Video Experimental Relacionado

Updated: Jan 4, 2026

Purification of Human S100A12 and Its Ion-induced Oligomers for Immune Cell Stimulation

Purification of Human S100A12 and Its Ion-induced Oligomers for Immune Cell Stimulation

Published on: September 29, 2019

Conjunto multimérico dependiente de disulfuro de las hormonas de la familia de las resistencias

Saurabh D Patel¹, Michael W Rajala, Luciano Rossetti

¹Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032, USA.

Science (New York, N.Y.)

|May 25, 2004

Resumen

La resistina, una hormona relacionada con la obesidad y la diabetes, circula como hexámero y trímero. La interrupción de los enlaces disulfuro en los trímeres de resistencia aumenta sus efectos sensibilizantes a la insulina, lo que sugiere un paso clave de activación.

Área de la Ciencia:

La bioquímica es la bioquímica.
Endocrinología Endocrinología.
Biología Estructural Biología estructural.

Sus antecedentes:

La resistina es una hormona secretada por los adipocitos.
Antagoniza la acción de la insulina en el hígado.
Resistin puede vincular la obesidad con la diabetes.

Objetivo del estudio:

Para investigar la estructura multimérica de las resistencias.
Determinar el papel de los enlaces disulfuro en la función de la resistin.
Para explorar el mecanismo de activación de la resistina.

Principales métodos:

Se utilizó la cristalografía de rayos X para determinar las estructuras de resistin y RELMbeta.
Se analizaron muestras de suero para identificar estados de ensamblaje de resistin.
Se realizaron estudios de pinzas de insulina pancreática con resistencias de tipo silvestre y mutantes.

Principales resultados:

Resistin y RELMbeta exhiben estructuras multiméricas inusuales con dominios de cabeza y cola.
La resistin forma hexámeres a través de las interacciones bobina-bobina y enlaces disulfuro.
La resistina circula en formas hexámeras y trímeras.
Un mutante resistente que carecía de enlaces disulfuro de intertrímero mostró una mayor sensibilidad hepática a la insulina.

Conclusiones:

La estructura de Resistin incluye segmentos en espiral en espiral alfa-helical que forman hexámeres.
El procesamiento de enlaces disulfuro es crucial para la activación de la resistin.
Comprender la estructura y la activación de la resistina puede ofrecer nuevos objetivos terapéuticos para la diabetes.

Más Videos Relacionados

Combining Non-reducing SDS-PAGE Analysis and Chemical Crosslinking to Detect Multimeric Complexes Stabilized by Disulfide Linkages in Mammalian Cells in Culture

Combining Non-reducing SDS-PAGE Analysis and Chemical Crosslinking to Detect Multimeric Complexes Stabilized by Disulfide Linkages in Mammalian Cells in Culture

Published on: May 2, 2019

Production of Disulfide-stabilized Transmembrane Peptide Complexes for Structural Studies

Production of Disulfide-stabilized Transmembrane Peptide Complexes for Structural Studies

Published on: March 6, 2013

Videos de Conceptos Relacionados

Assembly of Signaling Complexes

Assembly of Signaling Complexes

Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...

Protein Modifications in the RER

Protein Modifications in the RER

Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal...

Protein Complex Assembly

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types. Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...

Protein and Protein Structure

Protein and Protein Structure

Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme...

Oligosaccharide Assembly

Oligosaccharide Assembly

Protein glycosylation starts in the ER lumen and continues in the Golgi apparatus. Glycosyltransferases catalyze the addition of sugar molecules or glycosylation of proteins. Usually, these enzymes add sugars to the hydroxyl groups of selected serine or threonine residues to form O-linked glycans or the amino groups of asparagine residues to form N-linked glycans. Different positions on the same polypeptide chain can contain differently linked glycans.
Multiple sugar molecules that may or may...

Protein Complexes with Interchangeable Parts

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order...