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PubMed1989

[The value of ultrasound in the diagnosis of capsule ligament injuries of the upper ankle joint].

Ankle ligament injuries are usually diagnosed by clinical and radiological examination. In this study we tried to determine the accuracy of dynamic sonography in the diagnosis of ankle ligament injuries. From 1 April 1987 to 1 July 1988, 72 patients with ligamentous injuries of the ankle were examined sonographically. The dynamic stability of the anterior talofibular ligament was determined by measuring the length of the ligaments under normal and stressed conditions. The anatomical course of the ligaments was used as the plane of section. Clinical and radiological examinations were used to determine whether an operation was indicated, and the results of these examinations were compared after the operation with the sonographic and intraoperative findings. Dynamic examination of the stability of the anterior talofibular ligament yielded findings compatible with the intraoperative findings in 64 of the 72 cases (88.8%). The mean difference in length between normal and stressed conditions was 7.4 mm, with a range of 6-12 mm in the case of rupture of the ligament. A high level of agreement between sonographic and intraoperative findings was also found for the calcaneofibular ligament. In 62 of the 72 cases (86.1%) a correct diagnosis was possible. The mean difference in length in this plane of section was 10.6 mm, with a range of 7-17 mm. The sensitivity and specificity of ultrasound in the diagnosis of rupture of the ligaments were between 80% and 90%, respectively, and the positive predictive value was about 95%. Sonography with a high-resolution scanner allows a correct diagnosis of ligamentous lesions at the ankle joint in 80-90% of cases.(ABSTRACT TRUNCATED AT 250 WORDS)

Adult↗
PubMed1985

Tubulin, hybrid dimers, and tubulin S. Stepwise charge reduction and polymerization.

Limited proteolysis of rat brain tubulin (alpha beta) by subtilisin cleaves a 1-2-kDa fragment from the carboxyl-terminal ends of both the alpha and beta subunits with a corresponding loss in negative charge of the proteins. The beta subunit is split much more rapidly (and exclusively at 5 degrees C), yielding a protein with cleaved beta and intact alpha subunit, called alpha beta s, which is of intermediate charge. Further proteolysis cleaves the carboxyl terminus of the alpha subunit leading, irreversibly, to the doubly cleaved product, named tubulin S, with a composition alpha s beta s. Both cleavage products are polymerization-competent and their polymers are resistant to 1 mM Ca2+- and 0.24 M NaCl-induced depolymerization. The two polymers differ in that the alpha beta s polymer is stable to cold, GDP, and podophyllotoxin, whereas tubulin S polymer is disassembled by these agents; moreover, alpha beta s forms ring-shaped polymers, whereas alpha s beta s forms filaments associated into bundles and sheets. Tubulin S co-polymerizes with native tubulin yielding a mixed product of intermediate stability. The presence of low mole fractions of tubulin S leads to a marked reduction in the critical concentration for polymerization of the mixture.

Animals↗
PubMed1993

Intracellular localization of the Apn1 DNA repair enzyme of Saccharomyces cerevisiae. Nuclear transport signals and biological role.

The Apn1 DNA repair enzyme of Saccharomyces cerevisiae acts on abasic sites and oxygen radical damages. Apn1 is homologous to the repair endonuclease IV of Escherichia coli, but the yeast protein is approximately 80 residues longer at the C terminus. The Apn1 C terminus is rich in basic amino acids and includes two lysine/arginine clusters related to the nuclear transport signals of some other proteins. We show here by indirect immunofluorescence that Apn1 is localized to the yeast nucleus. Mutant Apn1 proteins were engineered with progressive deletions inward from the C terminus. Elimination of just the last 12 residues from Apn1 (to yield Apn355) did not alter the stability in yeast cells or the in vitro activity of the enzyme. Greater truncation of Apn1 produced proteins of apparently lower (Apn334) or much lower (Apn315 and Apn293) in vivo stability. Both Apn355 and Apn334 failed to concentrate in the yeast nucleus and remained in the cytoplasm. These delocalized derivatives also failed to restore wild-type resistance to oxidative or alkylating agents in a delta apn1 strain. Apn355 and Apn334 complemented repair-deficient E. coli as effectively as did wild-type Apn1. Resistance to these DNA-damaging agents in yeast was restored if Apn355 and Apn334 (but not Apn315 or Apn293) were overproduced approximately 20-fold, which suggests either weak active transport or passive diffusion of these derivatives into the nucleus. Replacement of the C-terminal 12 residues of Apn1 with the nuclear targeting sequence of SV40 T-antigen did not restore effective function or nuclear localization in yeast.

