Molecular cloning and mRNA tissue distribution of a novel matrix metalloproteinase isolated from porcine enamel organ

Bartlett, John D.; Simmer, James P.; Xue, Jing; Margolis, Henry C.; Moreno, E.C.

doi:10.1016/s0378-1119(96)00525-2

Cited by 202 publications

(167 citation statements)

References 22 publications

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“…During enamel formation almost all of the protein supporting mineral formation is removed, and much research has been devoted to the study of the roles of proteases in this process (Bartlett and Simmer, 1999;Simmer and Hu, 2002). Eventually it was demonstrated that two proteases are involved: matrix metalloproteinase 20 (Bartlett et al, 1996) and kallikrein 4 . These enzymes undoubtedly play critical roles in dental enamel formation, as mutations in MMP20 and KLK4 cause autosomal recessive amelogenesis imperfecta (Hart et al, 2004;Kim et al, 2005;Ozdemir et al, 2005;Papagerakis et al, 2008).…”

Section: Dental Enamelmentioning

confidence: 99%

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Functions of KLK4 and MMP-20 in dental enamel formation

Papagerakis²,

Yamakoshi

et al. 2008

BCHM

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219

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Two proteases are secreted into the enamel matrix of developing teeth. The early protease is enamelysin . The late protease is kallikrein 4 (KLK4). Mutations in MMP20 and KLK4 both cause autosomal recessive amelogenesis imperfecta, a condition featuring soft, porous enamel containing residual protein. MMP-20 is secreted along with enamel proteins by secretory stage ameloblasts. Enamel protein cleavage products accumulate in the space between the crystal ribbons, helping to support them. MMP-20 steadily cleaves accumulated enamel proteins, so their concentration decreases with depth. Kallikrein 4 is secreted by transition and maturation stage ameloblasts. KLK4 aggressively degrades the retained organic matrix following the termination of enamel protein secretion. The principle functions of MMP-20 and KLK4 in dental enamel formation are to facilitate the orderly replacement of organic matrix with mineral, generating an enamel layer that is harder, less porous, and unstained by retained enamel proteins.

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Section: Dental Enamelmentioning

confidence: 99%

“…Proteases serve vital functions in dental enamel formation and two enzymes, MMP-20 and KLK4, were originally discovered and their cDNAs were initially cloned from developing teeth (Bartlett et al, 1996;. This is a concise review of MMP-20 and KLK4, and the roles they play in dental enamel formation.…”

Section: Introductionmentioning

confidence: 99%

Functions of KLK4 and MMP-20 in dental enamel formation

Papagerakis²,

Yamakoshi

et al. 2008

BCHM

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219

190

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“…Recently, autosomal-dominant hypoplastic Al has been linked to chromosome 4q21, providing the first genomic location for an autosomally inherited Al type (Backman et al, 1994;Forsman et al, 1994). Ameloblastin, a recently discovered enamel protein, is linked to this region, making it a prime candidate gene for this Al type (Krebsbach et al, 1996;MacDougall et al, 1997a (Deutsch et al, 1995;Bartlett et al, 1996;Hu et al, 1997 (Stevens et al, 1996) and Ehlers-Danlos syndrome (Byers, 1994). Determining the genetic defects in patients with Al is also critical to providing appropriate counseling on recurrence risks, since it is currently extremely difficult and often impossible to differentiate between autosomal and X-linked cases and to delineate autosomal-recessive inheritance from new autosomaldominant mutations.…”

