Treatment of Chronic Lower Extremity Ulcers with A New Er:Yag Laser Technology.

Chronic lower extremity ulcers (CLEUs) have a high prevalence and are difficult to treat due to their various aetiologies. The aim of this study is to evaluate the results achieved in treating CLEUs using an Erbium: YAG (Er:YAG) laser with RecoSMA technology. This laser emits thousands of microbeams of energy causing superficial epidermal ablation and a separation of dermal fibres due to a mechanical-acoustic and resonance effect. The evaluation of the results achieved was carried out by questionnaires completed by 18 patients enrolled in the study. Histological studies and photographs taken before each session (16 sessions in total) were analysed to visually monitor the clinical progress. The analyses were carried out with the help of computer software. The results after 16 treatment sessions showed the complete healing of ulcers or a decrease in their initial area of at least 55% in over 65% of the patients treated. The Student's t-test and Fisher's exact test were used for statistical analysis. The Er:YAG laser and RecoSMA technology ablates few epidermal cell layers, producing a mechanical-acoustic effect with resonance action leading to tissue regeneration mechanisms. This technology offers an effective and safe alternative for treating CLEUs.

A novel method of facial rejuvenation using a 2940-nm erbium:YAG laser with spatially modulated ablation: a pilot study.

The objective of this study was to determine the efficacy and safety of a novel method of facial rejuvenation using a 2940-nm erbium:YAG laser with Spatially Modulated Ablation™. A pilot study was performed in 16 women with moderate to severe signs of facial aging relative to chronological age, who underwent two treatment sessions with an Er:YAG laser coupled to the RecoSMA™ technology (Linline, Minsk, Belarus). The whole face was treated in all patients. Clinical efficacy, tolerance, adverse effects, complications, and histological changes due to the treatment were evaluated. Clinical photographs and biopsies were taken before treatment and 3 months after the second treatment session. All patients completed the study and presented no significant complications. Histological changes in the epidermis and dermis as a result of treatment were found. Fine lines, wrinkles, and overall facial aging improved significantly (p < 0.0001). The mean reduction of fine lines and wrinkles was 59 % (r = 40-75 %). The mean improvement of overall facial aging was 74 % (r = 55-90 %). After showing the patients the comparative photographs before and after treatment, 75 % of women stated that they were satisfied or very satisfied and would recommend the treatment. Preliminary results show an excellent safety/efficacy profile for this novel technology, which, based on observed results, can be considered to have advantages over other methods of facial rejuvenation with lasers.

Perspectivas en el uso de materiales de relleno inyectables para tejidos blandos, desde nuestra experiencia. 2ª Parte / Perspectives on the use of soft tissue fillers from our experience. Part II

El médico que emplea un determinado material de relleno dérmico debe dominar la técnica de inyección, conocer las características del producto a fondo y los posibles efectos adversos derivados de su actuación. Las indicaciones que realizamos desde nuestra experiencia no agotan las posibilidades de lograr una mejoría estética evidente solo con el empleo de materiales inyectables; por el contrario, la buena formación y el conocimiento de técnicas afines pueden ser claves para el rejuvenecimiento de las zonas que lo precisan, redundando siempre en beneficio de los pacientes. La mayoría de efectos adversos que pueden producirse son leves y/o transitorios. Destacan el eritema ,edema, equímosis o hematomas; otros pueden ser potencialmente graves o prolongarse en el tiempo hasta que se resuelven. Destacan las reacciones de hipersensibilidad, las infecciones, granulomas o necrosis. Las recomendaciones sobre el tratamiento de las complicaciones deben seguir los principios básicos de la Medicina en relación a su diagnóstico y a las recomendaciones de la literatura experta que exponemos. La creciente demanda de tratamientos con materiales de relleno dérmicos, no debe suponer un incremento de los efectos adversos asociados si se tienen en cuenta y se conocen bien las indicaciones de empleo de cada uno de ellos (AU)

It is mandatory for doctors who use dermal fillers to dominate the injection technique and to know the product characteristics as well as the possible side effects that can derive from the procedure. Indications on fillers given in this paper, based on the authors' experience, do not prevent the use of other aesthetic treatments; moreover, a solid formation and a deep knowledge of the different adjunctive techniques that can be used are the key to achieve an aesthetic rejuvenation of the treated areas and, consequently, attain patients’ satisfaction. Most of the incidents or side effects that can appear with the use of dermal fillers are mild and brief. Erythema, edema, ecchymosis and/or haematomas are the most common ones. However, other effects such as cutaneous reaction to the product, granuloma formation and/or necrosis are more serious complications. Treatment in all of these cases should follow the basic medical knowledge principles in accordance to the complication diagnosed as well as to the recommendations given in related expert medical literature. The increased demand of treatments with fillers should not imply an increase in adverse effects if indications and correct use of the different available materials are taken into account (AU)

