Role of matrix vesicles in biomineralization

Golub, Ellis E.

doi:10.1016/j.bbagen.2009.09.006

Cited by 316 publications

(282 citation statements)

References 147 publications

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“…Experimental evidence has pointed to the presence of HA crystals along collagen fibrils in the ECM (Glimcher 2006) and also within the lumen of chondroblastand osteoblast-derived matrix vesicles (MVs) (Anderson et al 2005;Golub 2009;Simão et al 2007Simão et al , 2010b. PP i , derived both from ectoplasmic PC-1/nucleotide pyrophosphatase/ phosphodiesterase-1 (NPP1)-catalyzed production from extracellular nucleoside triphosphates (Terkeltaub 2001) and by intracellular export via the ankylosis protein (ANK) transporter, inhibits matrix mineralization (Ho et al 2000).…”

Section: New Perspectives For Applications Of Proteoliposomesmentioning

confidence: 99%

“…This inhibition is released through the action of TNAP, which hydrolyzes PP i , thus simultaneously removing the inhibitor and providing additional P i for mineral formation Harmey et al 2004). Mineralization is said to proceed in two phases: an initial formation of apatite within MVs, and a subsequent propagation phase in the matrix (Anderson et al 2005;Golub 2009). According to this mechanism, Ca 2+ enters MVs via an annexin channel and phosphate enters via a type III Na + -dependent phosphate transporter (PiT), and possibly others, to form apatite within MVs (Arispe et al 1996;Wu et al 2003).…”

Section: New Perspectives For Applications Of Proteoliposomesmentioning

confidence: 99%

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Proteoliposomes in nanobiotechnology

et al. 2012

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Proteoliposomes are systems that mimic lipid membranes (liposomes) to which a protein has been incorporated or inserted. During the last decade, these systems have gained prominence as tools for biophysical studies on lipid-protein interactions as well as for their biotechnological applications. Proteoliposomes have a major advantage when compared with natural membrane systems, since they can be obtained with a smaller number of lipidic (and protein) components, facilitating the design and interpretation of certain experiments. However, they have the disadvantage of requiring methodological standardization for incorporation of each specific protein, and the need to verify that the reconstitution procedure has yielded the correct orientation of the protein in the proteoliposome system with recovery of its functional activity. In this review, we chose two proteins under study in our laboratory to exemplify the steps necessary for the standardization of the reconstitution of membrane proteins in liposome systems: (1) alkaline phosphatase, a protein with a glycosylphosphatidylinositol anchor, and (2) Na,K-ATPase, an integral membrane protein. In these examples, we focus on the production of the specific proteoliposomes, as well as on their biochemical and biophysical characterization, with emphasis on studies of lipid-protein interactions. We conclude the chapter by highlighting current prospects of this technology for biotechnological applications, including the construction of nanosensors and of a multiprotein nanovesicular biomimetic to study the processes of initiation of skeletal mineralization.

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Section: New Perspectives For Applications Of Proteoliposomesmentioning

confidence: 99%

Section: New Perspectives For Applications Of Proteoliposomesmentioning

confidence: 99%

Proteoliposomes in nanobiotechnology

et al. 2012

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“…Various experiments have revealed the presence of HA crystals both inside and outside collagen fibrils in the ECM (McNally et al 2012) and also within the lumen of matrix vesicles (MVs) (Ali et al 1970;Anderson 1969;Bonucci 1970). MVs are extracellular vesicles with a diameter ranging from approximately 100 to 300 nm (Anderson 2003;Anderson et al 2010;Cui et al 2016;Golub 2009;Wuthier and Lipscomb 2011) which harbor the biochemical machinery needed to establish the appropriate inorganic pyrophosphate (PP i ) to inorganic phosphate (P i ) ratio (Ciancaglini et al 2006Harmey et al 2004;Hessle et al 2002;Johnson et al 2000;Roberts et al 2007;Yadav et al 2011;Zhou et al 2012) required to initiate the synthesis of apatitic mineral (Bechkoff et al 2008;Thouverey et al 2009;Wu et al 1997), which will subsequently be propagated onto the collagenous ECM. These vesicles are released from the hypertrophic chondrocytes and mature osteoblasts, the cells responsible for endochondral and membranous ossification.…”

Section: Mineralization Process and The Biogenesis Of Matrix Vesiclesmentioning

confidence: 99%

“…These vesicles are released from the hypertrophic chondrocytes and mature osteoblasts, the cells responsible for endochondral and membranous ossification. Hypertrophic chondrocyte differentiation is related to high tissue nonspecific alkaline phosphatase (TNAP) activity and to the synthesis and secretion of type X and II collagens by proliferating and pre-hypertrophic chondrocytes (Golub 2009;McKee et al 2013).…”

Section: Mineralization Process and The Biogenesis Of Matrix Vesiclesmentioning

confidence: 99%

Biophysical aspects of biomineralization

et al. 2017

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During the process of endochondral bone formation, chondrocytes and osteoblasts mineralize their extracellular matrix (ECM) by promoting the synthesis of hydroxyapatite (HA) seed crystals in the sheltered interior of membranelimited matrix vesicles (MVs). Several lipid and proteins present in the membrane of the MVs mediate the interactions of MVs with the ECM and regulate the initial mineral deposition and posterior propagation. Among the proteins of MV membranes, ion transporters control the availability of phosphate and calcium needed for initial HA deposition. Phosphatases (orphan phosphatase 1, ectonucleotide pyrophosphatase/ phosphodiesterase 1 and tissue-nonspecific alkaline phosphatase) play a crucial role in controlling the inorganic pyrophosphate/inorganic phosphate ratio that allows MVmediated initiation of mineralization. The lipidic microenvironment can help in the nucleation process of first crystals and also plays a crucial physiological role in the function of MVassociated enzymes and transporters (type III sodiumdependent phosphate transporters, annexins and Na + /K + ATPase). The whole process is mediated and regulated by the action of several molecules and steps, which make the process complex and highly regulated. Liposomes and proteoliposomes, as models of biological membranes, facilitate the understanding of lipid-protein interactions with emphasis on the properties of physicochemical and biochemical processes. In this review, we discuss the use of proteoliposomes as multiple protein carrier systems intended to mimic the various functions of MVs during the initiation and propagation of mineral growth in the course of biomineralization. We focus on studies applying biophysical tools to characterize the biomimetic models in order to gain an understanding of the importance of lipid-protein and lipid-lipid interfaces throughout the process.Keywords Lipid microenvironment . Biomineralization . Matrix vesicles . Liposome . Proteoliposome . Hydroxyapatite Mineralization process and the biogenesis of matrix vesiclesMineralization of cartilage and bone occurs by a series of physicochemical and biochemical processes that together facilitate the deposition of calcium phosphate. The deposited calcium phosphate is subsequently converted into hydroxyapatite (HA) [Ca 10 (PO 4 ) 6 (OH) 2 ] in specific areas of the extracellular matrix (ECM). Various experiments have revealed the presence of HA crystals both inside and outside collagen fibrils in the ECM (McNally et al. 2012) and also within the

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“…Usually, the MVs or MV-like particles are released into the pre-mineralized organic matrix prior to the onset of matrix mineralization, and act as a key constituent in both physiological and pathological mineralization. Current evidences support two possible mechanisms for MVs involving mineralization: first, they modulate the local Pi/Ppi ratio in the mineralizing matrix; secondly, they provide initial mineral nucleation sites for mineralization (4,5).…”

Section: Introductionmentioning

confidence: 99%