Author: Annemieke Aagje de Melker
Publisher:
ISBN:
Category :
Languages : en
Pages : 167
Book Description
The Integrins [alpha]3[beta]1 and [alpha]6[beta]1
Author: Annemieke Aagje de Melker
Publisher:
ISBN:
Category :
Languages : en
Pages : 167
Book Description
Publisher:
ISBN:
Category :
Languages : en
Pages : 167
Book Description
Integrins in Health and Disease
Author: Donald Gullberg
Publisher: Springer Nature
ISBN: 3031237811
Category : Science
Languages : en
Pages : 473
Book Description
Integrins are heterodimeric cell surface receptors which anchor cells to different extracellular matrix proteins or act as cell-cell receptors. They play pivotal roles not only across a wide range of physiological processes including tissue morphogenesis, wound healing, and regulation of cell growth, but also in numerous pathological conditions such as autoimmunity, infectious disease, and carcinogenesis. This book aims to provide readers a summary of the most important integrins and their respective biological functions. Readers will learn about knockout- and animal models to study the functionality of key collagen-, laminin-, and nephronectin-binding integrins. Additionally, the role of integrins in pathological tissue remodeling in joints and in developing and diseased cardiac tissue are discussed. Reviews of the current knowledge of the role of integrins in tissue and tumor fibrosis, angiogenesis and tumor progression are an important part of this work. Finally, the book discusses integrins in the context of the immune system, how to target integrin-ligand interactions with antibodies, and the role of integrins as receptors for bacterial and viral cell invasion. Both experienced researchers and clinicians, as well as PhD students who wish to study the extracellular matrix and cell adhesion molecules will find “Integrins in Health and Disease - Key Effectors of Cell-Matrix and Cell-Cell Interactions” authoritative, easily accessible, and vastly informative. The series Biology of Extracellular Matrix is published in collaboration with the American Society for Matrix Biology and the International Society for Matrix Biology.
Publisher: Springer Nature
ISBN: 3031237811
Category : Science
Languages : en
Pages : 473
Book Description
Integrins are heterodimeric cell surface receptors which anchor cells to different extracellular matrix proteins or act as cell-cell receptors. They play pivotal roles not only across a wide range of physiological processes including tissue morphogenesis, wound healing, and regulation of cell growth, but also in numerous pathological conditions such as autoimmunity, infectious disease, and carcinogenesis. This book aims to provide readers a summary of the most important integrins and their respective biological functions. Readers will learn about knockout- and animal models to study the functionality of key collagen-, laminin-, and nephronectin-binding integrins. Additionally, the role of integrins in pathological tissue remodeling in joints and in developing and diseased cardiac tissue are discussed. Reviews of the current knowledge of the role of integrins in tissue and tumor fibrosis, angiogenesis and tumor progression are an important part of this work. Finally, the book discusses integrins in the context of the immune system, how to target integrin-ligand interactions with antibodies, and the role of integrins as receptors for bacterial and viral cell invasion. Both experienced researchers and clinicians, as well as PhD students who wish to study the extracellular matrix and cell adhesion molecules will find “Integrins in Health and Disease - Key Effectors of Cell-Matrix and Cell-Cell Interactions” authoritative, easily accessible, and vastly informative. The series Biology of Extracellular Matrix is published in collaboration with the American Society for Matrix Biology and the International Society for Matrix Biology.
Integrins
Author:
Publisher: Elsevier
ISBN: 0080551386
Category : Science
Languages : en
Pages : 613
Book Description
An integrin, or integrin receptor, is an integral membrane protein in the plasma membrane of cells. It plays a role in the attachment of a cell to the extracellular matrix (ECM) and to other cells, and in signal transduction from the ECM to the cell. There are many types of integrin, and many cells have multiple types on their surface. Integrins are of vital importance to all metazoans, from humans to sponges. This volume in Methods in Enzymology presents methods for studying integrins.
Publisher: Elsevier
ISBN: 0080551386
Category : Science
Languages : en
Pages : 613
Book Description
An integrin, or integrin receptor, is an integral membrane protein in the plasma membrane of cells. It plays a role in the attachment of a cell to the extracellular matrix (ECM) and to other cells, and in signal transduction from the ECM to the cell. There are many types of integrin, and many cells have multiple types on their surface. Integrins are of vital importance to all metazoans, from humans to sponges. This volume in Methods in Enzymology presents methods for studying integrins.