Perspectivas en el uso de materiales de relleno inyectables para tejidos blandos, desde nuestra experiencia. 1ª Parte / Perspectives on the use of soft tissue fillers from our experience. Part I

Los materiales de relleno inyectable empleados con finalidad estética o para recuperar el volumen en las atrofiasgrasas cutáneas, suponen uno de los procedimientos esté-ticos más empleados en España. El conocimiento de sus características, su técnica de depósito y correcta localización, así como saber los riesgos potenciales que pueden derivarse de su uso, son capitales para una elección adecuada a fin de obtener resultados correctos con mínimos efectos adversos. La elección de un tipo de material de relleno u otro dependerá de la evaluación del área a inyectar, de la experiencia de cada profesional y del seguimiento de las recomendaciones y técnicas particulares que requiere cada producto. El adecuado aprendizaje, asesoramiento y desarrollo de experiencia, representan la garantía del éxito (AU)

Treatment with fillers for aesthetic purposes or to replace subcutaneous fat loss produced by muscle atrophyis one of the aesthetic procedures more frequently carried out in Spain. Knowledge of the properties of the products, the injection technique, correct location of the area and awareness of the potential side effects and risks involved are important at the time of selecting this therapy, with the aim of obtaining good results with minimum of adverse effects. The selection of one type of filler or another will depend on the evaluation of the area to be filled, the experience of each professional and following the advice and specific techniques that each product requires. An adequate training, assessment and experience will represent a successful outcome (AU)

Proteolytic activity of the different fragments of factor B on the third component of complement (C3). Involvement of the N-terminal domain of Bb in magnesium binding.

Kinetic experiments measuring the proteolytic activity of Bb and 33Kd fragment (the C-terminal domain of factor B) on C3 were performed in several conditions, in order to assess the role of factor B domains in the catalytic activity and magnesium binding. The experiments were carried out in fluid phase with 125I-C3 or C3(H2O) as substrates and in the presence of nonradioactive C3b as cofactor. The results indicate: (a) The C-terminal domain, 33Kd, possesses proteolytic activity on C3, which is Mg2(+)-independent, whereas proteolysis by Bb is enhanced in 5 mM Mg2+. (b) C3b behaves as cofactor of 33Kd proteolytic activity on C3 and factor H is able to inhibit this activity. (d) Kinetics of C3 proteolysis by 33Kd shows a lag phase which is also displayed by Bb in the absence but not in the presence of Mg2+. Taken together these data are consistent with the involvement of the N-terminal domain of Bb in Mg2+ binding, which results in an enhancement of the proteolytic activity on C3 of the adjacent C-terminal domain. A C3 convertase model accounting for these results is presented.

Separation of active and inactive forms of the third component of human complement, C3, by fast protein liquid chromatography (FPLC).

C3(H2O), an inactive form of C3 present to a variable extent in most C3 preparations, has been isolated in 40 min from previously purified C3 using FPLC ion exchange chromatography on a Mono Q column. As many as six peaks were obtained from some C3 preparations, corresponding to different molecular forms of the protein. One of these peaks consisted of a molecular form of C3 with intact alpha and beta chains, a free sulfhydryl group but no hemolytic activity and was identified as C3(H2O). C3(H2O) eluted as a homogeneous peak well resolved from native C3, C3b, high molecular weight aggregates and small degradation fragments. The same C3(H2O) peak was generated from native C3 by repeated freeze-thaw cycles or NH2OH treatment. C3(H2O) alpha chain appeared as a doublet about 2 kDa heavier than native C3 alpha chain in low cross-linked gels. Two forms of C3b could be separated on the Mono S column, both able to form the C3 convertase. The present report describes a very fast method to resolve and isolate to homogeneity C3(H2O) and native C3 from C3 preparations. Both molecular forms of C3 are very suitable for studies of the initial and amplification C3 convertases of the alternative pathway of complement.

C3 binds covalently to the C gamma 3 domain of IgG immune aggregates during complement activation by the alternative pathway.