Amino Acid Sequence↗
PubMedDate not supplied

Management of valgus hindfoot deformity in pediatric cerebral palsy patients by medial displacement osteotomy.

To determine the clinical indications and efficacy of medial displacement osteotomy of the calcaneus in management of hindfoot valgus, we evaluated 18 feet (ten patients) prospectively. Average follow-up was 42 months; minimum follow-up was 24 months. The osteotomy was performed parallel to the subtalar joint through a lateral incision; the distal fragment was displaced > or = 50% and transfixed with two parallel pins for approximately 4 weeks. Analysis of hindfoot stability, foot position, and extremity function yielded excellent (n = 17) or fair (n = 1) results. Varus overcorrection in the "fair" foot required a closing wedge osteotomy.

Adolescent↗
PubMed1997

Calibration of Abbott AxSYM Ferritin kit using the WHO Human Liver Ferritin International Standard 80/602.

A commercial ferritin kit (Abbott AxSYM Ferritin) was calibrated using the WHO Human Liver Ferritin International Standard 80/602. The reconstituted WHO freeze-dried standard was diluted to obtain six concentration levels ranging from 10-840 micrograms/l. In the analysis of the data, logarithmic transformation of the results was performed in order to stabilize the variance. The AxSYM kit yielded slightly higher values than the WHO Ferritin Standard (p < 0.05). The relation between the AxSYM kit and the WHO Ferritin Standard (untransformed values) was described by a proportionality: FerritinAxSYM = 1.057 x FerritinWHO. WHO Ferritin Standard values of 12 and 15 micrograms/l (used as cut-off values for absent or small body iron reserves) yielded calculated AxSYM values of 12.7 and 15.9 micrograms/l. A WHO Ferritin Standard value of 30 micrograms/l (used threshold value for the presence of stainable bone marrow haemosiderin iron) yielded a calculated AxSYM value of 31.7 micrograms/l.

Calibration↗
PubMed1997

Stereocontrol in Intermolecular Dirhodium(II)-Catalyzed Carbonyl Ylide Formation and Reactions. Dioxolanes and Dihydrofurans.

Ethyl diazoacetate undergoes dirhodium(II)-catalyzed reactions with aryl aldehydes to form 1,3-dioxolanes as mixtures of diastereoisomers in good yields. Carbonyl ylides are reaction intermediates. Catalyst dependent diastereocontrol is observed for reactions with p-nitrobenzaldehyde, but not for those with p-anisaldehyde or benzaldehyde, so that at least with transformations involving p-nitrobenzaldehyde a metal-stabilized ylide is responsible for product formation. Higher yields are obtained with catalysis by dirhodium(II) carboxamidates than with the carboxylates. Diastereoselectivity in 1,3-dioxolane formation that occurs through the "free" ylide can be effectively controlled so that only one diastereomer is produced through the use of 2,6-di-tert-butyl-4-methylphenyl diazoacetate (BDA) or dicyclohexylmethyl diazoacetate (DCM). The thermodynamically least stable all-cis trisubstituted 1,3-dioxolane is the primary product from p-nitrobenzaldehyde "cycloaddition" to the metal-stabilized ylide. Reactions that take place in the presence of p-anisaldehyde and dimethyl acetylenedicarboxylate (DMAD) result in the formation of one 2,5-dihydrofuran-2-carboxylate stereoisomer in good yield. In contrast, with p-nitrobenzaldehyde and DMAD both dihydrofuran stereoisomers are produced along with, mainly, the dioxolane derived from the metal-stabilized ylide; there is in this case competition between addition reactions of the "free" ylide and the metal-associated ylide.

Journal Article↗
PubMed2003

Thermal and urea-induced unfolding of the marginally stable lac repressor DNA-binding domain: a model system for analysis of solute effects on protein processes.

