Cardiovascular studies on copper deficient swine. XII. Partial purification of a soluble protein resembling elastin

Smith, Don W.; Weissman, Norman; Carnes, William H.

doi:10.1016/0006-291x(68)90476-2

Cited by 108 publications

(5 citation statements)

References 10 publications

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“…In contrast to membraneless organelles, understanding the molecular origins of chain disorder in protein polymers was a more straightforward process. The sequence origins of disorder were readily identified during early work with tropoelastin and resilin, two native proteins that have provided much inspiration for the design of protein polymers. , Tropoelastin, the soluble precursor to elastin, is perhaps the most extensively studied IDP, and characterization of its unstructured regions predates our current understanding of protein disorder by a half-century. − The conformational flexibility of tropoelastin was experimentally verified in the 1960s when the protein was observed to be highly disordered at low temperatures . Subsequent sequencing of both animal and human tropoelastin led to the discovery that elastin is composed of alternating ordered, hydrophilic domains and disordered, hydrophobic domains. ,, Noting the conserved low-sequence complexity tandem repeats, Urry pioneered the development of an even more reductionist version of the disordered hydrophobic domains of tropoelastin, which he termed elastin-like polypeptides (ELPs), that consist of polymers of VPGXG units, a pentapeptide , that recurs in the primary sequence of the hydrophobic, disordered domains of tropoelastin.…”

Section: Disorder and Phase Behavior Are Two Features That Unite Prot...mentioning

confidence: 99%

Convergence of Artificial Protein Polymers and Intrinsically Disordered Proteins

2018

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A flurry of research in recent years has revealed the molecular origins of many membraneless organelles to be the liquid phase separation of intrinsically disordered proteins (IDPs). Consequently, protein disorder has emerged as an important driver of intracellular compartmentalization by providing specialized microenvironments chemically distinct from the surrounding medium. Though the importance of protein disorder and its relationship to intracellular phase behavior are clear, a detailed understanding of how such phase behavior can be predicted and controlled remains elusive. While research in IDPs has largely focused on the implications of structural disorder on cellular function and disease, another field, that of artificial protein polymers, has focused on the de novo design of protein polymers with controllable material properties. A subset of these polymers, specifically those derived from structural proteins such as elastin and resilin, are also disordered sequences that undergo liquid-liquid phase separation. This phase separation has been used in a variety of biomedical applications, and researchers studying these polymers have developed methods to precisely characterize and tune their phase behavior. Despite their disparate origins, both fields are complementary as they study the phase behavior of intrinsically disordered polypeptides. This Perspective hopes to stimulate collaborative efforts by highlighting the similarities between these two fields and by providing examples of how such collaboration could be mutually beneficial.

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Section: Disorder and Phase Behavior Are Two Features That Unite Prot...mentioning

confidence: 99%

Convergence of Artificial Protein Polymers and Intrinsically Disordered Proteins

2018

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“…D-Penicillamine chelates copper and thereby increases copper excretion; furthermore, D-penicillamine is preferentially concentrated in the skin (Ruocco et al 1983) and it could therefore be that there is enhanced copper deficiency locally within the skin. Experimentally-induced copper deficiency produces a decrease in the amount of mature cross-linked elastin (Starcher et al 1964, Smith et al 1968), probably as a consequence of inhibition of the enzyme lysyl oxidase (Lapiere 1973). Miller et al (1965 demonstrated that copper deficiency in pigs led to a decreased production from lysine of desmosine and isodesmosine, the elastin cross-links; furthermore they demonstrated decreased incorporation of`4Clabelled lysine, thereby preventing formation or condensation of the intermediate compounds which normally form elastin cross-links.…”

Section: Case Reportmentioning

confidence: 99%

Pseudoxanthoma Elasticum-Like Skin Changes Induced by Penicillamine

et al. 1984

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“…Elastin is a major component of elastic tissues such as arterial walls, lungs, and skin. Tropoelastin, a precursor protein of elastin1, 2, assembles in a regular manner and is then cross‐linked by lysyl oxidase to form mature insoluble elastin in vivo . The self‐association of the tropoelastin molecule, which is called coacervation, is the most important step in the process of elastin biosynthesis.…”

Section: Introductionmentioning

confidence: 99%

Structural requirements essential for elastin coacervation: favorable spatial arrangements of valine ridges on the three‐dimensional structure of elastin‐derived polypeptide (VPGVG)n

Maeda

Fukumoto

Nose

et al. 2011

Journal of Peptide Science

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The elastin precursor tropoelastin possesses a number of polymeric peptides with repeating 3-9 mer sequences. One of these is the pentapeptide Val-Pro-Gly-Val-Gly (VPGVG) present in almost all animal species, and its polymer (VPGVG)n coacervates just as does tropoelastin. In the present study, in order to explore the structural requirements essential for coacervation, (VPGVG)n and its shortened repeat analogs (VPGV)n, (VPG)n, and (PGVG)n were synthesized and their structural properties were investigated. In our turbidity measurements, (VPGVG)n demonstrated complete reversible coacervation in agreement with previous findings. The Gly(5) -deleted polymer (VPGV)n also achieved self-association, though the onset of self-association occurred at a lower temperature. However, the dissociation of (VPGV)n upon temperature lowering was found to occur in a three-step process; the Val(i) (4) -Val(i+1) (1) structure arising in the VPGV polypeptide appeared to perturb the dissociation. No self-association was observed for (VPG)n or (PGVG)n repeats. Spectroscopic measurements by CD, FT-IR, and (1) H-NMR showed that the (VPGV)n and (VPG)n both assumed ordered structures similar to that of (VPGVG)n. These results demonstrated that VPGVG is a structural element essential to achieving the β-spiral structure required for self-association followed by coacervation, probably due to the ideal spatial arrangement of the hydrophobic Val residues.

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Cardiovascular studies on copper deficient swine. XII. Partial purification of a soluble protein resembling elastin

Cited by 108 publications

References 10 publications

Convergence of Artificial Protein Polymers and Intrinsically Disordered Proteins

Convergence of Artificial Protein Polymers and Intrinsically Disordered Proteins

Pseudoxanthoma Elasticum-Like Skin Changes Induced by Penicillamine

Structural requirements essential for elastin coacervation: favorable spatial arrangements of valine ridges on the three‐dimensional structure of elastin‐derived polypeptide (VPGVG)n

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