The Microfibril-Elastin Fiber System Distribution in Left Atrioventricular Valve of the Rat
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The Science of Aging Skin Leslie Baumann, MD; Susan Weinkle, MD
REVIEW Improving Elasticity: The Science of Aging Skin Leslie Baumann, MD; Susan Weinkle, MD Although collagen changes from both chronologic aging and photoaging have been well stud- ied, there is a dearth of research into the elastin component of the dermis. No products have been approved by the US Food and Drug Administration for either replacing elastin or stimulating its syn- thesis. Recently, a zinc complex was shown to increase dermal elastin staining, hypodermal fat, and epidermal thickness in animal studies. Histologic studies of the same zinc complex in humans have revealed increased deposition of functional elastin fibers following 10 days of use. In the clinical trials reported here, there was an increase in functional elastin, as well as improvements in fine lines and wrinkles. COSNo adverse events were noted. DERM ollagen and elastin are the fibers that make collagen bundles and endow the skin with rebounding up the dermal matrix. Cosmetic dermatol- properties. Tropoelastin molecules, which are precur- ogists have long used topical medications, sors to elastin, bind covalently with cross-links to form fillers, and light-based and laser-based elastin. Elastin fibers are assembled on bundles of micro- therapies to improve the loss of collagen fibrils composed of fibrillin. The latter forms a template Cthat occurs in aging skin. However, until recently, no fill- on which elastin is deposited.1 Most elastin production ers orDo topical agents have been availableNot to treat the loss is restricted Copy to a narrow window of development. Elas- of function of elastin, which is also an important feature togenesis increases dramatically during fetal life, peaks of dermal photoaging. -
Flavio Akira Sakae Distribuição Das Fibras Colágenas E Do Sistema De
Flavio Akira Sakae Distribuição das fibras colágenas e do sistema de fibras elásticas na camada superficial da lâmina própria da prega vocal com edema de Reinke Tese apresentada à Faculdade de Medicina da Universidade de São Paulo para obtenção do título de Doutor em Ciências Área de concentração: Otorrinolaringologia Orientador: Prof. Dr. Domingos Hiroshi Tsuji São Paulo 2008 Dados Internacionais de Catalogação na Publicação (CIP) Preparada pela Biblioteca da Faculdade de Medicina da Universidade de São Paulo Óreprodução autorizada pelo autor Sakae, Flavio Akira Distribuição das fibras colágenas e do sistema de fibras elásticas na camada superficial da lâmina própria da prega vocal com edema de Reinke / Flavio Akira Sakae. -- São Paulo, 2008. Tese(doutorado)--Faculdade de Medicina da Universidade de São Paulo. Departamento de Oftalmologia e Otorrinolaringologia. Área de concentração: Otorrinolaringologia. Orientador: Domingos Hiroshi Tsuji. Descritores: 1.Edema laríngeo 2.Colágeno 3.Tecido elástico 4.Membrana mucosa 5.Cordas vocais USP/FM/SBD-146/08 "O único homem que está isento de erros, é aquele que não arrisca acertar." Albert Einstein Dedicatória Aos meus queridos pais, Masao e Junko, por tudo que fazem por mim, pelo apoio incondicional e amor eterno. São os meus ídolos. A minha esposa, Renata, amor da minha vida, pela alegria de viver, companheirismo e incentivo constante. A minha irmã, Cristiane, por ter contribuído em todos os passos de minha vida. Agradecimentos Ao meu orientador, Prof. Dr. Domingos Hiroshi Tsuji pela oportunidade e apoio na concretização deste sonho. Sua amizade e franqueza foram essenciais na elaboração deste trabalho. É o grande mestre. Ao Prof. Dr. -
Loss of Skin Elasticity Is Associated with Pulmonary Emphysema, Biomarkers of Inflammation, and Matrix Metalloproteinase Activity in Smokers Michael E
O’Brien et al. Respiratory Research (2019) 20:128 https://doi.org/10.1186/s12931-019-1098-7 RESEARCH Open Access Loss of skin elasticity is associated with pulmonary emphysema, biomarkers of inflammation, and matrix metalloproteinase activity in smokers Michael E. O’Brien1, Divay Chandra1, Robert C. Wilson1, Chad M. Karoleski1, Carl R. Fuhrman2, Joseph K. Leader2, Jiantao Pu2, Yingze Zhang1, Alison Morris1,3, Seyed Nouraie1, Jessica Bon1,4, Zsolt Urban5 and Frank C. Sciurba1* Abstract Background: Elastin breakdown and the resultant loss of lung elastic recoil is a hallmark of pulmonary emphysema in susceptible individuals as a consequence of tobacco smoke exposure. Systemic alterations to the synthesis and degradation of