presumably reduced. (4) Heparan sulfate and chondroitin sulfate chains of medium and cell layer-associated PG appeared oversulfated. (5) The pattern of cell layer associated PG was modified with a decrease in HSPG and a correlative increase in CSPG. Cholera toxin and dBcAMP also dramatically stimulated hyaluronan synthesis by possible phosphorylation induced activation of hyaluronan synthase(s).

1-Methyl-3-isobutylxanthine↗
PubMed1998

[Complications of vascular surgery].

Vascular surgery, which in certain life-threatening situations is the only possible therapeutic option, has progressed considerably since its beginning in the 1950s. Because of the constant progression of vascular diseases, this surgery will present, in the forthcoming years, a major public health problem. Because of advances in medico-surgical management, evermore elderly and frail patients can be treated. Perioperative mortality is constantly decreasing, but much progress remains to be accomplished to prevent, avoid or treat, postoperative complications. They are common and serious in these typical patients with cardiovascular diseases (men over 50 years of age, heavy smokers, atheromatous ...). The AA divide these complications into 3 main groups depending on the surgical procedure: abdominal aortic surgery, carotid surgery and arterial and venous surgery of the lower limbs. There is much data on abdominal aortic surgery because these long and complex procedures produce repercussions often involving many systems. The postoperative complications are treated according to the system they involve: cardiovascular, the most serious, respiratory, the commonest, alimentary, neurological, renal, others, as well as combined systems. The AA do not deal with the specific problems associated with cardiac and cardio-thoracic surgery. The AA discuss the different epidemiological findings of the large surgical series published in the 1970s and 1980s. The more recent literature analyses the relationship between preoperative risk factors (atheroma, COAD, hypertension ...), peroperative problems (surgical difficulties, emergencies, massive transfusions, others) and the corresponding postoperative morbidity. Thus a few general outlines of the physiopathology of these different complications emerge. In the light of these notions the few proposed methods will be evaluated in order to improve the preoperative condition of the vascular patient. The AA also review the relevance of the preoperative investigation in patients for vascular surgery. All these measures aim at reducing the incidence and severity of perioperative morbidity.

Aorta, Abdominal↗
PubMed1997

IGF-1 stimulates synthesis of undersulfated proteoglycans and of hyaluronic acid by peritubular cells from immature rat testis.

The exposure of confluent peritubular (PT) cells from immature rat testis to insulin-like growth factor-1 (IGF-1) induced a time and dose-dependent increase of [35S]-sulfate and [3H]-D-glucosamine incorporations in newly synthesized proteoglycans (PG). This increased content of PG was the result of an enhancement of PG synthesis rather than a decreased rate of degradation. IGF-1 had no effect on the molecular weight of synthesized PG nor on the nature and distribution of the constitutive glycosaminoglycan chains, both in medium and in cell layer. The stimulation of PG synthesis by IGF-1 appeared to be due, at least partially, to an increase of glycosylation processes. IGF-1 effect was mediated by the classical tyrosine kinase signalling process, since IGF-1 action on PG synthesis was abolished by genistein and tyrphostin A9, two well known tyrosine kinase inhibitors. The increase of PG synthesis was accompanied with an undersulfation of constitutive glycosaminoglycan (GAG) chains (chondroitin sulfate and heparan sulfate chains) since the [35S]/[3H] ratio was reduced by about 20-25% in presence of IGF-1. Although the mechanism of hyaluronic acid synthesis was completely different from those of other GAG, IGF-1 also dramatically enhanced its production by PT cells.

Animals↗
PubMed1996

Transfer of cholesterol between high density lipoproteins and cultured rat Sertoli cells.

In the testes, the Sertoli cells are separated from the blood capillaries by the basement membrane, thereby excluding the passage of low density lipoproteins (LDLs) but allowing the passage of high density lipoproteins (HDLs). The present study examines first the capacity of Sertoli cells to uptake cholesterol from HDL and secondly the role of apolipoproteins (apo) A-I and E in cholesterol flux between HDL and cultured rat Sertoli cells. In the presence of HDL in cultured medium, rat Sertoli cells accumulated few amounts of esterified cholesterol. Incubation of [14C] cholesterol-labelled Sertoli cells with [3H]cholesterol-labelled HDL showed that the amount of cholesterol influx slightly exceeded its efflux, thus resulting in a net uptake of cholesterol from HDL to rat Sertoli cells. The amount of HDL-cholesterol converted to steroids by Sertoli cells was about 32% of influx. Uptake of cholesterol by Sertoli cells was three times higher with phospholipid-apo A-I vesicles and seven times higher with phospholipid- apo E vesicles than that with phospholipid vesicles without apolipoprotein. Phospholipid- apo A-I vesicles promoted cholesterol efflux at the same rate as native HDL and twice as efficiently as phospholipid- apo E vesicles. Thus, this study shows that rat Sertoli cells have the capacity to take up HDL-cholesterol for membrane renewal and steroid production mainly by apo E dependent pathways.