Section: Genetic Conditions Affecting Enamelmentioning

confidence: 99%

The Impact of Molecular Genetics on Oral Health Paradigms

Hart

Marazita

Wright

2000

Critical Reviews in Oral Biology & Medicine

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As a result of our increased understanding of the human genome, and the functional interrelationships of gene products with each other and with the environment, it is becoming increasingly evident that many human diseases are influenced by heritable alterations in the structure or function of genes. Significant advances in research methods and newly emerging partnerships between private and public sector interests are creating new possibilities for utilization of genetic information for the diagnosis and treatment of human diseases. The availability and application of genetic information to the understanding of normal and abnormal human growth and development are fundamentally changing the way we approach the study of human diseases. As a result, the issues and principles of medical genetics are coming to bear across all disciplines of health care. In this review, we discuss some of the potential applications of human molecular genetics for the diagnosis and treatment of oral diseases. This discussion is presented in the context of the ongoing technological advances and conceptual changes that are occurring in the field of medical genetics. To realize the promise of this new molecular genetics, we must be prepared to foresee the possibilities and to incorporate these newly emergent technologies into the evolving discipline of dentistry. By using examples of human conditions, we illustrate the broad application of this emerging technology to the study of simple as well as complex genetic diseases. Throughout this paper, we will use the following terminology: Penetrance In a population, defined as the proportion of individuals posessing a disease-causing genotype who express the disease phenotype. When this proportion is less than 100%, the disease is said to have reduced or incomplete penetrance. Polymerase chain reaction (PCR)-A technique for amplifying a large number of copies of a specific DNA sequence flanked by two oligonucleotide primers. The DNA is alternately heated and cooled in the presence of DNA polymerase and free nucleotides, so that the specified DNA segment is denatured, hybridized with primers, and extended by DNA polymerase. MIM-Mendelian Inheritance in Man catalogue number from V. McKusick's Mendelian Inheritance in man (OMIM, 1998).

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“…During the secretory stage, ameloblasts secrete enamel proteins such as amelogenin (the most abundant enamel matrix protein; Eastoe, 1979), ameloblastin (Krebsbach et al, 1996) and enamelin (Hu et al, 1997) into the enamel matrix. This extracellular matrix undergoes enzymatic modification by enamelysin and kallikrein 4 (KLK4) in the transition and maturation stages, which results in the formation of a mature enamel that is mainly composed of hydroxyapatite crystallites and a minor amount of residual proteins (Bartlett et al, 1996;Nanci and Smith, 2000). Mutations in amelogenin, enamelin, MMP-20 and KLK4 genes all cause human hereditary amelogenesis imperfecta (AI), in which both enamel formation and its mineralization are affected (Hu et al, 2007).…”

Section: Introductionmentioning

confidence: 99%

Critical role for αvβ6 integrin in enamel biomineralization

Mohazab

Koivisto

Jiang

et al. 2012

Journal of Cell Science

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SummaryTooth enamel has the highest degree of biomineralization of all vertebrate hard tissues. During the secretory stage of enamel formation, ameloblasts deposit an extracellular matrix that is in direct contact with the ameloblast plasma membrane. Although it is known that integrins mediate cell-matrix adhesion and regulate cell signaling in most cell types, the receptors that regulate ameloblast adhesion and matrix production are not well characterized. We hypothesized that avb6 integrin is expressed in ameloblasts where it regulates biomineralization of enamel. Human and mouse ameloblasts were found to express both b6 integrin mRNA and protein. The maxillary incisors of Itgb6 2/2 mice lacked yellow pigment and their mandibular incisors appeared chalky and rounded. Molars of Itgb6 2/2 mice showed signs of reduced mineralization and severe attrition. The mineral-to-protein ratio in the incisors was significantly reduced in Itgb6 2/2 enamel, mimicking hypomineralized amelogenesis imperfecta. Interestingly, amelogenin-rich extracellular matrix abnormally accumulated between the ameloblast layer of Itgb6 2/2 mouse incisors and the forming enamel surface, and also between ameloblasts. This accumulation was related to increased synthesis of amelogenin, rather than to reduced removal of the matrix proteins. This was confirmed in cultured ameloblast-like cells, in which avb6 integrin was not an endocytosis receptor for amelogenins, although it participated in cell adhesion on this matrix indirectly via endogenously produced matrix proteins. In summary, integrin avb6 is expressed by ameloblasts and it plays a crucial role in regulating amelogenin deposition and/or turnover and subsequent enamel biomineralization.

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Molecular cloning and mRNA tissue distribution of a novel matrix metalloproteinase isolated from porcine enamel organ

Cited by 202 publications

References 22 publications

Functions of KLK4 and MMP-20 in dental enamel formation

Functions of KLK4 and MMP-20 in dental enamel formation

The Impact of Molecular Genetics on Oral Health Paradigms

Critical role for αvβ6 integrin in enamel biomineralization

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