The Structure and Function of the [alpha]3[beta]1 and [alpha]6[beta]1 Integrins
Author: Gerredina Ozia Delwel
Publisher:
ISBN:
Category :
Languages : en
Pages : 125
Book Description
Publisher:
ISBN:
Category :
Languages : en
Pages : 125
Book Description
Integrin alpha Chains: Advances in Research and Application: 2011 Edition
Author:
Publisher: ScholarlyEditions
ISBN: 1464959218
Category : Science
Languages : en
Pages : 19
Book Description
Integrin alpha Chains: Advances in Research and Application: 2011 Edition is a ScholarlyPaper™ that delivers timely, authoritative, and intensively focused information about Integrin alpha Chains in a compact format. The editors have built Integrin alpha Chains: Advances in Research and Application: 2011 Edition on the vast information databases of ScholarlyNews.™ You can expect the information about Integrin alpha Chains in this eBook to be deeper than what you can access anywhere else, as well as consistently reliable, authoritative, informed, and relevant. The content of Integrin alpha Chains: Advances in Research and Application: 2011 Edition has been produced by the world’s leading scientists, engineers, analysts, research institutions, and companies. All of the content is from peer-reviewed sources, and all of it is written, assembled, and edited by the editors at ScholarlyEditions™ and available exclusively from us. You now have a source you can cite with authority, confidence, and credibility. More information is available at http://www.ScholarlyEditions.com/.
Publisher: ScholarlyEditions
ISBN: 1464959218
Category : Science
Languages : en
Pages : 19
Book Description
Integrin alpha Chains: Advances in Research and Application: 2011 Edition is a ScholarlyPaper™ that delivers timely, authoritative, and intensively focused information about Integrin alpha Chains in a compact format. The editors have built Integrin alpha Chains: Advances in Research and Application: 2011 Edition on the vast information databases of ScholarlyNews.™ You can expect the information about Integrin alpha Chains in this eBook to be deeper than what you can access anywhere else, as well as consistently reliable, authoritative, informed, and relevant. The content of Integrin alpha Chains: Advances in Research and Application: 2011 Edition has been produced by the world’s leading scientists, engineers, analysts, research institutions, and companies. All of the content is from peer-reviewed sources, and all of it is written, assembled, and edited by the editors at ScholarlyEditions™ and available exclusively from us. You now have a source you can cite with authority, confidence, and credibility. More information is available at http://www.ScholarlyEditions.com/.
Regulation of the Alpha-6/beta-1 Integrin Function by the Cytoplasmic Domains of the Alpha-6 Subunit
Author: Leslie MacDougall Shaw
Publisher:
ISBN:
Category : Cytoplasm
Languages : en
Pages : 220
Book Description
Publisher:
ISBN:
Category : Cytoplasm
Languages : en
Pages : 220
Book Description
The Integrin [alpha]6[beta]4
Author: Catharina Maria Niessen
Publisher:
ISBN:
Category :
Languages : en
Pages : 176
Book Description
Publisher:
ISBN:
Category :
Languages : en
Pages : 176
Book Description
Integrin Alpha Subunit Ratios, Cytoplasmic Domains, and Growth Factor Synergy Regulate Muscle Proliferation, Differentiation, and Signaling
Author:
Publisher:
ISBN:
Category :
Languages : en
Pages :
Book Description
Publisher:
ISBN:
Category :
Languages : en
Pages :
Book Description
Molecular Dynamics Models of Integrin Clustering and Activation Mechanisms
Author: Mehrdad Mehrbod
Publisher:
ISBN:
Category :
Languages : en
Pages : 114
Book Description
Integrins are Alpha-Beta transmembrane receptors that mediate cell-matrix and cell-cell adhesion, comprised of multi-domain, massive ectodomains, single-pass, transmembrane domains, and short, floppy cytoplasmic domains. They link the extracellular matrix or counter-receptors on other cells with the contractile cytoskeleton, mediating the transduction of mechanochemical signals across the plasma membrane and playing critical roles in a host of cellular functions, such as migration, cell traction, motility, platelet aggregation, and leukocyte transmigration. Functionally, integrins are switch-like proteins that can take on at least three different functional states: inactive, active, and ligand-bound. Integrin function is dependent upon allosteric conformational changes in its structure. Integrins are by default in an inactive (low affinity) state and can be activated via interacting with cytoplasmic proteins (e.g. talin) and/or engaging with extracellular ligands (e.g. fibrinogen). Integrin activation triggered by a cytoplasmic signal is called inside-out signaling, while outside-in signaling is defined as ligand-integrin binding followed by conformational changes in the transmembrane and cytoplasmic domains. Association of the integrin with the ligand induces quaternary changes in the integrin, leading to cell signaling and dynamic cell adhesion. However, atomistic details of