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1. Polarization-resolved SHG microscopy of rat-tail tendon with controlled mechanical strain

Author

Ivan Gusachenko, Jean-Marc Allain, Viet Samuel Tran, Y. Goulam Houssen, Marie-Claire Schanne-Klein, Laboratoire d'optique et biosciences (LOB), École polytechnique (X)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Laboratoire de mécanique des solides (LMS), École polytechnique (X)-MINES ParisTech - École nationale supérieure des mines de Paris, and Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Centre National de la Recherche Scientifique (CNRS)

Subjects
[PHYS.PHYS.PHYS-OPTICS]Physics [physics]/Physics [physics]/Optics [physics.optics], Materials science, business.industry, [SDV.IB.IMA]Life Sciences [q-bio]/Bioengineering/Imaging, Shg microscopy, Second-harmonic generation, Polarization (waves), Fibril, Tendon, Collagen fibril, medicine.anatomical_structure, Optics, Rat tail tendon, Microscopy, medicine, business, ComputingMilieux_MISCELLANEOUS, Biomedical engineering
Abstract

We combined polarization-resolved SHG microscopy with mechanical assays in rat-tail-tendon and measured collagen remodeling upon controlled stretching. This approach aimed to analyze the relationship between macroscopic response and sub-micrometer scale organization of collagen fibrils. We observed a straightening of the crimps followed by a sliding of the fibrils with increasing stretching of the tendon fascicles. Polarization resolution of the SHG images provided complementary information about the orientation dispersion of collagen fibrils within the focal volume and enabled monitoring of collagen remodeling at the sub-micrometer scale. Our approach can be readily generalized to other tissues and should bring new valuable information about biomechanics of microstructured tissues.

Published
2013
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2. Rab27A and its effector MyRIP link secretory granules to F-actin and control their motion towards release sites

Author

Isabelle Fanget, Sébastien Huet, François Darchen, Christine Petit, Catherine Chapuis, Graça Raposo, Viet Samuel Tran, Sophie Cribier, Geneviève de Saint Basile, Gaël Ménasché, Aziz El-Amraoui, Claire Desnos, Jean-Sébastien Schonn, Jean-Pierre Henry, Biologie cellulaire et moléculaire de la sécrétion (BCMS), Centre National de la Recherche Scientifique (CNRS), Institut de biologie physico-chimique (IBPC), Génétique des Déficits sensoriels, Institut Pasteur [Paris]-Centre National de la Recherche Scientifique (CNRS), Compartimentation et dynamique cellulaires (CDC), Centre National de la Recherche Scientifique (CNRS)-Institut Curie-Université Pierre et Marie Curie - Paris 6 (UPMC), Inserm U429 (CHU Necker - Enfants Malades [AP-HP]), Institut National de la Santé et de la Recherche Médicale (INSERM)-CHU Necker - Enfants Malades [AP-HP], Laboratoire de biologie physico-chimique des protéines membranaires (LBPC-PM (UMR_7099)), Université Paris Diderot - Paris 7 (UPD7)-Centre National de la Recherche Scientifique (CNRS)-Institut de biologie physico-chimique (IBPC), Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), J.-S. Schonn was supported by a fellowship from the Fondation de la Recherche Médicale, and S. Huet was supported by the Direction Générale de l’Armement. This work was supported by a grant from the Ministère de la Recherche (DRAB)., Centre National de la Recherche Scientifique (CNRS)-Institut Curie [Paris]-Université Pierre et Marie Curie - Paris 6 (UPMC), Developpement Normal et Pathologique du Système Immunitaire, Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Chaire Génétique et physiologie cellulaire, Collège de France (CdF (institution)), Institut de biologie physico-chimique (IBPC (FR_550)), Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS)-Université Paris Diderot - Paris 7 (UPD7)-Centre National de la Recherche Scientifique (CNRS), J.-S. Schonn was supported by a fellowship from the Fondation de la Recherche Médicale, and S. Huet was supported by the Direction Générale de l'Armement. This work was supported by a grant from the Ministère de la Recherche (DRAB)., Chapuis, Catherine, Institut Pasteur [Paris] (IP)-Centre National de la Recherche Scientifique (CNRS), Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut Curie [Paris]-Centre National de la Recherche Scientifique (CNRS), Collège de France - Chaire Génétique et physiologie cellulaire, Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS)-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS)-Université Paris Diderot - Paris 7 (UPD7)-Centre National de la Recherche Scientifique (CNRS), Biologie cellulaire et moléculaire de la sécrétion ( BCMS ), Centre National de la Recherche Scientifique ( CNRS ), Institut de Génétique et Développement de Rennes ( IGDR ), Université de Rennes 1 ( UR1 ), Université de Rennes ( UNIV-RENNES ) -Université de Rennes ( UNIV-RENNES ) -Centre National de la Recherche Scientifique ( CNRS ) -Structure Fédérative de Recherche en Biologie et Santé de Rennes ( Biosit : Biologie - Santé - Innovation Technologique ), Institut Pasteur [Paris]-Centre National de la Recherche Scientifique ( CNRS ), Compartimentation et dynamique cellulaires ( CDC ), Centre National de la Recherche Scientifique ( CNRS ) -INSTITUT CURIE-Université Pierre et Marie Curie - Paris 6 ( UPMC ), Université Paris Descartes - Paris 5 ( UPD5 ) -Institut National de la Santé et de la Recherche Médicale ( INSERM ) -Centre National de la Recherche Scientifique ( CNRS ), Laboratoire de biologie physico-chimique des protéines membranaires ( LBPC-PM ), and Université Paris Diderot - Paris 7 ( UPD7 ) -Institut de Biologie Physico-Chimique-Centre National de la Recherche Scientifique ( CNRS )

