Anatomical study and reanalysis of the nomenclature of the anterolateral complex of the knee focusing on the distal iliotibial band: identification and description of the condylar strap

Background: The capsulo-osseous layer, short lateral ligament, mid-third lateral capsular ligament, lateral capsular ligament and anterolateral ligament are terms that have been used interchangeably to describe what is probably the same structure. This has resulted in confusion regarding the anatomy and function of the anterolateral complex of the knee and its relation to the distal iliotibial band. Purpose: To characterize the macroscopic anatomy of the anterolateral complex of the knee, in particular the femoral condylar attachment of the distal iliotibial band (ITB). We identified a specific and consistent anatomical structure that was not accurately described previously, connects the deep surface of the ITB to the condylar area, and is distinct from the anterolateral ligament, the capsulo-osseous layer and the Kaplan fibers. Study Design: Descriptive laboratory study. Methods: Sixteen fresh-frozen human cadaveric knees were used to study the anterolateral complex of the knee. Standardized dissections were performed that included a qualitative and quantitative assessment of the anatomy through both anterior (n=5) and posterior (n=11) approaches. Results: The femoral condylar attachment of the distal ITB was not reliably identified by anterior dissection but was in all posterior dissections. A distinct anatomical structure, hereafter termed condylar strap (CS), was identified between the femur and the lateral gastrocnemius on one side and the deep surface of the ITB on the other, in all posteriorly dissected specimens. The structure had a mean thickness of 0.88 mm, and its femoral insertion was located between the distal Kaplan fibers and the epicondyle. The proximal femoral attachment of the structure had a mean width of 15.82 mm and the width of the distal insertion of the structure on the ITB was 13.27 mm. The mean length of the structure was 26.33 mm on its distal border and 21.88 mm on its proximal border. Qualitative evaluation of behavior in internal rotation revealed that this anatomical structure became tensioned and created a tenodesis effect on the ITB. Conclusions: There is a consistent structure that attaches to the deep ITB and the femoral epicondylar area. The orientation of fibers suggest that it may have a role in anterolateral knee stability. Clinical Relevance: This new anatomical description may help surgeons to optimize technical aspects of lateral extra-articular procedures in cases of anterolateral knee laxity

Subcarrier index-power modulated optical OFDM with dual superposition multiplexing for IMDD PON systems

International audienc

Composición de gluteninas de alto peso molecular de variedades de trigo blando registradas en España y su relación con la calidad panadera

[EN] Variation in high-molecular weight (HMW) glutenin subunit composition amongst 110 Spanish registered bread wheat varieties was investigated using polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulphate (SDS-PAGE) and the allelic composition of the varieties at each of the three loci controlling those subunits was determined. Three alleles were identified at the Glu-Al locus, seven at the Glu-B1 locus and five at the Glu-D1. Only one variety, Marca, was found to consist of two biotypes with respect to HMW glutenin subunit composition. Forty three different patterns for the HMW glutenins were found amongst the analyzed varieties. On the basis of previous work, which related individual subunits to bread-making quality, Glu-1 quality scores were calculated for the Spanish registered varieties.[ES] Se investigó la composición en gluteninas de alto peso molecular (HMW) en 110 variedades de trigo blando registradas en España utilizando electrofóresis en gel de poliacrilamida en presencia de dodecil sulfato sódico (SDS-PAGE) y se determinó la composición alélica de las variedades en cada uno de los tres loci que controlan dichas subunidades. Se identificaron tres alelos en el locus Glu-A1, siete en el locus Glu-B1 y cinco en el Glu-D1. Solamente en una variedad, Marca, se encontró variación, dos biotipos, con respecto a la composición en subunidades de gluteninas HMW. En las variedades analizadas se encontraron 43 diferentes modelos en la combinación de gluteninas HMW. Basándose en trabajos previos, que relacionaban subunidades individuales a calidad panadera, se calcularon las puntuaciones de calidad en los loci Glu-1 para las variedades españolas registradas.Peer reviewe

Dual-polarization multi-band optical OFDM transmission and receiver limitations for up to 500 Gb/s uncompensated long-haul links

International audienc

Human intestine luminal ACE2 and amino acid transporter expression increased by ACE-inhibitors

Sodium-dependent neutral amino acid transporter B(0)AT1 (SLC6A19) and imino acid (proline) transporter SIT1 (SLC6A20) are expressed at the luminal membrane of small intestine enterocytes and proximal tubule kidney cells where they exert key functions for amino acid (re)absorption as documented by their role in Hartnup disorder and iminoglycinuria, respectively. Expression of B(0)AT1 was shown in rodent intestine to depend on the presence of the carboxypeptidase angiotensin-converting enzyme 2 (ACE2). This enzyme belongs to the renin-angiotensin system and its expression is induced by treatment with ACE-inhibitors (ACEIs) or angiotensin II AT1 receptor blockers (ARBs) in many rodent tissues. We show here in the Xenopus laevis oocyte expression system that human ACE2 also functionally interacts with SIT1. To investigate in human intestine the potential effect of ACEIs or ARBs on ACE2, we analysed intestinal biopsies taken during routine gastroduodenoscopy and ileocolonoscopy from 46 patients of which 9 were under ACEI and 13 ARB treatment. Analysis of transcript expression by real-time PCR and of proteins by immunofluorescence showed a co-localization of SIT1 and B(0)AT1 with ACE2 in the brush-border membrane of human small intestine enterocytes and a distinct axial expression pattern of the tested gene products along the intestine. Patients treated with ACEIs displayed in comparison with untreated controls increased intestinal mRNA levels of ACE2, peptide transporter PEPT1 (SLC15A1) and AA transporters B(0)AT1 and PAT1 (SLC36A1). This study unravels in human intestine the localization and distribution of intestinal transporters involved in amino acid absorption and suggests that ACEIs impact on their expression