Thermodynamic and structural evidence indicates that the DNA binding domains of lac repressor (lacI) exhibit significant conformational adaptability in operator binding, and that the marginally stable helix-turn-helix (HTH) recognition element is greatly stabilized by operator binding. Here we use circular dichroism at 222 nm to quantify the thermodynamics of the urea- and thermally induced unfolding of the marginally stable lacI HTH. Van't Hoff analysis of the two-state unfolding data, highly accurate because of the large transition breadth and experimental access to the temperature of maximum stability (T(S); 6-10 degrees C), yields standard-state thermodynamic functions (deltaG(o)(obs), deltaH(o)(obs), deltaS(o)(obs), deltaC(o)(P,obs)) over the temperature range 4-40 degrees C and urea concentration range 0 </= C(3) </= 6 M. For unfolding the HTH, deltaG(o)(obs) decreases linearly with increasing C(3) at all temperatures examined, which directly confirms the validity of the linear extrapolation method (LEM) to obtain the intrinsic stability of this protein. At 25 degrees C (pH 7.3 and 50 mM K(+)), both linear extrapolation and extrapolation via the local-bulk domain model (LBDM) to C(3) = 0 yield deltaG(o)(obs) = 1.23 +/- 0.05 kcal mol(-)(1), in agreement with direct measurement (1.24 +/- 0.30 kcal mol(-)(1)). Like deltaG(o)(obs), both deltaH(o)(obs) and deltaS(o)(obs) decrease linearly with increasing C(3); the derivatives with respect to C(3) of deltaG(o)(obs), deltaH(o)(obs) and TdeltaS(o)(obs) (in cal mol(-)(1) M(-)(1)) are -449 +/- 11, -661 +/- 90, and -203 +/- 91 at 25 degrees C, indicating that the effect of urea on deltaG(o)(obs) is primarily enthalpic. The deltaC(o)(P,obs) of unfolding (0.63 +/- 0.05 kcal mol(-)(1) K(-)(1)) is not detectibly dependent on C(3) or temperature. The urea m-value of the lacI HTH (-d deltaG(o)(obs),/dC(3) = 449 +/- 11 cal mol(-)(1) M(-)(1) at 25 degrees C) is independent of C(3) up to at least 6 M. Use of the LBDM to fit the C(3)-dependence of deltaG(o)(obs) yields the local-bulk partition coefficient for accumulation of urea at the protein surface exposed upon denaturation: K(P) = 1.103 +/- 0.002 at 25 degrees C. This partition coefficient is the same within uncertainty as those previously determined by LBDM analysis of osmometric data for solutions of urea and native (folded) bovine serum albumin, as well as LBDM analysis of the proportionality of m-values to changes in water accessible surface area upon protein unfolding. From the correspondence between values of K(P), we conclude that the average local urea concentration at both folded and unfolded protein surface exceeds the bulk by approximately 10% at 25 degrees C. The observed decrease in m-value for the lacI HTH with increasing temperature, together with the observed reductions in both deltaH(o)(obs) and deltaS(o)(obs) of unfolding with increasing urea concentration, demonstrate that K(P) for urea decreases with increasing temperature and that transfer of urea from the bulk solution to the local domain at the protein surface exposed on denaturation is enthalpically driven and entropically unfavorable.

Bacterial Proteins↗
PubMed1986

Enzymatic semisynthesis of [LeuB30] insulin.

Experimental conditions for the preparation of [LeuB30] insulin by coupling of des-AlaB30 insulin with Leu-OBu(t) were determined using Achromobacter protease I and trypsin as catalysts. Successful coupling required a large excess of the amine component (0.8 M), a high concentration of organic cosolvent (35-50%) and neutral pH of the reaction mixture. The coupling yield of Achromobacter protease I after 24 h at 37 degrees C was almost the same or a little higher than that at 25 degrees C. With trypsin, the coupling yield at 37 degrees C after 24 h was considerably lower than at 25 degrees C. This was partly ascribed to the difference in concentration of organic cosolvent at 37 degrees C and 25 degrees C; 35% and 50%, respectively, or possibly of enzyme stability at these temperatures. The maximum product yield was about 90% with both enzymes under optimal conditions. A preparative scale experiment was performed with Achromobacter protease I; the yield of [LeuB30] insulin was 51% using porcine insulin as the starting material. This semisynthetic insulin was identified by HPLC and amino acid analysis. No difference was observed in CD spectra between [LeuB30] insulin and human insulin.

Alcaligenes↗
PubMed1996

Reactions of Charged Substrates. 6. The Methoxymethyl Carbenium Ion Problem. 1. A Semiempirical Study of the Kinetic and Thermodynamic Stabilities of Linear and Cyclic Oxo- and Thiocarbenium Ions Generated from Pyridinium and Dimethylanilinium Ions.