elastin may be important to our understanding of disease phenotypes in chronic obstructive pulmonary disease. We investigated the association of skin elasticity with pulmonary emphysema, obstructive lung disease, and blood biomarkers of inflammation and tissue protease activity in tobacco-exposed individuals. Methods: Two hundred and thirty-six Caucasian individuals were recruited into a sub-study of the University of Pittsburgh Specialized Center for Clinically Orientated Research in chronic obstructive pulmonary disease, a prospective cohort study of current and former smokers. The skin viscoelastic modulus (VE), a determinant of skin elasticity, was recorded from the volar forearm and facial wrinkling severity was determined using the Daniell scoring system. Results: In a multiple regression analysis, reduced VE was significantly associated with cross-sectional measurement of airflow obstruction (FEV1/FVC) and emphysema quantified from computed tomography (CT) images, β = 0.26, p = 0.001 and β = 0.24, p = 0.001 respectively. -
Differentiation of the Secondary Elastic Cartilage in the External Ear of the Rat
Int..I. Dc\'. Bi,,!. 35: 311-320 (1991) 311 Differentiation of the secondary elastic cartilage in the external ear of the rat ZELIMIR BRADAMANTE*', LJILJANA KOSTOVIC-KNEZEVIC', BOZICA LEVAK-SVAJGER' and ANTON SVAJGER' 'Institute of Histology and Embryology and 2/nstitute of Biology, Faculty of Medicine, University of Zagreb, Republic of Croatia, Yugoslavia ABSTRACT The cartilage in the external ear of the rat belongs to the group of secondary cartilages and it has a unique structural organization. The chondrocytes aretransformed intotypical adipose cells, the proteoglycan cartilage matrix is reduced to thin capsules around the cells and the rest of the extracelullar matrix is occupied by a network of coarse elastic fibers. It appears late in development 116-day fetus) and needs more than one month for final development. The differentiation proceeds in several steps which partly overlap: the appearance of collagen fibrils, elastin fibers, the proteoglycan matrix, and the adipose transformation of chondrocytes. The phenotype of this cartilage and the course of its differentiation are very stable, even in very atypical experimental environmental conditions. The only exceptions are explants in organ culture in vitro and perichondrial regenerates. In these conditions the development of elastic fibers is slow and poor while the production of the proteogycan matrix is abundant. The resulting cartilage then displays structural characteristics of hyaline cartilage rather than those of the initial elastic one. KEY WORDS: elastic mrlilagf, tI/(Wdrogfllt'.\'i.\. plasfogellf'.\is, extenuil Ntr, rat Introduction Structural organization The elastic cartilage belongs to the group of secondary or ac- According to Baecker (1928) and Schaffer (1930) the cartilage cessory cartilages since it is not a part of the cartilagineous in the external ear (external auditory meatus and pinna) of the rat primordium of the body skeleton as is most hyaline cartilage can be defined as: a) cellular or parenchymatous, [jecause of the (Schaffer, 1930). -
Clinical Outcomes of Elastin Fibre Defects
ytology & f C H i o s l t a o n l o r g u y o Hassan et al., J Cytol Histol 2013, 4:1 J Journal of Cytology & Histology DOI: 10.4172/2157-7099.1000166 ISSN: 2157-7099 CommentaryResearch Article OpenOpen Access Access Clinical Outcomes of Elastin Fibre Defects Ashfaq Ul Hassan1*, Ghulam Hassan2, Zahida Rasool3 and Shabinul Hassan3 1Anatomy Department, SKIMS Medical College, Bemina, Srinagar, Kashmir, India 2Department of Anatomy, Al Qassim University, Saudi Arabia 3Islamic University of Science and Technology, Kashmir, India Abstract Elastic fibres are a major class of extracellular matrix fibres that are abundant in dynamic connective tissues such as arteries, lungs, skin and ligaments. Their structural role is to endow tissues with elastic recoil and resilience. They also act as an important adhesion template for cells, and they regulate growth factor availability. Mutations in major structural components of elastic fibres, especially elastin, fibrillins and fibulin-5, cause severe, often life-threatening, heritable connective tissue diseases such as Marfan syndrome, Menkes Syndrome, Cutis laxa. Elastic-fibre function is also frequently compromised in damaged or aged elastic tissues. The ability to regenerate or engineer elastic fibres and tissues remains a significant challenge, requiring improved understanding of the molecular and cellular basis of elastic-fibre biology and pathology. The aim of the article is to present in brief the structural details of elastin fibres, the defects and pleiotrophic effects as a result of damage and various clinical conditions associated with defects in elastin fibres ranging from rare pediatric syndromes to common entities like hypertension. -
