Macromolecules Relevant to Stone Formation

Ryall, Rosemary L.; Cook, Alison F.; Thurgood, Lauren A.; Grover, Phulwinder K.

doi:10.1063/1.2723569

Cited by 5 publications

(4 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…OPN and its acidic peptides strongly inhibit growth on COM {100}, but fluorescently tagged OPN is better overgrown by {100} growth sectors on COD, not COM. ,, Incorporation of the OPN 220–235 peptide becomes stronger with the number of phosphorylated residues . On the other hand, protein G and its mutant as well as prothrombin fragment 1 and HSA are preferentially captured by {121̅} and probably {021} (at some conditions, HSA is incorporated into {010} sectors). ,, These proteins, however, do not significantly inhibit COM. PolyD, Asp-rich peptides, and OPN strongly inhibit growth of COD {100} and {110}.…”

Section: Incorporationmentioning

confidence: 99%

“…83 On the other hand, protein G and its mutant as well as prothrombin fragment 1 and HSA are preferentially captured by {121̅ } and probably {021} (at some conditions, HSA is incorporated into {010} sectors). 418,419,442 These proteins, however, do not significantly inhibit COM. PolyD, Asp-rich peptides, and OPN strongly inhibit growth of COD {100} and {110}.…”

Section: Incorporationmentioning

confidence: 99%

See 1 more Smart Citation

Crystal Growth with Macromolecular Additives

2017

View full text Add to dashboard Cite

Interactions of macromolecules with growing crystalline surfaces play an important role in biomineralization, determine survival of some organisms at low temperatures, and offer a range of potential industrial applications. The current understanding of crystal growth processes in the presence of macromolecules, including peptides and proteins, is reviewed, with a focus on interactions between macromolecules and surfaces of crystalline materials, macromolecule adsorption on different types of crystal surfaces, crystallization kinetics in the presence of macromolecular additives, macromolecule incorporation, and defect generation. Throughout, special attention is paid to the selectivity of macromolecule adsorption on, and incorporation within, crystal surfaces. The special role played by the size and complexity of macromolecules as compared to other crystallization additives is emphasized.

show abstract

Section: Incorporationmentioning

confidence: 99%

Section: Incorporationmentioning

confidence: 99%

Crystal Growth with Macromolecular Additives

2017

View full text Add to dashboard Cite

show abstract

“…Other potential matrix proteins are bikunin, prothrombin fragment 1, and fetuin-A. Ryall and colleagues have reviewed the macromolecules relevant to stone formation in a paper in this proceedings [9]. No evidence of cell injury, inflammation, interstitial fibrosis or intratubular crystalline material was detected in any of the ICSF papillary biopsies.…”

Section: Randall's Plaque Is Unique To Idiopathic Calcium Oxalate Stomentioning

confidence: 99%

Histopathology Predicts the Mechanism of Stone Formation

Evan

2007

AIP Conference Proceedings

View full text Add to dashboard Cite

About 5% of American women and 12% of men will develop a kidney stone at some time in their life and these numbers appear to be on the rise. Despite years of scientific research into the mechanisms of stone formation and growth, limited advances have been made until recently. Randall's original observations and thoughts on the mechanisms for kidney stone formation have been validated for idiopathic calcium oxalate stone formers (ICSF) but not for most other stone forming groups. Our current studies on selected groups of human stone formers using intraoperative papillary biopsies has shown overwhelming evidence for the presence of Randall's plaque in ICSF and that stone formation and growth are exclusively linked to its availability to urinary ions and proteins. Intense investigation of the plaque-stone junction is needed if we are to understand the factors leading to the overgrowth process on exposed regions of plaque. Such information should allow the development of treatment strategies to block stone formation in ICSF patients. Patients who form brushite stones, or who form apatite stones because of distal renal tubular acidosis (dRTA), or patients with calcium oxalate stones due to obesity bypass procedures, or patients with cystinuria, get plugged inner medullary collecting ducts (IMCD) which leads to total destruction of the lining cells and focal sites of interstitial fibrosis. These stone formers have plaque but at levels equal to or below non-stone formers, which would suggest that they form stones by a different mechanism than do ICSF patients.

show abstract

“…Human kidney stones are biologically induced biominerals [5] composed principally of calcium oxalate (CaOx) which, like their salubrious counterparts, always contain a macromolecular matrix distributed throughout the entire structure. Until recently, only 20 or so stone matrix proteins had been identified immunologically or by amino acid sequence analysis [6]. Although > 68 have now been identified in the matrix of CaOx monohydrate (COM) stones [7], it is most unlikely that they all fulfil specific roles in stone formation.…”

Section: Introductionmentioning

confidence: 99%

Face‐specific binding of prothrombin fragment 1 and human serum albumin to inorganic and urinary calcium oxalate monohydrate crystals

2009

Self Cite

View full text Add to dashboard Cite

PTF1 to the top, side and apical faces of the COM crystal. RESULTSPTF1 alone always adsorbed predominantly to the COM apical surfaces, while HSA bound principally to the side faces under inorganic conditions, but to the apical faces in urine. In the presence of each other, both proteins competed for adsorption to the apical faces, with attachment of PTF1 dominating over that of HSA. Modelling showed that urinary PTF1 had equal theoretical bonding potential for all three COM surfaces. CONCLUSIONS(i) Anisotropic inclusion of HSA and PTF1 into urinary and inorganic COM crystals results from their preferential binding to specific COM faces; (ii) the binding preference of HSA differs under inorganic and urinary conditions; (iii) preferential binding of PTF1 to the apical faces of COM is more complex than can be explained by interactions between Gla groups and surface atomic arrays; (iv) future studies of interactions between urinary proteins and stone mineral crystal surfaces should be performed in urine. KEYWORDScalcium oxalate, urolithiasis, intracrystalline protein, prothrombin fragment 1, human serum albumin, biomineralization OBJECTIVETo compare the intracrystalline distributions of prothrombin fragment 1 (PTF1) and human serum albumin (HSA) within inorganic and urinary calcium oxalate (CaOx) monohydrate (COM) crystals and to determine whether binding of PTF1 can be explained by interactions between particular γ -carboxyglutamic (Gla) residues and atomic arrays on individual faces of the COM crystal. MATERIALS AND METHODSCOM crystals were precipitated from inorganic solutions and ultrafiltered urine containing fluorescent HSA or PTF1 at different relative concentrations and examined by fluorescence microscopy. Accelrys Materials Studio and Discovery Studio were used to model the binding of

show abstract

Macromolecules Relevant to Stone Formation

Cited by 5 publications

References 0 publications

Crystal Growth with Macromolecular Additives

Crystal Growth with Macromolecular Additives

Histopathology Predicts the Mechanism of Stone Formation

Face‐specific binding of prothrombin fragment 1 and human serum albumin to inorganic and urinary calcium oxalate monohydrate crystals

Contact Info

Product

Resources

About