Structural phosphate: Difference between revisions
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Mineralization in the extracellular matrix starting with hydroxyapatite deposition into a collagenous scaffolding of cartilage, cementum, dentin and bone is initially regulated locally by calcium, orthophosphate, and pyrophosphate ion concentrations. | |||
Although cuboid calcium phosphate crystals are absent in young articular cartilage, they are sometimes present in old normal articular cartilage occasionally adjacent to larger areas of pyrophosphate crystals.<ref name=Ali>{{ cite journal |author=Ali SY, Griffiths S |title=Formation of calcium phosphate crystals in normal and osteoarthritic cartilage |journal=Ann Rheum Dis. |month=Aug |year=1983 |volume=42 |issue=Suppl 1 |pages=45-8 |pmid= 6615026 }}</ref> | Although cuboid calcium phosphate crystals are absent in young articular cartilage, they are sometimes present in old normal articular cartilage occasionally adjacent to larger areas of pyrophosphate crystals.<ref name=Ali>{{ cite journal |author=Ali SY, Griffiths S |title=Formation of calcium phosphate crystals in normal and osteoarthritic cartilage |journal=Ann Rheum Dis. |month=Aug |year=1983 |volume=42 |issue=Suppl 1 |pages=45-8 |pmid= 6615026 }}</ref> | ||
Revision as of 05:02, 11 May 2009
Editor-In-Chief: Henry A. Hoff
Overview
Inside a cell, phosphate may be structural to a nucleic acid such as DNA and RNA or phospholipid. Outside the cell, phosphate may be dissolved in extracellular fluid (ECF) or form structures such as bone and teeth. Bringing phosphate in any form into the cell from a phosphate containing structure or for such a structure and when needed transporting phosphate out of the cell perhaps to a structure is a necessary activity of phosphate homeostasis for that cell.
Introduction
Inorganic phosphate (Pi) (structural phosphate) behaves as a serine phosphate and is not the same as the enzyme-bound phosphate (catalytic phosphate) derived from ATP during a catalytic reaction.[1] The catalytic phosphate in a nucleotide is usually the phosphate farthest from the nucleoside. The structural phosphate becomes the hydrolyzed nucleotide after the catalysis that associates with the binding of the polymer. The structural phosphate is a part of each polymer whether it is a microfilament, microtubule, phospholipid, or nucleic acid. Inorganic phosphates such as Pi and PPi can be precipitated with divalent cations like Ca2+, Mg2+, or others, e.g. Mn2+, to form a variety of tissue and mineral composites: cartilage, teeth, and bone. These in turn eventually become localized to the natural environment and form phosphorites.
Catalytic phosphate
Inorganic phosphate (Pi) (structural phosphate) behaves as a serine phosphate and is not the same as the enzyme-bound phosphate (catalytic phosphate) derived from ATP during a lyase reaction of EC 4.1.3.8.[1] Evidence indicates that EC 4.1.3.8 contains one structural phosphate for each catalytic phosphate, which does not affect its catalytic activity.[1] The γ phosphate of ATP is the catalytic phosphate. EC 4.1.3.8 ATP citrate lyase contains acid-labile, catalytic phosphate after the enzyme is reacted with ATP and Mg2+, whereas the structural phosphate is acid-stable, base-labile.[2] There are 2 mol of acid-labile catalytic phosphate and 2 mol of base-labile structural phosphate per tetramer. The pH 7.5 buffer contained concentrations of ADP, Pi, and free Mg2+ similar to those found in vivo.[2] Glucagon induces an incorporation of acid-stable phosphate into ATP citrate lyase without a concomitant change in enzyme activity.[2]
Intracellular structural phosphate
In the mathematical modeling of cell growth and phosphatase biosynthesis it is necessary to determine the intracellular concentration of structural phosphate.[3]
Nucleotides
Analysis of the phosphate moiety present in mononucleotides (NMP) can allow the identification of structural phosphate binding motifs.[4]
When nucleotide hydrolysis is coupled to the polymerization process, the two ends of the polymer behave differently, and the critical concentration required for assembly at one end is different from that required for the opposite end. However, NTP hydrolysis is usually associated but not directly coupled with polymerization. When there are NTP-bound subunits at the ends, the polymer is stable and continues to grow slowly. When at the polymer ends there are subunits containing NDP, the polymer is in a shrinking phase, depolymerizes rapidly and completely, and much faster at lower mer concentrations.
