Anagram & Information om | Engelska ordet INTEGRINS

Exempel på hur man kan använda INTEGRINS i en mening

• Fibronectin is a high-molecular weight (~500-~600 kDa) glycoprotein of the extracellular matrix that binds to membrane-spanning receptor proteins called integrins.
• CAMs are classified into four major families: integrins, immunoglobulin (Ig) superfamily, cadherins, and selectins.
• Fibronectin and other ECM proteins bind to cell surface receptor proteins called integrins that are built into the plasma membrane.
• Instead of desmogleins and desmocollins in the extracellular space, hemidesmosomes utilize integrins.
• Springer, Latham Family Professor of Pathology, CBR Institute for Biomedical Research, Harvard University Medical School: X-ray crystallography of integrins and their cytoplasmic activators.
• Like desmosomes, they tie to intermediate filaments in the cytoplasm, but in contrast to desmosomes, their transmembrane anchors are integrins rather than cadherins.
• This subunit is involved in the formation of the β-2 integrins (LFA-1, integrin alphaXbeta2/CR4/p150,95, and Mac-1/CR3) by dimerization with different CD11 subunits.
• It binds to integrins of type CD11a / CD18, or CD11b / CD18 and is also exploited by rhinovirus as a receptor for entry into respiratory epithelium.
• Fibronectin a glycoprotein that binds to receptor proteins known as integrins within the cytoskeleton is a key player in the hypothesized method of fibrillogenesis.
• After the physical barrier is removed, under the influence of the growth factors VEGF with addition contributions of other factors like angiopoietin-1, integrins, and chemokines play an essential role.
• In cell biology, CD11 is the α (alpha) component of various integrins, especially ones in which the β (beta) component is CD18 (β2) and mediate leukocyte adhesion.
• This protein can bind to fibrinogen, fibronectin, laminin, collagens types V and VII and integrins alpha-V/beta-1.
• Some of the highlights include the discovery of the RGD tripeptide as the cell attachment site in fibronectin, fibrinogen, and other adhesive proteins, and the discovery of integrins, the cell surface receptors that recognize the RGD sequence in matrix proteins.
• L-selectin is able to mediate vessel adhesion whereas α4 integrins, α4β1 or α4β7, can perform primary or secondary adhesion through a stronger tethering and even contribute to transendothelial migration of lymphocytes.
• This is achieved by activating the thromboxane receptor, which results in platelet-shape change, inside-out activation of integrins, and degranulation.
• This is assisted through juxtacrine activation of integrins by chemokines and soluble factors released by endothelial cells.
• GAB2 mediates the interactions between receptor tyrosine kinases (RTK) or non-RTK receptors, such as G protein coupled receptors, cytokine receptors, multichain immune recognition receptors and integrins, and the molecules of the intracellular signaling pathways.
• The LW glycoprotein has recently been renamed ICAM-4 due to its similarity to intercellular adhesion molecule, although exactly which integrins bind to ICAM-4 is subject to controversy.
• The protein links integrin subunits to the tyrosine kinase FYN, an initiating step in coupling integrins to the Ras-ERK pathway and promoting cell cycle progression.
• Although it is identified as a cell adhesion molecule, EpCAM does not structurally resemble any of the four major families of cell adhesion molecules, namely cadherins, integrins, selectins, and members of the immunoglobulin super-family.

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