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  • Macromolecular organization and fine structure of the human basilar membrane - RELEVANCE for cochlear implantation.

Macromolecular organization and fine structure of the human basilar membrane - RELEVANCE for cochlear implantation.

Cell and tissue research (2015-02-11)
Wei Liu, Francesca Atturo, Robair Aldaya, Peter Santi, Sebahattin Cureoglu, Sabrina Obwegeser, Rudolf Glueckert, Kristian Pfaller, Annelies Schrott-Fischer, Helge Rask-Andersen
ABSTRACT

Cochlear micromechanics and frequency tuning depend on the macromolecular organization of the basilar membrane (BM), which is still unclear in man. Novel techniques in cochlear implantation (CI) motivate further analyses of the BM. Normal cochleae from patients undergoing removal of life-threatening petro-clival meningioma and an autopsy specimen from a normal human were used. Laser-confocal microscopy, high resolution scanning (SEM) and transmission electron microscopy (TEM) were carried out in combination. In addition, one human temporal bone was decellularized and investigated by SEM. The human BM consisted in four separate layers: (1) epithelial basement membrane positive for laminin-β2 and collagen IV, (2) BM "proper" composed of radial fibers expressing collagen II and XI, (3) layer of collagen IV and (4) tympanic covering layer (TCL) expressing collagen IV, fibronectin and integrin. BM thickness varied both radially and longitudinally (mean 0.55-1.16 μm). BM was thinnest near the OHC region and laterally. There are several important similarities and differences between the morphology of the BM in humans and animals. Unlike in animals, it does not contain a distinct pars tecta (arcuate) and pectinata. Its width increases and thickness decreases as it travels apically in the cochlea. Findings show that the human BM is thinnest and probably most vibration-sensitive at the outer pillar feet/Deiter cells at the OHCs. The inner pillar and IHCs seem situated on a fairly rigid part of the BM. The gradient design of the BM suggests that its vulnerability increases apical wards when performing hearing preservation CI surgery.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
Anti-Fibronectin Frag Antibody, cell attachment fragment, clone 3E3, clone 3E3, Chemicon®, from mouse
Sigma-Aldrich
Anti-Collagen Type IV Antibody, Chemicon®, from goat
Sigma-Aldrich
Anti-Elastin Antibody, clone 10B8, clone 10B8, Chemicon®, from mouse
Sigma-Aldrich
Anti-Tubulin Antibody, beta III isoform, CT, clone TU-20 (Similar to TUJ1), ascites fluid, clone TU-20 (Similar to TUJ1), Chemicon®
Sigma-Aldrich
Anti-Collagen Type II (Ab-1) Mouse mAb (II-4C11), liquid, clone II-4C11, Calbiochem®
Sigma-Aldrich
Anti-Laminin B2 Antibody, clone A5, clone A5, Upstate®, from rat