The Role of Type I Collagen Heterotrimers and Homotrimers in Mechanical Strength and Collagen Cleavage PDF Download
Are you looking for read ebook online? Search for your book and save it on your Kindle device, PC, phones or tablets. Download The Role of Type I Collagen Heterotrimers and Homotrimers in Mechanical Strength and Collagen Cleavage PDF full book. Access full book title The Role of Type I Collagen Heterotrimers and Homotrimers in Mechanical Strength and Collagen Cleavage by Shu-Wei Chang (Ph. D.). Download full books in PDF and EPUB format.
Author: Shu-Wei Chang (Ph. D.)
Publisher:
ISBN:
Category :
Languages : en
Pages : 155
Get Book Here
Book Description
Collagen is a crucial structural protein, formed through a hierarchical assembly of molecules, arranged in collagen fibrils, which constitutes the basis for larger-scale fibers. Normal type I collagen is a heterotrimer triple-helical molecule consisting of two alpha-1 chains and one alpha-2 chain. A mouse model of the genetic brittle bone disease, osteogenesis imperfecta, oim, is characterized by a replacement of the alpha-2 chain by an alpha-1 chain, resulting in a homotrimer collagen molecule. Experimental studies of oim mice tendon and bone have shown reduced mechanical strength compared to normal mice. The relationship between the molecular content and the decrease in strength is, however, still unknown. In this thesis, we use a bottom-up molecular simulation approach to examine the role of type I normal collagen and oim collagen from a single collagen molecule to collagen microfibril to mineralized collagen microfibril. At the molecular level, we find that the replacement of the alpha-2 chain results in a collagen molecule with more kinks and a more thermally stable cleavage site. The higher thermal stability of the cleavage site of the homotrimer explains the enzyme resistances of homotrimers. Furthermore, we reveal a molecular mechanism of force induced stabilization of collagen against enzymatic breakdown for the heterotrimer. At the fibril level, we find that the kinks affect the packing of collagen molecules. The homotrimer microfibril has a less dense packing of collagen molecules which leads to a reduced modulus. The alterations on the assembly of collagen molecules further alter the space for mineral deposition at the mineralized collagen fibril level. We find that the mineralized homotrimer collagen fibril has more space for mineral deposition but the mineral size is smaller because the kinks at the molecular level result in a more discontinuous space for mineral deposition. The mineralized oim collagen microfibril has a reduced modulus due to the alterations on the collagen assembly and mineral deposition. Our results provide fundamental insight into the effect of the loss of alpha-2 chain at the molecular level and help understanding the molecular origin of many diseases such as the brittle bone at much larger length-scales.
Author: Shu-Wei Chang (Ph. D.)
Publisher:
ISBN:
Category :
Languages : en
Pages : 155
Get Book Here
Book Description
Collagen is a crucial structural protein, formed through a hierarchical assembly of molecules, arranged in collagen fibrils, which constitutes the basis for larger-scale fibers. Normal type I collagen is a heterotrimer triple-helical molecule consisting of two alpha-1 chains and one alpha-2 chain. A mouse model of the genetic brittle bone disease, osteogenesis imperfecta, oim, is characterized by a replacement of the alpha-2 chain by an alpha-1 chain, resulting in a homotrimer collagen molecule. Experimental studies of oim mice tendon and bone have shown reduced mechanical strength compared to normal mice. The relationship between the molecular content and the decrease in strength is, however, still unknown. In this thesis, we use a bottom-up molecular simulation approach to examine the role of type I normal collagen and oim collagen from a single collagen molecule to collagen microfibril to mineralized collagen microfibril. At the molecular level, we find that the replacement of the alpha-2 chain results in a collagen molecule with more kinks and a more thermally stable cleavage site. The higher thermal stability of the cleavage site of the homotrimer explains the enzyme resistances of homotrimers. Furthermore, we reveal a molecular mechanism of force induced stabilization of collagen against enzymatic breakdown for the heterotrimer. At the fibril level, we find that the kinks affect the packing of collagen molecules. The homotrimer microfibril has a less dense packing of collagen molecules which leads to a reduced modulus. The alterations on the assembly of collagen molecules further alter the space for mineral deposition at the mineralized collagen fibril level. We find that the mineralized homotrimer collagen fibril has more space for mineral deposition but the mineral size is smaller because the kinks at the molecular level result in a more discontinuous space for mineral deposition. The mineralized oim collagen microfibril has a reduced modulus due to the alterations on the collagen assembly and mineral deposition. Our results provide fundamental insight into the effect of the loss of alpha-2 chain at the molecular level and help understanding the molecular origin of many diseases such as the brittle bone at much larger length-scales.