Subjects
Chromaffin Cells, [SDV]Life Sciences [q-bio], Rab27A, MyRIP, exocytosis, actin, neuroendocrine cell, [SDV.BC.BC]Life Sciences [q-bio]/Cellular Biology/Subcellular Processes [q-bio.SC], PC12 Cells, rab27 GTP-Binding Proteins, 0302 clinical medicine, Depsipeptides, Myosin, 0303 health sciences, Secretory Vesicle, Cell biology, Actin Cytoskeleton, Melanophilin, Thiazolidines, endocrine system, Myosin Type V, macromolecular substances, [SDV.BC]Life Sciences [q-bio]/Cellular Biology, Biology, Peptides, Cyclic, Exocytosis, Article, 03 medical and health sciences, [SDV.BC.BC] Life Sciences [q-bio]/Cellular Biology/Subcellular Processes [q-bio.SC], Animals, RAB27, Actin, 030304 developmental biology, Adaptor Proteins, Signal Transducing, Myosin Heavy Chains, Secretory Vesicles, [ SDV.BC.BC ] Life Sciences [q-bio]/Cellular Biology/Subcellular Processes [q-bio.SC], Cell Biology, Actin cytoskeleton, Bridged Bicyclo Compounds, Heterocyclic, Actins, Rats, Microscopy, Electron, Thiazoles, rab GTP-Binding Proteins, Latrunculin, Cattle, Carrier Proteins, 030217 neurology & neurosurgery
Abstract

International audience; The GTPase Rab27A interacts with myosin-VIIa and myosin-Va via MyRIP or melanophilin and mediates melanosome binding to actin. Here we show that Rab27A and MyRIP are associated with secretory granules (SGs) in adrenal chromaffin cells and PC12 cells. Overexpression of Rab27A, GTPase-deficient Rab27A-Q78L, or MyRIP reduced secretory responses of PC12 cells. Amperometric recordings of single adrenal chromaffin cells revealed that Rab27A-Q78L and MyRIP reduced the sustained component of release. Moreover, these effects on secretion were partly suppressed by the actin-depolymerizing drug latrunculin but strengthened by jasplakinolide, which stabilizes the actin cortex. Finally, MyRIP and Rab27A-Q78L restricted the motion of SGs in the subplasmalemmal region of PC12 cells, as measured by evanescent-wave fluorescence microscopy. In contrast, the Rab27A-binding domain of MyRIP and a MyRIP construct that interacts with myosin-Va but not with actin increased the mobility of SGs. We propose that Rab27A and MyRIP link SGs to F-actin and control their motion toward release sites through the actin cortex.

Published
2003
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3. Analysis of Transient Behavior in Complex Trajectories: Application to Secretory Vesicle Dynamics

Author

Sophie Cribier, Viet Samuel Tran, Erdem Karatekin, Sébastien Huet, Isabelle Fanget, Jean-Pierre Henry, Biologie cellulaire et moléculaire de la sécrétion (BCMS), Centre National de la Recherche Scientifique (CNRS), Physico-chimie moléculaire des membranes biologiques (PCMMB), Centre National de la Recherche Scientifique (CNRS)-Université Paris Diderot - Paris 7 (UPD7), and Godard, Edith

Subjects
Physics, 0303 health sciences, Diffusion (acoustics), Movement, Secretory Vesicles, media_common.quotation_subject, Dynamics (mechanics), Biophysics, Motion (geometry), Curvature, Asymmetry, Displacement (vector), Cell Line, 03 medical and health sciences, 0302 clinical medicine, Microscopy, Fluorescence, Image Interpretation, Computer-Assisted, Trajectory, Humans, Transient (computer programming), Other, Biological system, 030217 neurology & neurosurgery, 030304 developmental biology, media_common
Abstract

Analysis of trajectories of dynamical biological objects, such as breeding ants or cell organelles, is essential to reveal the interactions they develop with their environments. Many previous works used a global characterization based on parameters calculated for entire trajectories. In cases where transient behavior was detected, this usually concerned only a particular type, such as confinement or directed motion. However, these approaches are not appropriate in situations in which the tracked objects may display many different types of transient motion. We have developed a method to exhaustively analyze different kinds of transient behavior that the tracked objects may exhibit. The method discriminates stalled periods, constrained and directed motions from random dynamics by evaluating the diffusion coefficient, the mean-square displacement curvature, and the trajectory asymmetry along individual trajectories. To detect transient motions of various durations, these parameters are calculated along trajectories using a rolling analysis window whose width is variable. The method was applied to the study of secretory vesicle dynamics in the subplasmalemmal region of human carcinoid BON cells. Analysis of transitions between transient motion periods, combined with plausible assumptions about the origin of each motion type, leads to a model of dynamical subplasmalemmal organization.

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