Microfilaments
During the assembly of actin into microfilaments, actin-ATP becomes actin ADP upon polymerization.
Microtubules
Pi, BeF3 or AIF4, structural phosphate analogs, have a stabilizing effect on microtubules containing GDP tubulin.[5] The structural phosphate of microtubules is the GDP in the interior of the polymer.
Phospholipid
Phospholipids are a major component of the plasma membrane and organelle membranes. In normal cell plasma membranes, phospholipids are asymmetrically distributed: phosphatidylcholine (PC) and sphingomyelin (SM) predominantly in the exoplasmic leaflet and phosphatidylserine (PS) and phosphatidylethanolamine (PE) in the cytoplasmic leaflet. All phospholipids in eukaryotic plasma membranes undergo a slow passive transbilayer movement.[6] Half-times of redistribution are 3.6 min for PS.[6] Both PC and SM have higher diffusion rates probably indicative of endocytosis.
A typical molecule of PC, SM, PS, or PE contains one monophosphate group.
Nucleic acid
Phosphate is a component of DNA and RNA. Most of the structural phosphate in nucleic acids is in the phospho-diester linkage.[7]
Ribonucleic acid (RNA)
The variety and type of RNA is extensive. Each has to be transcribed from the applicable portion of DNA in the euchromatin. The unfolded structure of euchromatin allows gene regulatory proteins and RNA polymerase (RNAP) complexes to bind to the DNA sequence, which can then initiate the transcription process. Control of the process of gene transcription affects patterns of gene expression and thereby allows a cell to adapt to a changing environment, perform specialized roles within an organism, and maintain basic metabolic processes necessary for survival. RNAP can initiate transcription at specific DNA sequences known as promoters. It then produces an RNA chain which is complementary to the template DNA strand. The process of adding nucleotides to the RNA strand is known as elongation.
| Type | Abbr. | Function | Distribution | Ref. |
|---|---|---|---|---|
| Messenger RNA | mRNA | Codes for protein | All cells | |
| Ribosomal RNA | rRNA | Translation | All cells | |
| Signal recognition particle RNA | 7SL RNA or SRP RNA | Membrane integration / mRNA tagging for export | All organisms | [8] |
| Transfer RNA | tRNA | Translation | All cells | |
| Transfer-messenger RNA | tmRNA | Rescuing stalled ribosomes Terminating translation | Bacteria | [9] |
| Type | Abbr. | Function | Distribution | Ref. |
|---|---|---|---|---|
| Small nuclear RNA | snRNA | Splicing and other functions | Eukaryotes and archaea | [10] |
| Small nucleolar RNA | snoRNA | Nucleotide modification of RNAs RNA editing | Eukaryotes and archaea | [11] |
| SmY RNA | SmY | mRNA trans-splicing | Nematodes | [12] |
| Small Cajal body-specific RNA | scaRNA | Type of snoRNA; Nucleotide modification of RNAs | ||
| Guide RNA | gRNA | mRNA nucleotide modification / RNA editing | Kinetoplastid mitochondria | [13] |
| Ribonuclease P | RNase P | tRNA maturation | All organisms | [14] |
| Ribonuclease MRP | RNase MRP | rRNA maturation, DNA replication | Eukaryotes | [15] |
| Y RNA | RNA processing, DNA replication | Animals | [16] | |
| Telomerase RNA | Telomere synthesis | Most eukaryotes | [17] | |
| Ribozyme | Catalysis | All cells | ||
| Transposon | Self-propagating | All cells |
| Type | Abbr. | Function | Distribution | Ref. |
|---|---|---|---|---|
| Antisense RNA | aRNA | Transcriptional attenuation / mRNA degradation / mRNA stabilisation / Translation block Gene regulation | All organisms | [18][19] |
| Cis-natural antisense transcript | Gene regulation | |||
| CRISPR RNA | crRNA | Resistance to parasites, probably by targeting their DNA | Bacteria and archaea | [20] |
| Long noncoding RNA | Long ncRNA | Various | Eukaryotes | |
| MicroRNA | miRNA | Gene regulation | Most eukaryotes | [21] |
| Piwi-interacting RNA | piRNA | Transposon defense Gene regulation | Animal germline cells | [22][23] |
| Small interfering RNA | siRNA | Gene regulation | Most eukaryotes | [24] |
| Trans-acting siRNA | tasiRNA | Gene regulation | Land plants | [25] |
| Repeat associated siRNA | rasiRNA | Type of piRNA; transposon defense | Drosophila | [26] |
Enstructuring Pi into any RNA is usually not reacted directly with ribose for RNA, deoxyribose present in DNA, purines, or pyrimidines. Although DNA records the sequence of nucleobases that are connected by ribose to Pi, the transcription process chosen by probably all life on Earth requires triphosphate nucleotides (NTPs).