Author: Morten Karsdal
Publisher: Academic Press
ISBN: 0128098996
Category : Science
Languages : en
Pages : 274
Get Book Here
Book Description
Biochemistry of Collagens, Laminins, and Elastin: Structure, Function, and Biomarkers provides a comprehensive introduction to collagen and structural proteins. Type I collagen is one of the most abundant molecules in the body, playing essential roles in different tissues, particularly bone and skin. A key aspect of type I collagen is its post-translational modifications which are essential for correct synthesis and structural integrity of collagens, for tissue-specific functionality, as well as for application as biomarkers of different pathologies. This volume summarizes current data on key structural proteins (collagens, laminins and elastin), reviews how these molecules affect pathologies, and describes selected modifications of proteins that result in altered signaling properties of the original extracellular matrix component. Further, it discusses the novel concept that an increasing number of components of the ECM harbor cryptic signaling functions that may be viewed as endocrine functions. Additionally, it highlights how this knowledge can be exploited to modulate fibrotic disease. - Provides a comprehensive introduction to collagen and structural proteins - Provides insight into emerging analytical technologies that can detect biomarkers of extracellular matrix degradation - Includes a chapter dedicated to the biomarkers of structural proteins - Contains insights into the biochemical interactions and changes to structural composition of proteins in disease states
Author: Peter Fratzl
Publisher: Springer Science & Business Media
ISBN: 0387739068
Category : Technology & Engineering
Languages : en
Pages : 516
Get Book Here
Book Description
Not only does this book provide a comprehensive review of current research advances in collagen structure and mechanics, it also explores this biological macromolecule’s many applications in biomaterials and tissue engineering. Readers gain an understanding of the structure and mechanical behavior of type I collagen and collagen-based tissues in vertebrates across all length scales, from the molecular (nano) to the organ (macro) level.
Author: Jaroslava Halper
Publisher: Springer Science & Business Media
ISBN: 9400778937
Category : Medical
Languages : en
Pages : 246
Get Book Here
Book Description
This volume is a reference handbook focusing on diseases like Marfan syndrome, Ehlers-Danlos syndrome, Loeys-Dietz syndrome and other heritable soft connective tissue diseases. The book presents detailed information for both basic scientists and for clinicians seeing patients. It is also a stepping stone for new investigations and studies that goes beyond the facts about the composition and biochemistry of the connective tissue and extracellular matrix, as the authors connect individual components to specific aspects of various soft tissue disorders and to the actual or potential treatment of them. Progress in Heritable Soft Connective Tissue Diseases features very prominent physicians and scientists as contributors who bring their most recent discoveries to the benefit of readers. Their expertise will help clinicians with proper diagnosis of sometimes elusive and uncommon heritable diseases of soft connective tissues. This book also offers an update on the pathophysiology of these diseases, including an emphasis on unifying aspects such as connections between embryonic development of the different types of connective tissues and systems, and the role of TGF-beta in development and physiology of soft tissues. This new set of data explains, at least in part, why many of these disorders are interconnected, though the primary pathophysiological events, such as gene mutations, may be different for each disorder.
Author: Sylvie Ricard-Blum
Publisher: Oxford University Press, USA
ISBN: 9780198505457
Category : Medical
Languages : en
Pages : 178
Get Book Here
Book Description
This Protein Profile issue covers collagens VI, VII, VIII, IX, X, XII, XIV, XVI, and XIX. It contains information about constituents chains, biosynthesis and post-translational modifications, genes, molecular and supramolecular assemblies, interactions, tissue distribution, and degradation, genetic and acquired diseases. Also available are the EBI sequence data and alignments and a full bibliography.
Author: David A.D. Parry
Publisher: Springer
ISBN: 3319496743
Category : Science
Languages : en
Pages : 630
Get Book Here
Book Description
This book provides the readers with an up-to-date review of the design, structure and function of a representative selection of fibrous proteins in both health and disease. The importance of the α-helical coiled coil, a conformational motif based on the heptad repeat in the amino acid sequence of all α-fibrous proteins (and parts of some globular proteins) is underlined by three Chapters devoted to its design, structure, function and topology. Specific proteins covered in the text and which depend on the coiled coil for their structure and function, include the intermediate filament proteins, tropomyosin, myosin, paramyosin, fibrin and members of the spectrin superfamily. Also described are fibrous proteins based on the β-pleated sheet and collagen conformations. Recombinant structural proteins, especially of silk and collagen, are discussed in the context of developing new biomaterials with varied applications. Established researchers and postgraduate students in the fields of protein chemistry, biochemistry and structural biophysics will find Fibrous Proteins: Structures and Mechanisms to be an invaluable collection of topical reviews that describe the basic advances made in the field of fibrous proteins over the past decade. This book, written by recognized authorities in the field, provides a clear account of the current status of fibrous protein research and, in addition, establishes the basis for deciding the most appropriate directions for future activity, including the applications of protein engineering and the commercial exploitation of new biomaterials.