AM1-calculated energy profiles for dissociation of (methoxymethyl)pyridinium and dimethylanilinium ion substrates show that the methoxymethyl carbenium ion is not sufficiently stable to exist as an intermediate on the reaction coordinate for this model reaction. [(Thiomethoxy)methyl]pyridinium ion, however, has a distinct transition state because of the stability of the resulting ion-neutral complex. The complete potential energy surfaces for water displacement on the methoxymethyl substrate with either pyridine or dimethylaniline as the leaving group show distinct transition states and very flat surfaces for the ion-neutral complexes in which interaction of the carbenium ion with both leaving group and nucleophile is stabilizing. Secondary systems studied, including linear methoxy and thiomethoxy substrates, 5- and 6-membered cyclic oxo and thio substrates, and ribosyl-, xylopyranosyl-, and glucopyranosylpyridinium ions yield ion-neutral complexes with sufficient intrinsic stability to exist as intermediates. Comparison with solution data, primarily activation entropy and Brønsted coefficients, suggests that the sugar oxocarbenium ions, either as distinct, solvent-equilibrated intermediates or elements of ion-neutral complexes, are formed by unimolecular dissociation of the respective substrates in solution.

Journal Article↗
PubMed1999

Stability and folding of dihydrofolate reductase from the hyperthermophilic bacterium Thermotoga maritima.

Dihydrofolate reductase (DHFR) has been a well-established model system for protein folding. The enzyme DHFR from the hyperthermophilic bacterium Thermotoga maritima (TmDHFR) displays distinct adaptations toward high temperatures at the level of both structure and stability. The enzyme represents an extremely stable dimer; no isolated structured monomers could be detected in equilibrium or during unfolding. The equilibrium unfolding strictly follows the two-state model for a dimer (N(2) right harpoon over left harpoon 2U), with a free energy of stabilization of DeltaG = -142 +/- 10 kJ/mol at 15 degrees C. The two-state model is applicable over the whole temperature range (5-70 degrees C), yielding a DeltaG vs T profile with maximum stability at around 35 degrees C. There is no flattening of the stability profile. Instead, the enhanced thermostability is characterized by shifts toward higher overall stability and higher temperature of maximum stability. TmDHFR unfolds in a highly cooperative manner via a nativelike transition state without intermediates. The unfolding reaction is much slower (ca. 10(8) times) compared to DHFR from Escherichia coli (EcDHFR). In contrast to EcDHFR, no evidence for heterogeneity of the native state is detectable. Refolding proceeds via at least two intermediates and a burst-phase of rather low amplitude. Reassociation of monomeric intermediates is not rate-limiting on the folding pathway due to the high association constant of the dimer.

Bacterial Proteins↗
PubMed1998

Helix-stabilizing nonpolar interactions between tyrosine and leucine in aqueous and TFE solutions: 2D-1H NMR and CD studies in alanine-lysine peptides.

Interactions between side chains spaced (i,i + 3) and (i,i + 4) may explain the context dependence of helix propensities observed in different systems. Nonpolar residues with these spacings occur frequently in protein helices and stabilize isolated peptide helices. Here (i,i + 3) and (i,i + 4) nonpolar interactions between Tyr and Leu in different solution conditions are studied in detail in alanine-based peptides using 2D 1H NMR and CD spectroscopy. Helix contents analyzed using current models for helix-coil transitions yield interaction energies which demonstrate significant helix stabilization in aqueous 1 M NaCl solutions by Tyr-Leu or Leu-Tyr pairs when spaced (i,i + 4) and, to a smaller extent, when spaced (i,i + 3), comparable to those estimated for other residue pairs. The interactions persist in solutions containing TFE, a helix-stabilizing solvent believed to diminish hydrophobic interactions, but not in helix-destabilizing 6 M urea. 1H NMR resonances for all peptides and solution conditions except in 6 M urea were completely assigned. NMR data indicate that the N-terminal residues are more helical and that the N-acetyl group participates in helix formation. The two (i,i + 4) spaced pairs show the same pattern of NOE cross-peaks between the Tyr and Leu side chains, as do the two (i,i + 3) pairs in 1 M NaCl as well in TFE solutions, and correspond well with that expected for the specific Tyr-Leu pair with side-chain contacts in protein helices.