For example, consider making a mRNA for a particular protein from the point of view of phosphate enstructuring. As of 2008 dystrophin has the longest gene known, at locus Xp21.2. The primary transcript measures 2.4 megabases (thus the gene comprises 0.008% of the human genome), and takes 16 hours to transcribe. The 79 exons[27] code for a protein of over 3500 amino acid (aa) residues. It is human GeneID: 1756.[28] Isoform Dp427c has 3677 aa[29] which are specified by 3677 codons of 3 nucleotides each. That's 11,031 NMPs with one Pi each.
But the gene portion that is transcribed also contains a 5' cap requiring one GTP, a 5' UTR, 78 introns, and a 3' UTR or as mentioned 2.4 Mb of one Pi each. Per the apparently available phosphate reserve in a cell or intracellular phosphate of about 10-3 Pi (1 molecule of Pi per 1000 other molecules, such as water) at any particular location and a rate of about 42 NTPs per second to transcribe this mRNA, some form of intranuclear transport other than diffusion is needed.
As indicated in phosphate reserves each ATP is recycled about once every minute on average. This may also be true for CTP, GTP, and UTP. That is 0.07 NTPs per second are available to transcribe on average.
Cartilage
Mineralization in the extracellular matrix starting with hydroxyapatite deposition into a collagenous scaffolding of cartilage, cementum, dentin and bone is initially regulated locally by calcium, orthophosphate, and pyrophosphate ion concentrations.
Although cuboid calcium phosphate crystals are absent in young articular cartilage, they are sometimes present in old normal articular cartilage occasionally adjacent to larger areas of pyrophosphate crystals.[30]
Endochondrial ossification of cartilage development ultimately leads to mineralization of the extracellular matrix.[31] Metabolism of Ca2+ and Pi by cartilage growth plate chondrocytes, involved in matrix vesicle formation, clearly are integral features of endochondrial calcification.[31] This calcification is apparently due to the diffusion barrier and avascularity progressing from the zone of proliferation to the zone of hypertrophy of the cartilage growth plate chondrocytes environment.[31]
Teeth
Hydroxyapatite, which is a crystalline calcium phosphate is the primary mineral of enamel.[32]
By weight, seventy percent of dentin consists of the mineral, hydroxylapatite, twenty percent is organic material, and ten percent is water.[33]
Cementum is a specialized bony substance covering the root of a tooth, composed of approximately 45% inorganic material (mainly hydroxyapatite), 33% organic material (mainly collagen) and 22% water.
Bone
During bone resorption high levels of phosphate are released into the ECF as osteoclasts tunnel into mineralized bone, breaking it down and releasing phosphate, that results in a transfer of phosphate from bone fluid to the blood. During childhood, bone formation exceeds resorption, but as the aging process occurs, resorption exceeds formation.