Determination of the Molecular Basis of Marfan Syndrome: a Growth Industry
Determination of the molecular basis of Marfan syndrome: a growth industry Peter H. Byers J Clin Invest. 2004;114(2):161-163. https://doi.org/10.1172/JCI22399. Commentary Although it has been known for more than a decade that Marfan syndrome — a dominantly inherited connective tissue disorder characterized by tall stature, arachnodactyly, lens subluxation, and a high risk of aortic aneurysm and dissection — results from mutations in the FBN1 gene, which encodes fibrillin-1, the precise mechanism by which the pleiotropic phenotype is produced has been unclear. A report in this issue now proposes that loss of fibrillin-1 protein by any of several mechanisms and the subsequent effect on the pool of TGF-β may be more relevant in the development of Marfan syndrome than mechanisms previously proposed in a dominant-negative disease model. The model proposed in this issue demonstrates several strategies for clinical intervention. Find the latest version: https://jci.me/22399/pdf Commentaries Determination of the molecular basis of Marfan syndrome: a growth industry Peter H. Byers Departments of Pathology and Medicine, University of Washington, Seattle, Washington, USA. Although it has been known for more than a decade that Marfan syndrome In this issue of the JCI, Judge and colleagues — a dominantly inherited connective tissue disorder characterized by tall test the hypothesis that haploinsufficiency is stature, arachnodactyly, lens subluxation, and a high risk of aortic aneurysm the major effect rather than the dominant- and dissection — results from mutations in the FBN1 gene, which encodes negative effect expected with multimeric pro- fibrillin-1, the precise mechanism by which the pleiotropic phenotype is teins (14). -
Fibrillin and Elastin Expression in Skin Regenerating from Cultured
Fibrillin and Elastin Expression in Skin Regenerating Frotn Cultured Keratinocyte Autografts: Morphogenesis of Microfibrils Begins At the Dertno-epidertnal Junction and Precedes Elastic Fiber Fortnation Michael Raghunath, Thomas Bachi, * Martin Meuli, -r Stefan Altermatt, t l:tita Gobet, t Leena Bruckner-Tuderman,:j: and Beat SteinmalID tDivision of Metabolj c and Molecular Disease and Pedi atric Bum Ccnter of the Ulljvcrsity Children's Hospital Ztirich, "' Electron microscopic Central Laboratory of the University of Ziirich, Switzerland; and t Departlllcnt of Dermatology at the University of Mtinstcr, F.R.G. The tetnporo-spatial expression of fibrillin and elas horizontailly undulating microfibrils of the neoder tin in skin regenerating frotn autologous keratino mis which had developed independently. Elastin was cyte grafts was studied in three burned children. Skin first identified in the deeper neodermis 1 month after biopsies taken between 5 days and 17 months after grafting as granular aggregates and 4 months after grafting were investigated by conventional immuno grafting on fibrillar structures and surrounding cap fluorescence, confocal laser scanning, and electron illaries of the upper neodermis. Association of elastin microscopy. Fibrillin, the major component of 10- with microfibrils in the papillary dermis was not 12-nm microfibrils, appeared 5 days after grafting in detectable before month 17. Our findings suggest a band-like fashion similar to collagen VII at the that the cutaneous microfibrillar apparatus develops prospective basctnent membrane, and then formed simultaneously at both the dermo-epidermal junc the characteristic tnicrofibrillar candelabra at the tion and the reticular dermis and is a prerequisite for dermo-epidermal junction by fusion of several fine elastic fiber formation. -
The Distribution of Elastin in Developing and Adult Rat Organs Using Immunocytochemical Techniques
