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Orthopaedic Proceedings
Vol. 84-B, Issue SUPP_I | Pages - 28
1 Mar 2002
Navalòn LG Valle JS Alonso AL
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Purpose of the study: The aim of this work was to determine whether erythrocyte sedimentation rate (ESR), C-reactive protein (CRP) and alpha-1-antitrypsin (A1AT) levels are correlated significantly with early postoperative infectious complications after hip prosthetic surgery.

Materials and methods: This prospective study was conducted on 100 total hip replacements performed between 1994 and 1995. ESR, CRP and A1AT were obtained before surgery then at 1, 2 and 6 weeks after surgery.

Results: Seven bacteriologically proven cases of infection were reported. Infection was considered to be superficial if it did not extend deeper than the muscles fascia. There was a strong statistical correlation between A1AT level and infection for all postoperative times (p < 0.0001). A1AT was highly sensitive (87.5 p. 100) and specific (85.8 p. 100) for infection compared with ESR (sensibility 70 p. 100 and specificity 65.9 p. 100) and CRP (sensitivity 63.6 p. 100 and specificity 80.1 p. 100).

Discussion and conclusion: In our hands, A1AT can be a most useful diagnostic tool for infection after prosthesis hip surgery. Although not totally specific, it is highly sensitive for infection compared with other tools such as ESR and CRP more frequently used. These findings suggest an avenue of research on the role of A1AT in infectious complications after prosthetic joint surgery.


The Journal of Bone & Joint Surgery British Volume
Vol. 81-B, Issue 3 | Pages 522 - 530
1 May 1999
Santander RG Arriba MAP Cuadrado GM Alonso AL Martinez MG Alonso FJM Monteagudo M Lobo MVT

We have studied the formation of collagen fibrils in ‘activated fibroblasts’ of tendo Achillis of rabbits. The tendon was in the process of regeneration after experimental partial tenotomy. Samples were taken from the peri-incisional region and analysed by transmission electron microscopy.

Ultrastructural examination showed the presence of a ‘fine dense granular substance’ inside the rough endoplasmic reticulum and procollagen filaments. These come together to form collagen fibrils in the dilated vacuoles of the rough endoplasmic reticulum. The possible intra- and extracellular origin of collagen fibrils is suggested. Within the cell biosynthesis of collagen fibrils take place with the formation of collagen substance which gives rise to procollagen filaments. These make contact in parallel apposition to produce striated ‘spindle-shaped bodies’ which elongate by the longitudinal attachment of more procollagen filaments and form intracellular nascent collagen fibrils.