A M Säämänen

University of Turku, Turku, Province of Western Finland, Finland

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Publications (35)101.68 Total impact

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    ABSTRACT: To study the expression and distribution of transcription factor Sox9 and type IIA procollagen in the developing and aging eyes of normal and transgenic Dell mice carrying pro(alpha)1(II) collagen transgenes with a short deletion mutation, which cause ocular abnormalities in this mouse line. The eyes of Del1 mice were studied on embryonic days E14.5, E16.5 and E18.5, and at the ages of 4 and nine months, using their nontransgenic littermates as controls. Sox9 and pro(alpha)1(IIA) collagen were detected by RNase protection assay and immunohistochemistry. RNase protection assay revealed Sox9 transcripts in the eyes of Del1 and control mice during development and aging. The mRNA for type IIA procollagen had a similar temporal expression pattern. On embryonic days E14.5, E16.5 and E18.5, Sox9 was located by immunohistochemistry in the nuclei and type IIA procollagen in the extracellular space of the developing retina. During growth and aging, the ocular expression of Sox9 mRNA and the immunohistochemical reaction for Sox9 antibody diminished, concomitant with the reduction in type II procollagen mRNA. However, at the age of nine months, levels of Sox9 and type IIA procollagen mRNAs were higher in the degenerating eyes of Del1 and control mice. The similarities in the temporo-spatial distribution of Sox9 and type IIA procollagen suggest that this transcription factor is involved in the activation of type II collagen expression in the eye, as has been demonstrated in prechondrogenic mesenchyme and immature cartilage. The increased production of Sox9 and type IIA procollagen in the aging retina and vitreous is analogous to degenerating articular cartilage where attempted tissue repair has also been observed.
    European journal of ophthalmology 01/2002; 12(6):450-8. · 0.91 Impact Factor
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    Arthritis Research & Therapy 01/2002; 4:1-1. · 4.30 Impact Factor
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    ABSTRACT: The genomic structure of murine fibromodulin was determined, and its age-related expression and distribution were characterized in knee epiphyses, with decorin studied for reference. Fibromodulin, as well as decorin, have roles in collagen fibrillogenesis both in vitro and in vivo. The murine fibromodulin gene, Fmod, was similar with that in other species, with three exons and 86% of the translated sequence in exon 2. The 2.7 kb long cDNA contains an open reading frame of 1131 nt. Fibromodulin mRNA levels were highest in tissues rich in fibrillar collagens type I or type II. During growth, the distribution of fibromodulin mRNA was similar with that of type II collagen, with the highest levels between 5 days and 1 month of age. Thereafter, the expression of type II collagen declined to a level near the detection limit, whereas the fibromodulin expression decreased less markedly to a level of approx. 35% of maximum, and remained constant throughout the rest of the observation period. In contrast, decorin mRNA levels were the highest in old animals. Pericellular deposition of fibromodulin was strong around the late-hypertrophic chondrocytes of the secondary ossification centre and in the growth plate. In young epiphyses, both fibromodulin and decorin were found interterritorially, mainly in the uncalcified and deep-calcified cartilage. In the old mice, calcified cartilage became enriched with regard to fibromodulin, while, in contrast, decorin deposition diminished, particularly near the tidemark. In the subchondral bone trabeculae, decorin was found in the endosteum of growing, but not in the mature, epiphyses. Differences in the expression and distribution profiles suggest different roles for fibromodulin and decorin in the regulation of collagen fibrillogenesis, maintenance of the fibril organization and matrix mineralization. As fibromodulin is deposited closer to cells than decorin, it may have a primary role in collagen fibrillogenesis, whereas decorin might be involved in the maintenance of fibril structures in the interterritorial matrix.
