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1.
Arch Orthop Trauma Surg ; 120(1-2): 103-7, 2000.
Artigo em Inglês | MEDLINE | ID: mdl-10653115

RESUMO

Thirty-three X-press cementless stems (Depuy) manufactured according to standardized X-rays were inserted from 1992 to 1994. The patients' mean age was 49 (range 15-79) years with a mean follow-up of 32 (+/-6) months. A characteristic radiographic pattern of aseptic loosening with erosion of the medial cortex by the tip of the stem occurred in 28 patients and a valgus shift of the implant in 14 cases. A radiolucent line with increased sclerosis below the tip (zone Gruen 4) was observed in 17 cases. Four stems were revised due to histologically confirmed aseptic loosening. Biomechanical investigation of one of the revised stems with the typical pattern of valgus angulation and medial cortex erosion included photoelasticity and finite-element analysis. The intertrochanteric fit and fill obviously resulted in an unfavorable distribution of contact areas, including peaks of high stress on the medial tip of the stem. These experimental findings are even evident for a postulated rotational stability. The clinical and radiographic results of the cementless X-press stems do not seem to support the fixation concept of intertrochanteric fit and fill of femoral components.


Assuntos
Análise de Elementos Finitos , Prótese de Quadril , Falha de Prótese , Adolescente , Adulto , Idoso , Elasticidade , Humanos , Pessoa de Meia-Idade , Estresse Mecânico
2.
Calcif Tissue Int ; 62(2): 140-7, 1998 Feb.
Artigo em Inglês | MEDLINE | ID: mdl-9437047

RESUMO

Currently, primary osteoporosis is the most frequent metabolic disease in women after menopause [1]. The resulting loss of bone mass is accompanied by an increased risk of skeletal fragility. One reason for the development of osteoporosis might be an impaired function of mature osteoblasts. To evaluate the involvement of specific growth factors in bone remodeling, cell cultures of osteoblastic cells derived from nonosteoporotic and osteoporotic postmenopausal women were established. The influences of TGF beta-1 and IGF-I on proliferation and mRNA expression of TGF beta-1 were investigated by [3H]-thymidine incorporation and competitive RT-PCR. We found IGF-I to have no significant effect on proliferation in cells of osteoporotic and nonosteoporotic patients. In contrast, differences were found in TGF beta-1 mRNA expression after application of IGF-I. Application of TGF beta-1 enhanced its own mRNA expression in both groups in a similar manner. Whereas the proliferation of cells of nonosteoporotic patients was inhibited by (10(-10) M) TGF beta-1, this treatment led to an increased proliferation of cells of osteoporotic patients.


Assuntos
Fator de Crescimento Insulin-Like I/farmacologia , Osteoblastos/metabolismo , Osteoporose/metabolismo , RNA Mensageiro/biossíntese , Fator de Crescimento Transformador beta/farmacologia , Idoso , Idoso de 80 Anos ou mais , Ligação Competitiva/genética , Divisão Celular/efeitos dos fármacos , Células Cultivadas , Feminino , Fêmur/citologia , Fêmur/patologia , Humanos , Pessoa de Meia-Idade , Osteoblastos/citologia , Osteoblastos/patologia , Osteoporose/patologia , Reação em Cadeia da Polimerase , RNA Mensageiro/efeitos dos fármacos , Fator de Crescimento Transformador beta/biossíntese , Fator de Crescimento Transformador beta/genética
3.
Calcif Tissue Int ; 60(6): 501-5, 1997 Jun.
Artigo em Inglês | MEDLINE | ID: mdl-9164823

RESUMO

The aim of this study was to investigate the extent of lysyl and prolyl hydroxylation of collagen I in osteoporosis and compare it with collagen I from "bone healthy" individuals. Collagen I was isolated from femoral heads of osteoporotic women, from women suffering from osteoarthrosis of the hip, and from healthy women 60-85 years of age. The femoral heads were dissected into compact and trabecular bone of the neck region and from trabecular bone of the head region, and collagen I was extracted by limited pepsin digestion. The amino acid analysis of individual alpha-chains showed a remarkably higher degree of hydroxylation of lysine residues both in the alpha1(I)- and in the alpha2(I)-chains in osteoporotic bone compared with osteoarthrotic and "normal" bone, whereas the prolyl hydroxylation was nearly unchanged. The lysyl overhydroxylation was observed in the compact as well as in the trabecular bone of osteoporotic femoral heads. These biochemical alterations may play a crucial role in the pathogenesis of osteoporosis.


Assuntos
Colágeno/metabolismo , Cabeça do Fêmur/metabolismo , Fraturas do Quadril/fisiopatologia , Osteoporose Pós-Menopausa/fisiopatologia , Idoso , Idoso de 80 Anos ou mais , Aminoácidos/análise , Aminoácidos/metabolismo , Colágeno/química , Colágeno/isolamento & purificação , Eletroforese em Gel de Poliacrilamida , Feminino , Cabeça do Fêmur/patologia , Fraturas do Quadril/etiologia , Fraturas do Quadril/metabolismo , Humanos , Hidroxilação , Pessoa de Meia-Idade , Osteoporose Pós-Menopausa/complicações , Tomografia Computadorizada de Emissão
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