Video Experimental Relacionado
Updated: Aug 18, 2026

10:31
Real-time Live Imaging of T-cell Signaling Complex Formation
Published on: June 23, 2013
Redistribución de los filamentos intermedios durante el encapsulamiento de las moléculas de superficie de los
Nature
|July 15, 1982
Resumen
Este estudio revela que la vimentina, un componente clave de los filamentos intermedios en los linfocitos humanos, se redistribuye a la tapa de la superficie celular durante la tapa. Esto sugiere que los filamentos intermedios se anclan dentro del urópodo.
Área de la Ciencia:
- Biología celular Biología celular.
- Dinámica del citoesqueleto Dinámica del citoesqueleto
- Inmunología Inmunología.
Sus antecedentes:
- Los filamentos intermedios (FI) forman una importante red citoplasmática en las células eucariotas, distinta de la actina y los microtúbulos.
- La vimentina es la principal proteína IF en las células mesenquimales y las células no mesenquimales cultivadas.
- Se identificó un anticuerpo monoclonal contra la vimentina en un paciente con macroglobulinemia de Waldenström.
Objetivo del estudio:
- Para investigar la presencia y la organización de la vimentina en los linfocitos humanos.
- Para determinar el efecto de la molécula de superficie que cubre la red de filamentos intermedios en los linfocitos.
- Explorar el papel potencial de los filamentos intermedios en el encapsulamiento de los linfocitos y la formación de urópodos.
Principales métodos:
- Inmunofluorescencia directa mediante el uso de un anticuerpo monoclonal anti-vimentin.
- Tratamiento de las células con colcemida para inducir la agregación de filamentos intermedios.
- Inducción del encapsulamiento de las moléculas superficiales (beta 2-microglobulina o inmunoglobulinas de membrana).
- Observación microscópica de la redistribución de la vimentina en respuesta al tope.
Principales resultados:
- Los linfocitos B y T humanos poseen filamentos intermedios compuestos de vimentina.
- El tratamiento con colcemida causó que la vimentina se agregara de manera juxtanuclear.
- El encapsulamiento de las moléculas superficiales condujo a la redistribución de vimentina debajo del encapsulamiento.
- En las células tratadas con colcemida, la ubicación de la tapa se superpuso constantemente con el agregado de vimentina.
Conclusiones:
- La vimentina es una importante proteína de filamento intermedio en los linfocitos humanos.
- La captura de la superficie de los linfocitos induce una reorganización dinámica de la red de vimentina.
- Los hallazgos sugieren que los filamentos intermedios están anclados dentro del urópodo, jugando un papel en el encapsulamiento de los linfocitos.
Videos de Conceptos Relacionados
Adaptability of Cytoskeletal Filaments
The cytoskeleton is a complex dynamic structure performing varied functions based on cellular requirements. The adaptability of the individual filaments in the cytoskeleton determines their ability to perform various functions within the cell. It can undergo rapid reorganization during processes like cell division or remain stable for several hours as in the interphase. The adaptability of these filaments depends on stringent regulatory mechanisms. The microfilament and microtubules of the...
Formation of Intermediate Filaments
Intermediate filaments are cytoskeletal proteins with higher tensile strength and flexibility than microfilaments and microtubules. Unlike the other two cytoskeletal proteins, intermediate filament formation lacks the enzymatic activity to hydrolyze nucleotides like ATP and GTP to generate energy for polymerization. Therefore, the formation of intermediate filaments is multistep self-assembly. The involvement of any accessory proteins in intermediate filament formation has not yet been reported.
Mechanism of Filopodia Formation
Filopodia are thin, actin-rich cellular protrusions that play an important role in many fundamental cellular functions. They vary in their occurrence, length, and positioning in different cell types, suggesting their diverse roles.
Their main function is to guide migrating cells during normal tissue morphogenesis or cancer metastasis by recognizing and making initial contacts with the extracellular matrix. However, they can also act as stationary cell anchors or help to establish communication...
Their main function is to guide migrating cells during normal tissue morphogenesis or cancer metastasis by recognizing and making initial contacts with the extracellular matrix. However, they can also act as stationary cell anchors or help to establish communication...
Mechanism of Lamellipodia Formation
Cells migrating in response to external stimuli form lamellipodia, which are thin membrane protrusions supported by a mesh of linked, branched, or unbranched actin filaments. These actin filaments interact with myosin motor proteins, creating the dynamic actomyosin complex within the cytoskeleton. Contractility, or the ability to generate contractile stress, is inherent to the actomyosin complex. It helps cells detect the stiffness of the surrounding ECM and exert contractile force for...
Disassembly of Intermediate Filaments
Intermediate filaments (IFs) do not undergo spontaneous disassembly. Enzymes, kinases, and phosphatases add and remove phosphates from specific sites to regulate their disassembly. The IF concentration in the cytoplasm also regulates the disassembly. If the concentration crosses a threshold, it activates the protein kinases in the vicinity, allowing the phosphorylation of IFs.
Keratin proteins, found at the cell periphery near cell junctions, undergo a cycle of assembly and disassembly. In Type...
Keratin proteins, found at the cell periphery near cell junctions, undergo a cycle of assembly and disassembly. In Type...
Immunoglobulin-like Cell Adhesion Molecules
Immunoglobulin-like cell adhesion molecules or Ig-CAMs are a versatile group of cell surface glycoproteins belonging to the immunoglobulin protein superfamily. Ig-CAMs possess the characteristic immunoglobulin protein domains and other domains such as the fibronectin type III domain. The Ig domains are glycosylated to varying degrees in different Ig-CAMs.
Ig-CAMs exhibit either homophilic binding (to other Ig-CAMs) or heterophilic binding (to other ligands such as integrins). While most Ig-CAMs...
Ig-CAMs exhibit either homophilic binding (to other Ig-CAMs) or heterophilic binding (to other ligands such as integrins). While most Ig-CAMs...