Transphosphorylation between nucleotides and hydroxyapatite (HA) results in a pyrophosphate on HA that is distinctive from pyrophosphate absorbed onto HA from solution. This may be due to a different orientation of the pyrophosphate on the surface depending on the origin of the pyrophosphate.[34]
Sedimentary phosphorites
Phosphogenesis under palaeoceanographic conditions that were different from modern phosphorite depositional systems occurred across a broad range of palaeoenvironments in the shallow and broad epicontinental Phosphoria Sea.[35] These conditions were revealed by oxygen isotope analyses of the structural phosphate in sedimentary phosphorites of the Upper Permian Phosphoria Formation.[35]
References
- ↑ 1.0 1.1 1.2 Linn TC, Srere PA (1979). "Identification of ATP citrate lyase as a phosphoprotein". J Biol Chem. 254 (5): 1691–8. PMID 762167. Unknown parameter
|month=ignored (help) - ↑ 2.0 2.1 2.2 Janski AM, Srere PA, Cornell NW, Veech RL (1979). "Phosphorylation of ATP Citrate Lyase in Response to Glucagon". J Biol Chem. 254 (19): 9365–8. PMID 489538. Unknown parameter
|month=ignored (help) - ↑ Toda K, Yabe I (2004). "Mathematical model of cell growth and phosphatase biosynthesis in Saccharomyces carlsbergensis under phosphate limitation". Biotech Bioeng. 21 (3): 487–502. doi:10.1002/bit.260210310. Unknown parameter
|month=ignored (help) - ↑ Babor M, Soboleva V, Edelman M (2002). "Conserved Positions for Ribose Recognition: Importance of Water Bridging Interactions Among ATP, ADP and FAD-protein Complexes". J Mol Biol. 323 (3): 523–32. doi:10.1016/S0022-2836(02)00975-0. Unknown parameter
|month=ignored (help) - ↑ Avila J (1990). "Microtubule dynamics". FASEB J. 4 (15): 3284–90. PMID 2253844. Unknown parameter
|month=ignored (help) - ↑ 6.0 6.1 Pomorski T, Muller P, Zimmermann B, Burger K, Devaux PF, Herrmann A (1996). "Transbilayer movement of fluorescent and spin-labeled phospholipids in the plasma membrane of human fibroblasts: a quantitative approach". J Cell Sci. 109 (Pt 3): 687–98. PMID 8907713. Unknown parameter
|month=ignored (help) - ↑ Battley EH (1992). "On the enthalpy of formation of Escherichia coli K-12 cells". Biotech Bioeng. 39 (1): 5–12. doi:10.1002/bit.260390103. Unknown parameter
|month=ignored (help) - ↑ Gribaldo S, Brochier-Armanet C (2006). "The origin and evolution of Archaea: a state of the art". Philos Trans R Soc Lond B Biol Sci. 361 (1470): 1007–22. doi:10.1098/rstb.2006.1841. PMID 16754611.
- ↑ Gillet R, Felden B (2001). "Emerging views on tmRNA-mediated protein tagging and ribosome rescue". Molecular Microbiology. 42 (4): 879–85. doi:10.1046/j.1365-2958.2001.02701.x.
- ↑ Thore S, Mayer C, Sauter C, Weeks S, Suck D (2003). "Crystal Structures of the Pyrococcus abyssi Sm Core and Its Complex with RNA". J. Biol. Chem. 278 (2): 1239–47. doi:10.1074/jbc.M207685200.
- ↑ Kiss T (2001). "Small nucleolar RNA-guided post-transcriptional modification of cellular RNAs". The EMBO Journal. 20: 3617–22. doi:10.1093/emboj/20.14.3617.
- ↑ Jones TA, Otto W, Marz M, Eddy SR, Stadler PF (2009). "A survey of nematode SmY RNAs". RNA Biol. 6 (1): 5–8. PMID 19106623.
- ↑ Alfonzo JD, Thiemann O, Simpson L (1997). "The mechanism of U insertion/deletion RNA editing in kinetoplastid mitochondria". Nucleic Acids Research. 25 (19): 3751–59. doi:10.1093/nar/25.19.3751. PMID 9380494.
- ↑ Pannucci JA, Haas ES, Hall TA, Harris JK, Brown JW (1999). "RNase P RNAs from some Archaea are catalytically active". Proc Natl Acad Sci USA. 96 (14): 7803–08. doi:10.1073/pnas.96.14.7803. PMID 10393902.
- ↑ Woodhams MD, Stadler PF, Penny D, Collins LJ (2007). "RNase MRP and the RNA processing cascade in the eukaryotic ancestor". BMC Evolutionary Biology. 7: S13. doi:10.1186/1471-2148-7-S1-S13.
- ↑ Perreault J, Perreault J-P, Boire G (2007). "Ro-associated Y RNAs in metazoans: evolution and diversification". Molecular Biology and Evolution. 24 (8): 1678–89. doi:10.1093/molbev/msm084.