Author: Florence Ruggiero
Publisher: Springer Nature
ISBN: 3030675920
Category : Science
Languages : en
Pages : 343
Get Book Here
Book Description
This book aims at providing insights into the collagen superfamily and the remarkable diversity of collagen function within the extracellular matrix. Additionally, the mechanisms underlying collagen-related diseases such as dystrophic epidermolysis bullosa, osteogenesis imperfecta, as well as collagen-related myopathies and neurological disorders are discussed. Collagens are the most abundant extracellular matrix proteins in organisms. Their primary function is to provide structural support and strength to cells and to maintain biomechanical integrity of tissues. However, collagens can no longer be considered just as structural proteins. They can act as extracellular modulators of signaling events and serve critical regulatory roles in various cell functions during embryonic development and adult homeostasis. Furthermore, collagens are associated with a broad spectrum of heritability-related diseases known as “collagenopathies” that affect a multitude of organs and tissues including sensorial organs. The book is a useful introduction to the field for junior scientists, interested in extracellular matrix research. It is also an interesting read for advanced scientists and clinicians working on collagens and collagenopathies, giving them a broader view of the field beyond their area of specialization.
Author: Rodney Grahame
Publisher: Springer Science & Business Media
ISBN: 1447139003
Category : Medical
Languages : en
Pages : 281
Get Book Here
Book Description
Joint hypermobility, joint laxity or "double-jointedness" is no longer regarded as just a quaint clinical entity, but has gained recognition as a feature common to a heterogeneous group of generalized hereditary connective tissue disorders. This monograph examines the scientific basis, clinical features and treatment of this syndrome. The second edition has been thoroughly updated, with new contributions to cover in depth three areas in which new scientific advances have been made: biochemistry, genetics, and biomechanics. The case histories make fascinating reading, and the comprehensive coverage of the rarer hereditary disorders provides a valuable reference. From the reviews of the first edition: "This little book deals with a somewhat neglected subject and will prove useful in a number of ways." British Journal of Plastic Surgery #1 "This is a delightful book full of stimulating ideas, by three authors who have pooled their thoughts and the results of their studies." Journal of the Royal Society of Medicine #2
Author: Anthony Atala
Publisher: Academic Press
ISBN: 0123814235
Category : Science
Languages : en
Pages : 1203
Get Book Here
Book Description
Virtually any disease that results from malfunctioning, damaged, or failing tissues may be potentially cured through regenerative medicine therapies, by either regenerating the damaged tissues in vivo, or by growing the tissues and organs in vitro and implanting them into the patient. Principles of Regenerative Medicine discusses the latest advances in technology and medicine for replacing tissues and organs damaged by disease and of developing therapies for previously untreatable conditions, such as diabetes, heart disease, liver disease, and renal failure. - Key for all researchers and instituions in Stem Cell Biology, Bioengineering, and Developmental Biology - The first of its kind to offer an advanced understanding of the latest technologies in regenerative medicine - New discoveries from leading researchers on restoration of diseased tissues and organs
Author: Greta Pifat-Mrzljak
Publisher: Springer Science & Business Media
ISBN: 3642709052
Category : Science
Languages : en
Pages : 197
Get Book Here
Book Description
During the past decade we have witnessed not only an increase in knowledge of the "traditional" biophysical problems, but also an understanding of the molecular basis of various biological phenomena. The principles and methods of biophysics now provide an underpin ning of all of the basic biosciences and are the rational language for discussion between scientists of different disciplines. The International School on Biophysics Supramolecular Structure and Function held in Dubrovnik in September 1984 had as its goal to provide comprehensive discussions on a large number of subjects both for younger scientists at the doctoral or postdoctoral level interested in the molecular nature of fundamental biological entities, and for experienced scientists wishing to gain a broader insight into molecular structures and functions. The topics discussed at the School were inter- and intramolecular interactions in biological systems, and the structure, organization, and function of biological macromolecules and supramolecular assemblies. A number of topics were centered around either a biological problem or a physical technique, sometimes giving an unbalanced view of the field under discussion. Some of the topics required previous knowledge of basic biophysical principles, which were then applied to gain greater insight into the molecular functions of diverse supramolecular systems. Although not all the lectures could be prepared for publication in this volume, I hope that it contains valuable up-to-date information on various aspects of the molecular basis of life.
