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Skidmore College

4 ARTICLES PUBLISHED IN JoVE

Neuroscience

Dissection and Lateral Mounting of Zebrafish Embryos: Analysis of Spinal Cord Development

Aaron P. Beck¹, Roland M. Watt¹, Jennifer Bonner¹

Developmental processes such as proliferation, patterning, differentiation, and axon guidance can be readily modeled in the zebrafish spinal cord. In this article, we describe a mounting procedure for zebrafish embryos, which optimizes visualization of these events.

JoVE Core

Treating SCA1 Mice with Water-Soluble Compounds to Non-Specifically Boost Mitochondrial Function

Austin Ferro¹, Emily Carbone¹, Evan Marzouk¹, Asher Siegel², Donna Nguyen¹, Kailen Polley¹, Jessilyn Hartman¹, Kimberley Frederick², Stephen Ives³, Sarita Lagalwar¹

¹Neuroscience Program, Skidmore College, ²Chemistry Department, Skidmore College, ³Health and Exercise Science Department, Skidmore College

We present a biochemical and behavioral protocol to evaluate the efficacy of mitochondria-targeted water-soluble compounds for the treatment of Spinocerebellar ataxia type 1 (SCA1) and other cerebellar neurodegenerative diseases.

JoVE Core

Atomic Absorbance Spectroscopy to Measure Intracellular Zinc Pools in Mammalian Cells

Shellaina J.V. Gordon^*1, Yao Xiao^*2, Amanda L. Paskavitz³, Napoleón Navarro-Tito⁴, Juan G. Navea², Teresita Padilla-Benavides¹

¹Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, ²Department of Chemistry, Skidmore College, ³Candiac MR Center, Beth Israel Deaconess Medical Center, ⁴Facultad de Ciencias Químico Biológicas, Universidad Autónoma de Guerrero

Cultured primary or established cell lines are commonly used to address fundamental biological and mechanistic questions as an initial approach before using animal models. This protocol describes how to prepare whole cell extracts and subcellular fractions for studies of zinc (Zn) and other trace elements with atomic absorbance spectroscopy.

Biochemistry

Concanavalin A-Based Sedimentation Assay to Measure Substrate Binding of Glucan Phosphatases

Eliana M. Wolpaw^*1, Marissa L. Frenett^*1, Claudia A. Mak¹, Sloane M. Zwanger¹, Madushi Raththagala¹

¹Department of Chemistry, Skidmore College

This method describes a lectin-based in vitro sedimentation assay to quantify the binding affinity of glucan phosphatase and amylopectin. This co-sedimentation assay is reliable for measuring glucan phosphatase substrate binding and can be applied to various solubilized glucan substrates.