- ↑ Lustig AJ (1999). "Crisis intervention: The role of telomerase". Proc Natl Acad Sci USA. 96 (7): 3339–41. doi:10.1073/pnas.96.7.3339. PMID 10097039.
- ↑ Brantl S (2002). "Antisense-RNA regulation and RNA interference". Biochimica et Biophysica Acta. 1575 (1–3): 15–25. PMID 12020814.
- ↑ Brantl S (2007). "Regulatory mechanisms employed by cis-encoded antisense RNAs". Curr Opin Microbiol. 10 (2): 102–9. doi:10.1016/j.mib.2007.03.012. PMID 17387036.
- ↑ Brouns SJ, Jore MM, Lundgren M; et al. (2008). "Small CRISPR RNAs guide antiviral defense in prokaryotes". Science (New York, N.Y.). 321 (5891): 960–4. doi:10.1126/science.1159689. PMID 18703739. Unknown parameter
|month=ignored (help) - ↑ Lin S-L, Miller JD, Ying S-Y (2006). "Intronic microRNA (miRNA)". Journal of Biomedicine and Biotechnology. 2006: 1–13. doi:10.1155/JBB/2006/26818. PMID 17057362.
- ↑ Horwich MD, Li C Matranga C, Vagin V, Farley G, Wang P, Zamore PD (2007). "The Drosophila RNA methyltransferase, DmHen1, modifies germline piRNAs and single-stranded siRNAs in RISC". Current Biology. 17: 1265–72. doi:10.1016/j.cub.2007.06.030.
- ↑ Ghildiyal M, Zamore PD (2009). "Small silencing RNAs: an expanding universe". Nat. Rev. Genet. 10 (2): 94–108. doi:10.1038/nrg2504. PMID 19148191. Unknown parameter
|month=ignored (help) - ↑ Ahmad K, Henikoff S (2002). "Epigenetic consequences of nucleosome dynamics". Cell. 111 (3): 281–84. doi:10.1016/S0092-8674(02)01081-4.
- ↑ Vazquez F, Vaucheret H (2004). "Endogenous trans-acting siRNAs regulate the accumulation of Arabidopsis mRNAs". Mol. Cell (16): 1–13. PMID 17057362.
- ↑ Desset S, Buchon N, Meignin C, Coiffet M, Vaury C (2008). "In Drosophila melanogaster the COM locus directs the somatic silencing of two retrotransposons through both Piwi-dependent and -independent pathways". PLoS ONE. 3 (2): e1526. doi:10.1371/journal.pone.0001526. PMC 2211404. PMID 18253480.
- ↑ Strachan T, Read AP (1999). Human molecular genetics 2 (2nd ed.). New York, USA: John Wiley & Sons, Inc. ISBN 0471133736.
- ↑ "Entrez Gene: DMD dystrophin".
- ↑ "Entrez Protein - dystrophin Dp427c isoform [Homo spiens]".
- ↑ Ali SY, Griffiths S (1983). "Formation of calcium phosphate crystals in normal and osteoarthritic cartilage". Ann Rheum Dis. 42 (Suppl 1): 45–8. PMID 6615026. Unknown parameter
|month=ignored (help) - ↑ 31.0 31.1 31.2 Wuthier RE (1993). "Involvement of cellular metabolism of calcium and phosphate in calcification of avian growth plate cartilage". J Nutr. 123 (2 Suppl): 301–9. PMID 8429379. Unknown parameter
|month=ignored (help) - ↑ Johnson, Clarke (1998). "Biology of the Human Dentition".
- ↑ Cate, A.R. Ten. (1998). Oral Histology: development, structure, and function (5th ed.). pp. 150–5. ISBN 0-8151-2952-1.
- ↑ Taves DR, Reedy RC (1969). "A structural basis for the transphosphorylation of nucleotides with hydroxyapatite". Calcified Tissue International. 3 (1): 284–92. doi:10.1007/BF02058670. Unknown parameter
|month=ignored (help) - ↑ 35.0 35.1 Hiatt EE, Budd DA (2001). "Sedimentary phosphate formation in warm shallow waters: new insights into the palaeoceanography of the Permian Phosphoria Sea from analysis of phosphate oxygen isotopes". Sedimentary Geol. 145 (1–2): 119–33. doi:10.1016/S0037-0738(01)00127-0. Unknown parameter
|month=ignored (help)