Ovalbumin-antiovalbumin IgG immune aggregates were incubated with normal human serum in the presence of iodo[1-14C]acetamide, in conditions in which only the alternative pathway of complement was activated. The [14C]C3b-IgG covalent complexes formed were digested with pepsin, and analysed by SDS/polyacrylamide-gel electrophoresis and fluorography. Covalent complexes of [14C]C3-Fd and [14C]C3-pFc' were visualized, demonstrating that, during complement activation by the alternative pathway, C3 is covalently incorporated into the C gamma 3 domain of IgG, as well as into the Fd region. The C gamma 2 domain becomes protected from pepsin action by the bound C3b. All the covalent linkages between C3 and the IgG were sensitive to hydroxylamine. When [14C]C3-pFc' covalent complexes were treated with 1 M-NH2OH and loaded onto a Bio-Gel P-4 column, a radioactive peak of 3 kDa was obtained. The material released from [14C]C3-pFc' and [14C]C3-F(ab')2 complexes after treatment with 1 M-NH2OH was mixed and analysed in the Bio-Gel P-4 column. A similar radioactive peak of 3 kDa was obtained. When this peak, either from [14C]C3-pFc' alone or from the mixture of [14C]C3-F(ab')2 and [14C]C3-pFc', was fractionated by h.p.l.c., virtually the same radioactive peptide profile was obtained, indicating that very similar C3 peptides remained covalently bound to both regions (Fab and C gamma 3) of the antibody molecule. It is suggested that C3 bound to the C gamma 3 domain of IgG may interfere with the Fc-Fc interactions of immune aggregates and thus may be involved in several biological properties displayed by these complement-activating aggregates.

Formation of covalent complexes between the fourth component of human complement and IgG immune aggregates.

The binding properties of activated C4 to immune complexes (ovalbumin-rabbit IgG antiovalbumin) were studied by using 125I-IgG in the immune complexes or performing the C4 binding assays in the presence of 14C-iodoacetamide. High molecular weight complexes formed between C4 and IgG could be detected by the incorporation of 14C-iodoacetamide in the -SH group generated in the nascent C4b during the activation process. The same complexes with an apparent molecular weight of 180,000 daltons were detected when the immune aggregates contained 125I-IgG. Two-dimensional SDS-PAGE analysis of the C4b-IgG covalent complexes indicated: In the absence of control proteins, the complexes are formed by the alpha'-chain of C4b and the H chain of the antibody. The alpha'-H complexes are 36% sensitive to hydroxylamine and 64% resistant. This is consistent with the presence of two populations of C4, which are not equivalent in their covalent binding with immune complexes. Covalent complexes C4-C4b or C4b(like)-C4b(like) are generated during the C4 activation and they are detected as alpha-alpha' or alpha-alpha complexes, respectively. Interaction of C4b with the L chain of the antibody molecule also seems to occur, but to a lesser extent than with the H chain.

The interaction of 1-anilino-8-naphthalene sulphonate with human C1q.

C1q has 12 binding sites for 1-anilino-8-naphthalene sulphonate (ANS), two per peripheral subunit. This number increases to 18 upon weak-acid-induced conformational transition in the globular heads. One ANS binding site is present in each C gamma 2 domain of human IgG. ANS is bound by C1q with a higher affinity (Ka = 2.07 X 10(6) M-1) than by the Fc fragment (Ka = 9.07 X 10(4) M-1) of human IgGl. Hence the inhibitory capacity of C1q binding to IgG immune complexes of ANS probably reflects its preferential binding to the globular heads of C1q. The characteristics of ANS-C1q binding may in part explain the hydrophobic component of the C1q-IgG interaction. It is suggested that an ionic-hydrophobic two-step process is involved in the contact between C1q and IgG.

Breakdown of C3 covalently bound to F(ab')2 immune complexes after complement activation by the alternative pathway.

The activation and subsequent degradation of C3 covalently bound to immune complexes (IC) has been studied by using immune aggregates antiovalbumin-125I-F(ab')2-ovalbumin or 125I-C3 in the presence of serum. Kinetic experiments were performed in order to establish the physiological sequence of C3 degradation as a function of time. The results indicated: The interaction C3-IC, as analyzed in SDS-PAGE, results in bands of high molecular weight corresponding to C3 alpha-65-Fd and C3 alpha-41-Fd covalent complexes. In the first 7 min only C3 alpha-65-Fd complexes were detected. From 7 to 15 min a progressive increase in the C3 alpha-41-Fd complexes occurs. After this time the ratio C3 alpha-65-Fd/C3 alpha-41-Fd was kept constant for at least 45 min. Hence, C3b covalently bound to F(ab')2 IC is degraded in serum much faster than when it is bound to IgG IC. The spatial distribution of the Fab arms in the IC appears to be a critical feature in providing a protective environment for C3b. The orientation of the Fab arms was dependent on the presence of the Fc regions.