Animals↗
PubMed1996

[Synthesis of proteoglycans by purified Leydig cells in immature rats and mature rats].

In Percoll purified Leydig cells from mature rat incubated for 24 h in Ham F12/DME medium, we demonstrated that the testosterone production (6 ng/10(6) Leydig cells/24 h) is increased 11 fold by a saturating amount of hCG whereas rat Leydig cells the basal output of testosterone is 4.5 ng and increased 2.5 fold by hCG. In the sulfate-free Ham F12/DME medium used for the proteoglycan (PG) studies, the productions of testosterone are lower but the cells remain sensitive to hCG. Whatever the age, the Leydig cells synthesize labeled PG after 24 h of incubation in the presence of [3H] glucosamine and [35S] sulfate. In immature rat, the quantity of synthesized PG is 20% higher than in mature animal; the secreted PG represented respectively 70 and 85% of the immature and mature Leydig cells PG outputs. In addition, the immature Leydig cell HSPG represents 15% of the secreted PG whereas it is 5% in mature rat; irrespective of the age the associated-HSPG account for 10% of the PG. The addition of hCG improves the production of HSPG especially in the immature Leydig cells. Therefore we evidenced a rat Leydig cell synthesis of PG, especially HSPG which are likely involved in the regulation of the Leydig cell function.

Age Factors↗
PubMed1995

Inhibition of proteoglycan synthesis induces an increase in follicle stimulating hormone (FSH)-stimulated estradiol production by immature rat Sertoli cells.

In order to define the possible involvement of proteoglycans (PG) in the regulation of Sertoli cell functions, we have examined the effect of para-nitrophenyl-beta-D-xyloside (PNPX), a specific inhibitor of PG synthesis, on follicle stimulating hormone (FSH)-dependent estradiol production by immature rat Sertoli cells. Addition of PNPX to the culture medium induced a dose-dependent inhibition of 35S-labeled PG synthesis in Sertoli cells both in the medium and the cell layer. Simultaneously there was a drastic increase in 35S-labeled secreted glycosaminoglycans. By 1 mM PNPX, syntheses of chondroitin sulfate proteoglycans released into culture medium and of heparan sulfate proteoglycans associated with the cell layer were 35% of values from untreated cells. Simultaneously, PNPX induced a twofold (mean of seven experiments, range 17-250%) enhancement of FSH (100 ng/ml)-stimulated estradiol production. In each individual experiment, there was an inverse relationship between the amplitude of PNPX-induced increase in FSH responsiveness and the FSH capability to stimulate basal estradiol production in cultured rat Sertoli cells. The effect of PNPX on FSH-stimulated aromatase activity was not mimicked by para-nitrophenyl-beta-D-galactoside, a structural analog of PNPX that has no effect on PG synthesis. The (Bu)2cAMP-stimulated estradiol synthesis was not modified in the presence of PNPX. Moreover, PNPX enhancement of FSH-stimulated estradiol synthesis disappeared when Sertoli cells were cultured in the presence of 1-methyl-3-isobutylxanthine, an inhibitor of phosphodiesterase activity. These findings suggest that inhibition of PG synthesis under PNPX conditions did not affect signal transduction steps distal to cAMP but rather decreased the phosphodiesterase activity in Sertoli cells.(ABSTRACT TRUNCATED AT 250 WORDS)

1-Methyl-3-isobutylxanthine↗
PubMed1995

Progesterone secretion and proliferation in cultured rabbit granulosa cells under conditions of beta-D-xyloside-induced inhibition of proteoglycan synthesis.

Proteoglycans present in follicular fluid are synthesized by granulosa cells under gonadotropin control. An inhibitor of proteoglycan synthesis, p-nitrophenyl-beta-D-xyloside (beta-D-xyloside) was used as a probe to study rabbit granulosa cell steroidogenesis and proliferation under abrogated proteoglycan synthesis. Granulosa cells isolated from rabbit preovulatory follicles were cultured 24 h in Minimum Essential Medium plus 2.5% fetal calf serum in the presence or absence of beta-D-xyloside and were then treated with FSH or dibutyryl cAMP (db-cAMP) alone or in combination with beta-D-xyloside for a further 24 h. The exposure for 48 h of granulosa cells to 1 mM beta-D-xyloside in the absence or presence of FSH inhibited proteoglycan synthesis and increased the amount of glycosaminoglycans (GAG). FSH-stimulated progesterone production was significantly correlated only with proteoglycan synthesis and not with GAG production. The addition of various concentrations of beta-D-xyloside (0.1-4 mM) for 48 h to granulosa cells induced a dose-dependent inhibition of FSH-stimulated progesterone secretion and [3H]thymidine incorporation into DNA. beta-D-Xyloside concentrations lower than 1 mM induced an inhibition of FSH-stimulated progesterone secretion but had no significant effect on FSH-induced proliferation. One millimolar beta-D-xyloside did not modify basal progesterone production, but in the presence of various doses (0.1-2.5 ng/ml) of FSH or hCG (0.1-1 IU/ml) it exerted a significant inhibitory effect on steroid secretion. Fifty percent inhibition was obtained for doses of FSH above 0.5 ng/ml.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗
PubMed1994