    Biochemical Journal 06/2001; 355(Pt 3):577-85. · 4.65 Impact Factor
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    ABSTRACT: Although the presence of 'cartilage-specific' collagens in the eye has been documented earlier, very little is known about their synthesis rates during ocular development, growth and aging. The purpose of the present study was to follow changes in the mRNA levels and distribution of key components of the extracellular matrix in the eyes of normal and transgenic Del1 mice, harboring a short deletion mutation in the type II collagen gene, during ocular growth and aging. Total RNAs extracted from mouse eyes were studied by Northern analysis for mRNA levels of type I, II, III, VI, IX and XI collagens, biglycan, fibromodulin and decorin. A predominant finding of the present study was the marked reduction in the mRNA levels of type I and II collagens in the eye upon aging. The changes in the mRNA levels of type III and VI collagen and proteoglycans were smaller. Localization of type II and IX collagen in the eye was performed by immunohistochemistry. Despite the reduction in the type II collagen mRNA levels, immunohistochemistry confirmed widespread distribution of the protein also in aging mouse eyes, suggesting its slow turnover. Although the Del1 mutation caused gradual degenerative lesions in the eyes, the distribution of the protein remained essentially unchanged. The widespread distribution and marked downregulation of type II collagen production in the mouse eye upon aging probably explain the gradual development of degenerative lesions, particularly in the eyes of transgenic Del1 mice, where production of mutant type II collagen chains also contributes to the process.
    Experimental Eye Research 05/2001; 72(4):423-31. · 3.03 Impact Factor
  • Heli Salminen, Eero Vuorio, Anna‐Marja Säämänen
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    ABSTRACT: Objective To determine the capacity of chondrocytes in aging and degenerating articular cartilage to produce major components of the extracellular matrix and maintain the normal structure of articular cartilage in a transgenic mouse model of osteoarthritis.Methods Transcription factor Sox9 was used as an indicator of the activation and maintenance of the articular chondrocyte phenotype. Knee joints of Del1 mice carrying 6 copies of the pro1(II) collagen transgene with a short deletion mutation were analyzed at the age of 10 days and at 2, 3, 4, 6, 9, and 15 months by Northern hybridization, RNase protection assay, quantitative reverse transcription–polymerase chain reaction, and immunohistochemistry. Nontransgenic littermates were used as controls.ResultsWe demonstrated the presence of Sox9 in articular chondrocytes during development, growth, and aging, with the highest messenger RNA levels during the period of rapid growth. With the appearance of degenerative lesions in articular cartilage, 2 repair processes were observed. Local proliferation and activation of chondrocytes rich in Sox9, surrounded by type IIA procollagen and proteoglycans, was seen in articular cartilage. In contrast, metabolically inactive chondrocytes were observed at the margins of the defects. They were devoid of Sox9 and were surrounded by a proteoglycan-poor matrix. Sometimes, the lesions were filled with repair tissue that contained type III collagen but little proteoglycan or type II collagen.Conclusion The results indicate that chondrocytes in mature articular cartilage are capable of inducing the production of Sox9 and type IIA procollagen, which is typical of early chondrogenesis. Degenerative defects in the knee joints of transgenic Del1 mice are associated with local activation of chondrocytes, which probably contributes to the repair process. In other areas, the repair process produces a noncartilaginous matrix, which is insufficient to maintain the integrity of articular cartilage and which allows degeneration to proceed.
    Arthritis & Rheumatology 04/2001; 44(4):947 - 955. · 7.48 Impact Factor
  • H Salminen, E Vuorio, A M Säämänen
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    ABSTRACT: To determine the capacity of chondrocytes in aging and degenerating articular cartilage to produce major components of the extracellular matrix and maintain the normal structure of articular cartilage in a transgenic mouse model of osteoarthritis. Transcription factor Sox9 was used as an indicator of the activation and maintenance of the articular chondrocyte phenotype. Knee joints of Del1 mice carrying 6 copies of the pro alpha1(II) collagen transgene with a short deletion mutation were analyzed at the age of 10 days and at 2, 3, 4, 6, 9, and 15 months by Northern hybridization, RNase protection assay, quantitative reverse transcription-polymerase chain reaction, and immunohistochemistry. Nontransgenic littermates were used as controls. We demonstrated the presence of Sox9 in articular chondrocytes during development, growth, and aging, with the highest messenger RNA levels during the period of rapid growth. With the appearance of degenerative lesions in articular cartilage, 2 repair processes were observed. Local proliferation and activation of chondrocytes rich in Sox9, surrounded by type IIA procollagen and proteoglycans, was seen in articular cartilage. In contrast, metabolically inactive chondrocytes were observed at the margins of the defects. They were devoid of Sox9 and were surrounded by a proteoglycan-poor matrix. Sometimes, the lesions were filled with repair tissue that contained type III collagen but little proteoglycan or type II collagen. The results indicate that chondrocytes in mature articular cartilage are capable of inducing the production of Sox9 and type IIA procollagen, which is typical of early chondrogenesis. Degenerative defects in the knee joints of transgenic Del1 mice are associated with local activation of chondrocytes, which probably contributes to the repair process. In other areas, the repair process produces a noncartilaginous matrix, which is insufficient to maintain the integrity of articular cartilage and which allows degeneration to proceed.