J. Anat. (1989), 165, pp. 225-236 225 With 6 figures Printed in Great Britain The distribution of elastin in developing and adult rat organs using immunocytochemical techniques COLIN FARQUHARSON AND SIMON P. ROBINS Rowett Research Institute, Biochemistry Division, Bucksburn, Aberdeen, Scotland (Accepted 20 December 1988) INTRODUCTION Elastin is the major protein of elastic system fibres, the principal connective tissue components responsible for the elasticity of a number of compliant organs such as aorta and skin. The elastic system fibres include elastic fibres, elaunin fibres and oxytalan fibres (Cotta-Pereira, Rodrigo & Bittencourt-Sampio, 1976). The elastic fibre consists of two morphologically distinct components (Ross & Bornstein, 1969): large amounts of an amorphous elastin core surrounded by a few microfibrils which are glycoprotein in nature (Sear, Grant & Jackson, 1981). Elaunin fibres also contain both components but are composed predominantly of microfibrils with little amorphous elastin, whereas oxytalan fibres are, exclusively, bundles of microfibrils (Cotta-Pereira et al. 1976). Oxytalan and elaunin fibres appear to be precursors of the mature elastic fibre (Gawlik, 1965). By light microscopy, demonstration of elastin has relied on characteristic staining reactions, chiefly with orcein, aldehyde-fuchsin and resorcin-fuchsin based stains. These classical stains do not however provide unequivocal identification of elastin as their specificity is now in doubt (Puchtler, Meloan & Pollard, 1976; Fakan & Saskova, 1982), thus limiting the use of these tinctorial dyes. Recently, there have been a number of reports using immunocytochemical detection of elastin by light microscopy (McCullagh, Barnard, Davies & Partridge, 1980; Barnard et al. 1982a; Barnard, Davies & Young, 1982 b; Fukuda, Ferrans & Crystal, 1983; Akita, Barrach & Merker, 1986). -
Connective Tissue and Mesenchymal Tissue
Connective tissue & mesenchymal tissue Prepared by: Ms. BR Tsauses Anatomical Pathology 2A (ANP611S) April 2020 Learning objectives • Understand connective and mesenchymal tissues in order to describe and apply appropriate staining techniques in Histology. Pre-learning Quiz • Please take the pre-learning quiz before proceeding with the presentation. Introduction • Connective tissue (CT) is of the four tissue types • Derived fom latin word connectere meaning to bind. • Is to connect together and provide support Introduction cont… • During embryonic development: ectoderm + endoderm = mesoderm • This germ layer is known as mesenchymal • Mesos means middle • Enchyma means infusion Connective tissue CT are divided into: 1. Connective tissue proper (dense, areolar, regular,adipose regular and reticular 2. Cartilage (hyaline elastic, fibrocartilage) 3. Bone( spongy or cancellous and dense or cortical) 4. Blood 5. Blood-forming (hematopoietic) Connective tissue cell types • Fibroblast • Mast cells • Histocytes • Adipose cells • Reticulor cells • Osteoblast and osteocytes • Chondroblast and chondrocytes • Blood cells and blood forming cells Intercellular substance • Intercellular substance (ICS) is composed of both amorphous(sulfated and non sulfated mucopolysaccharides) and formed elements (collagen, reticular fibers and elastic fibers) • The nature of these substance varies according its function (hard or dense or soft.) • Classified into: formed or fibrous type : gel or amorphous type Formed or fibrous intercellular substances Collagenenic fibers • Most common ICS found in large quantities in most sites • Appear as individual fibers as in loose areolar tissues e. g tendon • Collagenic fibers do not branch • Collagen types: Type (i) up to (vi) Reticular fibers • Provide bulk of supporting network of more cellular organs e. g spleen, lymph nodes, liver. -
RIN2 Deficiency Results in Macrocephaly, Alopecia, Cutis Laxa
REPORT RIN2 Deficiency Results in Macrocephaly, Alopecia, Cutis Laxa, and Scoliosis: MACS Syndrome Lina Basel-Vanagaite,1,2,14 Ofer Sarig,4,14 Dov Hershkovitz,6,7 Dana Fuchs-Telem,2,4 Debora Rapaport,3 Andrea Gat,5 Gila Isman,4 Idit Shirazi,4 Mordechai Shohat,1,2 Claes D. Enk,10 Efrat Birk,2 Ju¨rgen Kohlhase,11 Uta Matysiak-Scholze,11 Idit Maya,1 Carlos Knopf,9 Anette Peffekoven,12 Hans-Christian Hennies,12 Reuven Bergman,8 Mia Horowitz,3 Akemi Ishida-Yamamoto,13 and Eli Sprecher2,4,6,* Inherited disorders of elastic tissue represent a complex and heterogeneous group of diseases, characterized often by sagging skin and occasionally by life-threatening visceral complications. In the present study, we report on an autosomal-recessive disorder that we have termed MACS syndrome (macrocephaly, alopecia, cutis laxa, and scoliosis). The disorder was mapped to chromosome 20p11.21-p11.23, and a homozygous frameshift mutation in RIN2 was found to segregate with the disease phenotype in a large consan- guineous kindred. The mutation identified results in decreased expression of RIN2, a ubiquitously expressed protein that interacts with Rab5 and is involved in the regulation of endocytic trafficking. RIN2 deficiency was found to be associated with paucity of dermal micro- fibrils and deficiency of fibulin-5, which may underlie the abnormal skin phenotype displayed by the patients. Disorders of elastic tissue often share common phenotypic shown to result in decreased secretion of elastin.9,10 In features, including redundant skin, hyperlaxity of joints, addition, -