these conformational changes as well as mechanisms of integrin clustering are not fully understood. This study employs molecular dynamics techniques to provide detailed, mechanistic answers for a few key questions on integrin (Alpha)IIb(Beta)3 function, a platelet-specific integrin member that plays a critical role in thrombosis. It is highly debated whether integrin transmembrane domains form homo-oligomers, leading to focal adhesion growth. This study suggests that homo- oligomerization of the Beta subunit potentially regulates integrin clustering, as opposed to the Alpha subunit, which appears to be a poor regulator for the clustering process. Two distinct hypotheses are proposed to explain the atomic mechanism of integrin activation and how conformational changes triggered by cytoplasmic/extracellular proteins are propagated across the integrin structure: The switch-blade and the deadbolt model. To reconcile these apparently-contradictory models for integrin activation, this work investigated the mechanism of integrin (Alpha)IIb(Beta)3 inside-out activation triggered by interactions with the cytoplasmic protein talin, and its outside-in activation as a result of exposure to the soluble RGD ligand. Finally, it was shown that the integrin Alpha subunit head domain regulates integrin-ligand binding affinity indirectly via inducing conformational changes in a key metal ion binding site (named LIMBS) in the Beta subunit head domain. Hence, it was concluded that different ligand binding affinities of integrin (Alpha)IIb(Beta)3 and (Alpha)V(Beta)3 is attributed to the larger attraction between the (Alpha)V subunit head domain and the metal ion binding site LIMBS.
Publisher:
ISBN:
Category :
Languages : en
Pages : 114
Book Description
Integrins are Alpha-Beta transmembrane receptors that mediate cell-matrix and cell-cell adhesion, comprised of multi-domain, massive ectodomains, single-pass, transmembrane domains, and short, floppy cytoplasmic domains. They link the extracellular matrix or counter-receptors on other cells with the contractile cytoskeleton, mediating the transduction of mechanochemical signals across the plasma membrane and playing critical roles in a host of cellular functions, such as migration, cell traction, motility, platelet aggregation, and leukocyte transmigration. Functionally, integrins are switch-like proteins that can take on at least three different functional states: inactive, active, and ligand-bound. Integrin function is dependent upon allosteric conformational changes in its structure. Integrins are by default in an inactive (low affinity) state and can be activated via interacting with cytoplasmic proteins (e.g. talin) and/or engaging with extracellular ligands (e.g. fibrinogen). Integrin activation triggered by a cytoplasmic signal is called inside-out signaling, while outside-in signaling is defined as ligand-integrin binding followed by conformational changes in the transmembrane and cytoplasmic domains. Association of the integrin with the ligand induces quaternary changes in the integrin, leading to cell signaling and dynamic cell adhesion. However, atomistic details of these conformational changes as well as mechanisms of integrin clustering are not fully understood. This study employs molecular dynamics techniques to provide detailed, mechanistic answers for a few key questions on integrin (Alpha)IIb(Beta)3 function, a platelet-specific integrin member that plays a critical role in thrombosis. It is highly debated whether integrin transmembrane domains form homo-oligomers, leading to focal adhesion growth. This study suggests that homo- oligomerization of the Beta subunit potentially regulates integrin clustering, as opposed to the Alpha subunit, which appears to be a poor regulator for the clustering process. Two distinct hypotheses are proposed to explain the atomic mechanism of integrin activation and how conformational changes triggered by cytoplasmic/extracellular proteins are propagated across the integrin structure: The switch-blade and the deadbolt model. To reconcile these apparently-contradictory models for integrin activation, this work investigated the mechanism of integrin (Alpha)IIb(Beta)3 inside-out activation triggered by interactions with the cytoplasmic protein talin, and its outside-in activation as a result of exposure to the soluble RGD ligand. Finally, it was shown that the integrin Alpha subunit head domain regulates integrin-ligand binding affinity indirectly via inducing conformational changes in a key metal ion binding site (named LIMBS) in the Beta subunit head domain. Hence, it was concluded that different ligand binding affinities of integrin (Alpha)IIb(Beta)3 and (Alpha)V(Beta)3 is attributed to the larger attraction between the (Alpha)V subunit head domain and the metal ion binding site LIMBS.
The Role of [alpha]7 Integrin During Myogenesis
Author: Chung-Chen Yao
Publisher:
ISBN:
Category : Integrins
Languages : en
Pages : 236
Book Description
Publisher:
ISBN:
Category : Integrins
Languages : en
Pages : 236
Book Description