    Arthritis & Rheumatology 04/2001; 44(4):947-55. · 7.48 Impact Factor
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    ABSTRACT: To investigate the suitability of cartilage oligomeric matrix protein (COMP) as a marker for articular cartilage degeneration in a transgenic mouse model of osteoarthritis (OA). Northern blot analysis of total RNA extracted from the knee joints of transgenic Del1 mice, which harbor a short deletion in a type II collagen transgene, and of their nontransgenic littermates was used to monitor changes in COMP messenger RNA (mRNA) levels during cartilage degeneration. Immunohistochemistry was used to determine the distribution of COMP in articular cartilage, and serum levels of COMP were measured by immunoassay. Transient up-regulation of COMP mRNA was seen in articular cartilage of transgenic Del1 mice at the onset of OA lesions at the age of 3 months. Compared with nontransgenic controls, COMP immunostaining of articular cartilage in 3-9-month-old transgenic mice was increased, especially at the border of uncalcified and calcified cartilage. There was also a change from predominantly interterritorial to pericellular/territorial deposition of COMP. This difference persisted until the age of 15 months, when the nontransgenic controls also demonstrated articular cartilage degeneration and increased COMP immunostaining. Increased serum levels of COMP were seen in Del1 mice at the age of 4 months, correlating temporally with the onset of cartilage degeneration. These findings suggest that upregulation of COMP mRNA and redistribution of the protein are characteristic of the early stages of articular cartilage degeneration in the transgenic mouse model in which OA results from a dominant-negative mutation in the type II collagen gene. The data provide additional support for the notion that COMP is a useful marker for altered cartilage metabolism in developing OA.
    Arthritis & Rheumatology 09/2000; 43(8):1742-8. · 7.48 Impact Factor
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    ABSTRACT: To perform a systematic study on the production and deposition of type X collagen in developing, aging, and osteoarthritic (OA) mouse articular cartilage. Immunohistochemistry was employed to define the distribution of type X collagen and Northern analyses to determine the messenger RNA levels as an indicator of the synthetic activity of the protein. Type X collagen was observed in the epiphyseal and articular cartilage of mouse knee joints throughout development and growth. Type X collagen deposition in the transitional zone of articular cartilage became evident toward cessation of growth, at the age of 2-3 months. The most intense staining for type X collagen was limited to the tidemark, the border between uncalcified and calcified cartilage. Northern analysis confirmed that the type X collagen gene is also transcribed by articular cartilage chondrocytes. Intense immunostaining was observed in the areas of OA lesions, specifically, at sites of osteophyte formation and surface fibrillation. Type X collagen deposition was also seen in degenerating menisci. This study demonstrates that type X collagen is a natural component of mouse articular cartilage throughout development, growth, and aging. This finding and the deposition of type X collagen at sites of OA lesions suggest that type X collagen may have a role in providing structural support for articular cartilage.
    Arthritis & Rheumatology 08/1998; 41(7):1287-95. · 7.48 Impact Factor
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    ABSTRACT: Skull morphology and histology in the heterozygous offspring of a transgenic founder mouse Del1, harbouring 6 copies of deletion mutation in Col2a1 gene, were compared with those in normal siblings. On visual observation and roentgenocephalometric examination the heads of heterozygous Del1 mice were smaller than normal. Histologically the sizes of cartilaginous structures of the cranial base were reduced. Severe defects were seen in the temporomandibular joint as progressive osteoarthritic lesions. These observations elucidate the relationship between the genotype and phenotype and demonstrate that heterozygous Del1 mice are a useful model for studies on a genetic disturbance where 'clinical' manifestations are not evident until adult age.