Alanine↗
PubMed2000

Palladium-catalyzed cyclocarbonylation of o-iodoanilines with heterocumulenes: regioselective preparation of 4(3H)-quinazolinone derivatives

A catalyst system comprising palladium acetate-bidentate phosphine is effective for the cyclocarbonylation of o-iodoanilines with heterocumulenes at 70-100 degrees C for 12-24 h to give the corresponding 4(3H)-quinazolinone derivatives in good yields. Utilizing o-iodoaniline with isocyanates, carbodiimides, and ketenimines for the reaction, 2,4-(1H,3H)-quinazolinediones, 2-amino-4(3H)-quinazolinones and 2-alkyl-4(3H)-quinazolinones were obtained, respectively. The nature of the substrates including the electrophilicity of the carbon center of the carbodiimide, and the stability of the ketenimine, influence the product yields of this reaction. Urea-type intermediates are believed to be generated first in situ from the reaction of o-iodoanilines with heterocumulenes, followed by palladium-catalyzed carbonylation and cyclization to yield the products.

Journal Article↗
PubMed2006

A comparative study of different vector designs for the mammalian expression of recombinant IgG antibodies.

Monoclonal antibodies (Mab) are the fastest growing group of biopharmaceuticals in development. For production in mammalian cells, the four polypeptide chains of the immunoglobulin diheterotetramer must be assembled prior to exit from the endoplasmic reticulum. Various recombinant Mab expression vectors have been developed utilizing mono-and bicistronic expression cassettes encoded on one or two plasmids. However, there are only few studies providing information on the type of vector design optimal for stable or transient production of recombinant IgG. Consequently, in this study, we have constructed a series of mammalian expression vectors for the production of recombinant human or chimeric IgG antibodies with different expression cassette designs. Versions for monocistronic and bicistronic expression with different promoters and cistron arrangements were generated. Antibody production levels were evaluated in transiently transfected 293T and CHO-K1 cells. Furthermore, stable CHO cell lines were generated and analyzed for antibody production levels and stability. Our results indicate that compared to monocistronic expression, EMCV IRES-mediated bicistronic expression constructs yield similar antibody expression levels and show long-term stability in CHO cell lines. Addition of a third cistron encoding YFP was shown to facilitate screening and isolation of clones using a FACS sorter.

5' Untranslated Regions↗
PubMed2000

Clustered cysteine residues in the kinase domain of v-Src: critical role for protein stability, cell transformation and sensitivity to herbimycin A.

We have previously reported the activation of Src by mercuric chloride based on the sulfhydryl modification. To evaluate the significance of cysteine residues in v-Src, we replaced each cysteine to alanine by oligonucleotide-directed mutagenesis and examined its effect on cell transformation. Of ten cysteine residues scattered over v-Src, four cysteines clustered in kinase domain, Cys483, Cys487, Cys496 and Cys498, were important for protein stability and cell transformation, whereas those in SH2 domain were dispensable. A single mutation in Cys498 yielded suppression of kinase activity and a temperature-sensitivity in anchorage independent growth. Double mutation either in Cys483/Cys487 or in Cys496/Cys498 yielded clear temperature-sensitivity in cell transformation and in stability of Src protein. Instability of Src protein was magnified by quadruple mutation in the cysteines, which decreased the half-life of Src to be less than one quarter of that of wild-type. In addition, both Cys483/Cyr487 and Cys496/Cys498 kinases became resistant to in vitro inactivation by herbimycin A, which directly inactivates v-Src in addition to its effect on HSP90. Taken together, our results strongly suggest that the cysteine clustered motif of v-Src are critical for protein stability, cell transformation and in vitro inactivation by herbimycin A.

Amino Acid Sequence↗
PubMed1984

Large-scale isolation of the Neurospora plasma membrane H+-ATPase.

A method for the purification of relatively large quantities of the Neurospora crassa plasma membrane proton translocating ATPase is described. Cells of the cell wall-less sl strain of Neurospora grown under O2 to increase cell yields are treated with concanavalin A to stabilize the plasma membrane and homogenized in deoxycholate, and the resulting lysate is centrifuged at 13,500g. The pellet obtained consists almost solely of concanavalin A-stabilized plasma membrane sheets greatly enriched in the H+-ATPase. After removal of the bulk of the concanavalin A by treatment of the sheets with alpha-methylmannoside, the membranes are treated with lysolecithin, which preferentially extracts the H+-ATPase. Purification of the lysolecithin-solubilized ATPase by glycerol density gradient sedimentation yields approximately 50 mg of enzyme that is 91% free of other proteins as judged by quantitative densitometry of Coomassie blue-stained gels. The specific activity of the enzyme at this stage is about 33 mumol of P1 released/min/mg of protein at 30 degrees C. A second glycerol density gradient sedimentation step yields ATPase that is about 97% pure with a specific activity of about 35. For chemical studies or other investigations that do not require catalytically active ATPase, virtually pure enzyme can be prepared by exclusion chromatography of the sodium dodecyl sulfate-disaggregated, gradient-purified ATPase on Sephacryl S-300.