Tumours of the Anterior Uvea. III. Oxytalan Fibres in the Differential Diagnosis of Leiomyoma and Malignant Melanoma of the Iris
Br J Ophthalmol: first published as 10.1136/bjo.64.11.867 on 1 November 1980. Downloaded from British Journal of Ophthalmology, 1980, 64, 867-874 Tumours of the anterior uvea. III. Oxytalan fibres in the differential diagnosis of leiomyoma and malignant melanoma of the iris M. S. NOOR SUNBA, A. H. S. RAHI, A. GARNER, R. A. ALEXANDER, AND G. MORGAN From the Department of Pathology, Institute of Ophthalmology, Judd Street, London SUMMARY The diagnostic potential of oxytalan fibre demonstration in differentiating between leiomyomas and spindle-cell malignant melanomas of the iris was investigated. It was found that oxytalan fibres were abundant in leiomyomata, both between and around the tumour cells, whereas they were found in small numbers only and usually near the iris muscle in malignant melanomata. Their presence and distribution, therefore, appear to offer a satisfactory method of differentiating between these tumours. Since the human choroid and ciliary body normally contain oxytalan fibres, the above findings are not relevant to malignant melanoma of these structures. Naevi and regressing aggregates of iris melanoma cells away from the main tumour mass may similarly be surrounded by misleading amounts of these fibres. Smooth muscle tumours of the iris have their origin the Mallory phosphotungstic acid haematoxylin copyright. in the dilator and sphincter muscles. Occasionally, stain, the Masson trichrome stain, and the gold however, they are found at other sites such as the impregnation technique is the most important anterior surface of the iris, where smooth muscle is diagnostic criterion. Since myoglial fibrils, which not naturally present.' Leiomyomas of the iris are are composed of contractile proteins, have been less common than malignant melanomata, their demonstrated in tissues other than smooth incidence varying between 4% and 33% of primary muscle,7-10 it is clear that their presence cannot be iris tumours.2 5 regarded as a pathognomonic feature of leiomyoma. -
And Suggest Distinct Pathogenetic Mechanisms Takeshi Aoyama,* Uta Francke,4911 Harry C
Quantitative Differences in Biosynthesis and Extracellular Deposition of Fibrillin in Cultured Fibroblasts Distinguish Five Groups of Marfan Syndrome Patients and Suggest Distinct Pathogenetic Mechanisms Takeshi Aoyama,* Uta Francke,4911 Harry C. Dietz,l and Heinz Furthmayr* *Departments of Pathology, tGenetics, §Pediatrics, I1Howard Hughes Medical Institute, Stanford University, Stanford, California 94305; and IDepartment of Pediatrics, The Johns Hopkins University School of Medicine, Baltimore, Maryland 21205 Abstract musculoskeletal, and cardiovascular systems ( 1). Several years ago, Sakai et al. (2) isolated fibrillin from the culture medium Pulse-chase studies of [3S]cysteine-labeled fibrillin were of dermal fibroblasts and provided substantial evidence for this performed on fibroblast strains from 55 patients with Mar- protein to be the major component of 10-nm microfibrils. Mi- fan syndrome (MFS), including 13 with identified mutations crofibrils are abundant in elastic and non-elastic tissues in or- in the fibrillin-1 gene and 10 controls. Quantitation of the gans that are significantly affected in patients with the Marfan soluble intracellular and insoluble extraceliular fibrillin al- syndrome. A dramatic decrease in the amount of such microfi- lowed discrimination of five groups. Groups I (n = 8) and brils has previously been demonstrated in the skin and in cul- H (n = 19) synthesize reduced amounts of normal-sized tured fibroblasts from such patients (3). fibrillin, while synthesis is normal in groups m (n = 6), Genetic linkage studies with random probes mapped the IV (n = 18), and V (n = 4). When extracellular fibrillin MFS locus to chromosome 15 (4). The fibrillin cDNA was deposition is measured, groups I and III deposit between 35 cloned (5) and mapped to the same site on human chromosome and 70% of control values, groups II and IV < 35%, and 15 by in situ hybridization (6).