    Journal of Anatomy 03/1997; 190 ( Pt 2):201-8. · 2.36 Impact Factor
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    ABSTRACT: The levels of six mRNAs coding for constituent alpha-chains of three minor collagens of cartilage were analyzed in an experimental fracture model in normal and transgenic Del1 mice harboring a deletion mutation of exon 7 in the type II collagen gene. Reduced and retarded chondrogenesis in Del1 mice was evident in callus samples as reduced mRNA levels for the cartilage specific type IX and XI collagens at days 7 and 9 of fracture healing. Analysis of the calluses for alternative splicing of pro alpha 1(II) collagen mRNA also suggested retarded chondrogenesis in Del1 calluses. Another developmentally regulated step in limb development, a switch between alternative promoters of the alpha 1(IX) collagen gene, was also seen during fracture healing but was less obvious in Del1 calluses. Finally, the current data suggest that the abnormality in bone remodelling in Del1 mice involves activation of the genes coding for alpha 1(XI) and alpha 2(VI) collagens.
    FEBS Letters 06/1995; 364(2):171-4. · 3.58 Impact Factor
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    ABSTRACT: The recovery of articular cartilage from atrophy induced by joint immobilization was investigated in immature dogs. In a previous study, we showed that 11 weeks of immobilization of the knee (stifle) joint of young dogs reduced the concentration of articular cartilage glycosaminoglycans (GAGs) by 13-47%. In the present study, right hindlimbs from six female beagles were immobilized for 11 weeks, as in the previous study, and then were remobilized for 15 weeks. Cartilage from the knee joint was compared with cartilage from nonimmobilized knees of eight age-matched control beagles. Histological samples taken from 11 different locations of the knee joint were stained with safranin O, and microspectrophotometry was used to demonstrate distribution of GAGs in the tissue. After remobilization, GAG concentration was restored in the patellofemoral region and tibial condyles. On the summits of the femoral condyles, and especially at the periphery of the femoral condyles, GAG concentration remained 8-26% less than the control values. On the summits, the thickness of the uncalcified cartilage was as much as 15% less than in the age-matched controls. Consequently, the changes induced by unloading were reversible to a great extent, but a full restoration of articular cartilage was not obtained at all sites of the knee joint within the 15 weeks of remobilization. Immobilization of the skeletally immature joint therefore may affect the development of articular cartilage in such a way that very slow recovery or permanent alterations are induced.
    Journal of Orthopaedic Research 04/1994; 12(2):161-7. · 2.88 Impact Factor
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    ABSTRACT: The effects of long distance running training on blood parameters, hormone responses and bone growth were studied in young growing dogs. A genetically uniform group of female beagles matched with respect to age and body mass were used. The runner dogs (n = 10) underwent gradually increased running exercise up to 40 km.day-1 on a treadmill with 15 degrees uphill gradient 5 days each week during a period of 1 year, while the littermate control dogs (n = 10) were kept in their cages throughout the study. Low plasma lactate concentrations of the runners measured immediately after the running training indicated the aerobic metabolism of the dogs while running. Significant decreases of blood haemoglobin concentrations (11%), blood erythrocyte number (10%), and erythrocyte packed cell volume (12%) were found in the runner group. Throughout the experiment, the value of thyroxine was slightly lower (13%) in the runners but no changes were found in tri-iodothyronine, free thyroxine, or cortisol serum concentrations. Serum oestradiol concentration at 56 weeks was significantly lower (42%) in the runner group than in the control group but was not as low (27%) at 70 weeks. Somatomedin-C concentration had decreased significantly by 37% at the age of 56 weeks in the runner group but was again at the level of the control dogs at the end of experiment (at 70 weeks). Ulna and radius bone mass as a ratio to the body mass had significantly increased in the runners. It would seem from our study that long distance running has a positive effect on bone growth.(ABSTRACT TRUNCATED AT 250 WORDS)
    European Journal of Applied Physiology and Occupational Physiology 02/1993; 67(4):321-9.
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    ABSTRACT: Collagen and proteoglycans in the intervertebral disc (LI-II) of young beagle dogs (age 55 weeks) were analyzed following a 15 weeks' daily 20 km running training on a treadmill with 15 degree uphill inclination. In nucleus pulposus no statistically significant alterations were found in the content of proteoglycans or collagen. In annulus fibrosus the total tissue wet weight and total amount of collagen (hydroxyproline) increased by 34-36% in the runners as compared to age-matched, untrained controls. Since the total amount of proteoglycans did not increase, the annulus fibrosus became relatively depleted of proteoglycans, as indicated by the 27% reduction in uronic acid concentration, expressed either per wet weight or hydroxyproline. The average molecular size of the remaining nonaggregating proteoglycans was larger, and there was also a trend towards increased proportion of proteoglycans aggregating with hyaluronan. Most of the chondroitin sulfate side chains were 6-sulfated (65-66%). Running did not alter the sulfation or length of the chondroitin sulfate chains. The decreased proteoglycan/collagen ratio in annulus fibrosus may result in altered mechanical properties of the tissue and reflects its adaptation to enhanced motion and stress.