Cell Membrane↗
PubMed1998

Twist knot cerclage wire: the appropriate wire tension for knot construction and fracture stability.

OBJECTIVE: The aim was to find the best wire tension in order to permit a reliable first twist and simultaneously provide the best stability of fracture fixation from the twist knot cerclage wire. DESIGN: Wires at different distal tensions, looped around the fracture, were measured during twist and compared with the yield strength of the wire. Then, the fracture stability of the twist knot cerclage wire was determined from the pull-out strength. METHODS: In order to measure wire tension during twist knot construction, an instrument was designed using the tension load cell of a universal testing machine, a 15 degrees oblique osteotomy femoral shaft and 1.25 mm diameter wire. A wire tensioner and a pair of extraction grips were then used for measuring the pull-out strength of the cerclage wire fixation. RESULT: Three wire tensions (160, 200 and 240 N) were used as looped wire for the first twist knot construction. The 200 N tension cerclage wire provided the best fracture stability. CONCLUSION: It was found that 200 N was the best wire tension for the construction of a twist knot cerclage wire. RELEVANCE: When a cerclage wire is twisted at a femoral shaft using 1.25 mm diameter wire, a wire tension of 200 N should be used to achieve a reliable first twist and the best stability of fracture fixation.

Journal Article↗
PubMed1995

Effects of two mutations detected in medium chain acyl-CoA dehydrogenase (MCAD)-deficient patients on folding, oligomer assembly, and stability of MCAD enzyme.

We have used expression of human medium chain acyl-CoA dehydrogenase (MCAD) in Escherichia coli as a model system for dissecting the molecular effects of two mutations detected in patients with MCAD deficiency. We demonstrate that the R28C mutation predominantly affects polypeptide folding. The amounts of active R28C mutant enzyme produced could be modulated between undetectable to 100% of the wild-type control by manipulating the level of available chaperonins and the growth temperature. For the prevalent K304E mutation, however, the amounts of active mutant enzyme could be modulated only in a range from undetectable to approximately 50% of the wild-type, and the assembled mutant enzyme displayed a decreased thermal stability. Two artificially constructed mutants (K304Q and K304E/D346K) yielded clearly higher amounts of active MCAD enzyme than the K304E mutant but were also responsive to chaperonin co-overexpression and growth at low temperature. The thermal stability profile of the K304E/D346K double mutant was shifted to even lower temperatures than that of the K304E mutant, whereas that of the K304Q mutant was closely similar to the wild-type. Taken together, the results show that the K304E mutation affects (i) polypeptide folding due to elimination of the positively charged lysine and (ii) oligomer assembly and stability due to replacement of lysine 304 with the negatively charged glutamic acid.

Acyl-CoA Dehydrogenase↗
PubMed1991

[Current aspects in the arthroscopic treatment of shoulder instability].

With regard to postoperative stability of the shoulder joint, the results yielded by the various arthroscopic refixation techniques are not as good as those obtained after open operation. The aim of this paper is to analyze the reasons for this and to present a new procedure which it is hoped will improve the arthroscopic results. The main reason for the high postoperative recurrence rate after arthroscopic joint stabilization seems to be that refixation of the capsule is not performed at the level of the lesion, but above it, because of the position of the subscapularis tendon. Another reason for the poor results of arthroscopy is that the enlarged capsule cannot be shortened as desired, because the glenoid labrum is used for refixation of the capsule. To improve the arthroscopic results we suggest basic changes of the procedure in cases with severe damage to the soft tissue at the antero-inferior aspect of the glenoid and/or in cases with an enlarged capsule: refixation of the capsule should not be carried out from inside the joint but from outside the capsule. To this end, we applied the so-called extraarticular screwing technique. Refixation is achieved by inserting small cannulated titanium screws by means of a special screwdriver. No metal is placed inside the joint. This technique requires a new portal, namely the so-called antero-inferior portal, which is placed 1.5 cm inferior to the coracoid process. If the precautionary measures described are duly observed, the musculocutaneous nerve cannot be damaged. The technique allows stable refixation of the capsule in the desired length by placement of one or two small screws in the center of the Bankart lesion. Our preference is based on experience with 83 patients with recurrent shoulder instability who were operated on by arthroscopic techniques.(ABSTRACT TRUNCATED AT 250 WORDS)

Adolescent↗