Membrane associated proteoglycans in rat testicular peritubular cells.

Confluent testicular peritubular cells derived from immature rats were used to study membrane associated proteoglycans (PG). Peripheral material (heparin releasable), membrane and intracellular material (Triton X-100 releasable) were collected, purified by anion exchange chromatography then characterized by gel filtration and by hydrophobic interaction chromatography, followed by enzymatic digestion and chemical treatment. The peripheral material was constituted of two populations of PG (Kav = 0 and 0.10 on Superose 6 column), each containing both heparan sulfate proteoglycans (HSPG) and chondroitin proteoglycans (CSPG) and perhaps a hybrid PG (HSCSPG). These PG being not retained on an octyl Sepharose column, they were devoided of hydrophobic properties. The integral membrane proteoglycans isolated on the basis of their hydrophobic properties represented 20% of the Triton X-100 releasable material, and were exclusively constituted of proteoheparan sulfate. There were no relationships between this membrane HSPG and the peripheral HSPG as evidenced by pulse chase experiments. The mode of intercalation of the hydrophobic HSPG in the cell membrane was studied. The majority of these macromolecules (80%) were sensitive to trypsin and only a minor proportion (20%) were sensitive to phosphatidylinositol specific phospholipase C. Thus, about 80% of the hydrophobic HSPG were intercalated in the cell membrane by a hydrophobic segment of the core protein whereas about 20% were associated with the cell membrane via a phosphatidylinositol residue covalently bound to the core protein of the PG.

Animals↗
PubMed1994

Effects of transforming growth factor-beta 1, interleukin-1 alpha and interleukin-6 on rat Sertoli cell proteoglycan synthesis.

In the testis, growth factors and cytokines are synthesized by Sertoli cells and peritubular cells. In different cell types, these mediators are known to regulate the metabolism of extracellular matrix molecules, such as proteoglycans. In this study, we have tested the action of three of these mediators (IL-1 alpha, IL-6 and TGF-beta 1) on the proteoglycan synthesis of rat Sertoli cells. The proteoglycan synthesis was unchanged by IL-1 alpha, nor by IL-6 up to 20 ng/ml, during any maturation stage (14, 21 and 35 days). By contrast, Transforming Growth Factor-beta 1 (TGF-beta 1) enhanced Sertoli cell proteoglycan production from 21 day-old rats, with an optimal response at 1 ng/ml. Kinetic studies showed that the effect of TGF-beta 1 (1ng/ml) was higher after 24 hours of incubation. In presence or in absence of TGF-beta 1, a proteoglycan accumulation was observed in the extracellular compartment between 12 and 48 hours, but this factor did not modify the proteoglycan distribution between cell layer and medium. Furthermore, TGF-beta 1 increased proteoglycan anabolism at all Sertoli cell maturation stages studied but this stimulation was greater for the early maturation stages (14 and 21 days). On the other hand, proteoglycan catabolism was not modified by TGF-beta 1. In conclusion, TGF-beta 1 secreted by rat Sertoli and peritubular cells could modulate, in an autocrine/paracrine way the synthesis of one of the main extracellular matrix components.

Animals↗
PubMed1993

Synthesis and distribution of rat Sertoli cell proteoglycans are modulated by linoleate and vitamin E.

In rat Sertoli cells, linoleate addition modified cell membrane fatty acid composition and changes depended on linoleate concentrations. In presence of the lowest 18:2 n-6 concentrations (2.5 and 7.5 microM), decrease in proteoglycan synthesis paralleled increase in n-6 linoleate-derived metabolites. At high concentration (21 microM), linoleate accumulated in membranes and level of n-6 linoleate-derived metabolites returned to basal value, without change in proteoglycan synthesis. Linoleate modified proteoglycan distribution in Sertoli cells by an increase in peripheral proteoglycans and a concomitant decrease in medium proteoglycans. Vitamin E (100 microM) did not alter fatty acid composition in control and linoleate-treated cells, but enhanced proteoglycan production. Furthermore, this agent counteracted linoleate-induced modifications in proteoglycan cell distribution.

Animals↗