    International Journal of Sports Medicine 02/1993; 14(1):48-51. · 2.27 Impact Factor
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    ABSTRACT: The influences of the strenuous running training program on the knee joint articular cartilage was studied in six female beagle dogs. At the age of 15 weeks, the dogs started running on a treadmill inclined 15 degrees uphill. Thereafter, the dogs were trained for 40 weeks, five times a week. For the final 15 weeks, the dogs ran 20 km/day. Six age-matched female beagles served as controls. The cartilage surfaces were intact after the running exercise. The training reduced the thickness of the uncalcified cartilage by 6% in the medial femoral condyle. The glycosaminoglycan concentration was reduced an average of 11% on the summits of the femoral condyles. The reduction was most pronounced (41%) in the superficial 50-micron cartilage zone. In other regions of the knee, such a decrease of glycosaminoglycans was not observed. A shift to strenuous running voided the increase in cartilage thickness and proteoglycan content previously observed after moderate running. Strenuous running induced marked depletion of proteoglycans from the superficial layer of the femoral condyles at sites subjected to highest impact loads.
    Clinical Orthopaedics and Related Research 11/1992; · 2.79 Impact Factor
  • Duodecim; lääketieteellinen aikakauskirja 02/1992; 108(12):1097-107.
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    R Tammi, A M Säämänen, H I Maibach, M Tammi
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    ABSTRACT: Human whole skin was labeled for 24 h with [6-3H]-glucosamine in organ culture and epidermis, dermis and culture medium were separately analyzed for the molecular mass and content of the [3H]-labeled hyaluronan (HA). Gel filtration on Sephacryl S-1000 of HA purified by HPLC showed a large proportion of the newly synthesized HA to be of a very high molecular mass (greater than 2 X 10(6) Da) in both epidermis and dermis, whereas HA in the medium was of a smaller size. After 24 h chase, most of the high molecular mass HA, and 42-48% of total labeled HA disappeared from both tissue compartments. The size of labeled HA recovered in the chase media was further reduced but the content roughly corresponded to that lost from tissue. The amount of unlabeled HA was not significantly altered in epidermis, whereas in dermis it was reduced to about 10% of the initial values during 5-d culture. The results demonstrate that HA of both epidermis and dermis is synthesized as a very high molecular mass compound but rapidly undergoes a limited degradation into large fragments. The fragmentation of HA is suggested to enhance its diffusion from the tissues, particularly dermis.
    Journal of Investigative Dermatology 08/1991; 97(1):126-30. · 6.19 Impact Factor
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    ABSTRACT: The distribution of proteoglycans (PGs) at 11 sites on the knee (stifle joint) cartilage of young female beagle dogs was studied following cast immobilization for 11 weeks in 90 degrees flexion and after a subsequent remobilization for 15 weeks. Immobilization induced a reduction in PG uronic acid at all sites (mean of -38%), but the greatest depletion (-64%) occurred at the anterior and posterior extremes of the femoral condyles, i.e., at locations where the immobilized cartilage lost contact to the opposing cartilage. Following remobilization, the content of uronic acid remained lower than in the age-matched controls (-18% on average), particularly at the minimum contact sites most affected by immobilization (-33%). The chondroitin-6-sulfate to chondroitin-4-sulfate ratio was reduced by immobilization in most locations (average of -14%) and returned to control values after remobilization. There was no consistent change in the percentage of aggregating PGs observed in Sephacryl S-1000 gel filtration after immobilization or remobilization. However, following remobilization, the aggregating PGs showed an enhanced proportion of the slower mobility band in agarose gel electrophoresis, indicative of a larger monomer size. In the contralateral, load-bearing knee joint, both the uronic acid content and PG monomer type distribution were identical to those observed in the experimental joint, suggesting that the state reached after the remobilization period was due to factor(s) influencing both sides. The results suggest that contact forces between articulating surfaces are required to maintain normal PG content and that the control mechanism works locally at each cartilage site. Restriction of joint mobility and loading in young animals is concluded to cause persistent changes in cartilage matrix. Furthermore, the use of the contralateral joint as the sole control in this kind of studies, although experimentally convenient, seems not to be appropriate.
    Journal of Orthopaedic Research 12/1990; 8(6):863-73. · 2.88 Impact Factor
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    ABSTRACT: The indentation stiffness of knee articular cartilage subjected to strenuous physical training (SPT: treadmill running 20 km day-1 for 15 weeks, n = 6) of young Beagles was tested and compared to that obtained from age-matched (55 weeks, n = 9) controls. The mathematical solution for the shear modulus, as determined from indentation of an elastic layer bonded to a rigid half space, was extended to small Poisson's ratios and applied to the analysis of cartilage response after a step stress (0.39 MPa) application. In these measurements with an impervious, plane-ended indenter, the equilibrium deformation was systematically greater than values predicted from the instant response by the linear biphasic theory. Therefore, the accurate determination of Poisson's ratio from the creep curves was not possible. The mean shear modulus (calculated by using the deformation at 900 s after load application and assuming a constant Poisson's ratio of 0.40 for the matrix) of canine knee articular cartilage was 0.37 MPa. While the cartilage thickness was not affected by SPT, the cartilage of the lateral tibial plateau was stiffer (13.3%, p less than 0.05) than that in controls. However, in the femoral condyles, the stiffness was at the control level or even below. Our results on cartilage structure and properties suggest that SPT, in contrast to our previous findings with moderate training, does not necessarily improve the biological properties of articular cartilage in young animals.
    Journal of Biomechanics 02/1990; 23(12):1239-46. · 2.72 Impact Factor
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    ABSTRACT: The levels and types of proteoglycans in articular cartilage of the knees of young beagle dogs were studied after 15 weeks of running exercise, at 4 km/day. Running increased the levels of proteoglycans in the cartilage of the patella, the superior patellofemoral groove, and the summit of the medial condyle of the femur, all of which are considered contact sites subject to enhanced loading caused by running. The elevated content of uronic acid at the femoral sites proved to be due to proteoglycans that were unable to aggregate with hyaluronic acid. There was no change in the content of aggregating proteoglycans. Analysis of chondroitinase AC-derived disaccharides at the same sites showed an increase in chondroitin-6-sulfate content as compared with chondroitin-4-sulfate levels. We believe that this modulation of the proteoglycan matrix reflects enhanced tissue maturation and physiologic adjustment to higher local contact pressures.
    Arthritis & Rheumatology 11/1989; 32(10):1282-92. · 7.48 Impact Factor
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    ABSTRACT: The restoration of the biomechanical properties of articular cartilage was studied after 15 weeks of remobilization of the knee joint in beagles previously immobilized with a cast for 11 weeks. The shear moduli were determined with an indentation creep test immediately after load application and at equilibrium at six predefined test points of femoral, tibial, and patellar cartilages. Permeability of the cartilage was estimated from the creep measurements. The values were compared with nontreated, age-matched (55 weeks) controls and with cartilage collected immediately after immobilization. Remobilization reduced the high creep rates created by immobilization and shifted the depressed equilibrium shear moduli towards those of the controls. However, in the femoral condylar cartilage, the equilibrium shear modulus remained at lower level (p less than 0.05) and permeability at higher level (p less than 0.05) as compared with the controls. We conclude that articular cartilage, showing signs of atrophy after long-term immobilization, was capable of restoring its biomechanical properties during remobilization. This repair was not, however, completed in all parts of the knee joint by the end of the observation period.
    Journal of Orthopaedic Research 02/1989; 7(3):352-8. · 2.88 Impact Factor

Publication Stats

1k Citations
101.68 Total Impact Points

Institutions

  • 1995–2001
    • University of Turku
      • Department of Surgery
      Turku, Province of Western Finland, Finland
  • 1992–1994
    • Kuopio University Hospital
      • Department of Surgery
      Kuopio, Province of Eastern Finland, Finland
  • 1984–1994
    • University of Kuopio
      • Department of Anatomy
      Kuopio, Eastern Finland Province, Finland