Isolation, crystallization, and primary amino acid sequence of human platelet factor 4.

Hermodson, Mark A.; Schmer, G; Kurachi, Kotoku

doi:10.1016/s0021-9258(17)39951-9

Cited by 159 publications

(19 citation statements)

References 17 publications

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“…They showed a single band on SDS PAGE in the presence or absence of 2-mercaptoethanol. Their amino acid compositions agreed with those expected from the published sequence of PF4 (13,24) and 13TG (4). A monospecific anti-PDGF IgG was prepared by Na2SO4 precipitation and DEAE-Sephacel chromatography of plasma from a goat immunized with purified PDGF.…”

Section: Methodssupporting

confidence: 83%

Platelet proteins, including platelet-derived growth factor, specifically depress a subset of the multiple components of the response elicited by glutathione in Hydra.

Hanai

Kato

Matsuhashi

et al. 1987

The Journal of Cell Biology

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Abstract. Human serum more strongly depressed the feeding response of Hydra (ball formation) elicited by S-methylglutathione than plasma. On the basis of the effect of several proteins released by platelets, at least five apparent components of the response (R1-R5) were suggested. Each of the platelet proteins examined specifically depressed a subset of these components. Among the platelet proteins examined, platelet-derived growth factor (PDGF) specifically depressed the R2 response (the concentration at which the depressing effect was 50% of the maximum [EDs0] was 0.17 pM), and basic fibroblast growth factor depressed the R3 and R5 responses (EDs0 0.50 aM) and the R2 response (EDs0 0.55 pM).With respect to the depression of the R2 response by PDGF, addition of an anti-PDGF IgG or chemical reduction of PDGF, both of which prevent PDGF from binding to its cell surface receptor on responsive cells, eliminated the depressing effect of PDGF on the hydra response. The implications of these observations are discussed.EDUCED glutathione elicits a feeding response in a small freshwater coelenterate, Hydra (29,31). The response is quantitatively measured in duration of tentacle ball formation, a response associated with feeding (18).The response is depressed by lectins such as Ulex europeus I, Ricinus communis I and II (19), and by dopamine and related amines (20). These agents depress the response elicited by S-methylglutathione (GSM) l at concentrations <0.2 ktM. The response elicited by GSM at higher concentrations (> 0.1 WVI) are selectively eliminated, after the animals are illuminated by near UV light in the presence of S-(p-azidophenacyl)glutathione (21). These observations imply that there are multiple components of the response evoked at different concentrations of glutathione.Although descendants of interstitial cells (nerve cells and nematocytes) may control the feeding response of Hydra (8,28), the precise location of a receptor cell or glutathione receptor molecules mediating the response remains to be identified. Recently, while attempting to isolate a monoDr. Kato's present address is National

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Section: Methodssupporting

confidence: 83%

Platelet proteins, including platelet-derived growth factor, specifically depress a subset of the multiple components of the response elicited by glutathione in Hydra.

Hanai

Kato

Matsuhashi

et al. 1987

The Journal of Cell Biology

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“…Sequenator Methodology. Pili protein (1-3 mg) was degraded in the Beckman 890C sequencer according to the methods of Hermodson et al (1972) using a peptide program (Hermodson et al, 1977). The Pth-amino acids were identified by gas-liquid chromatography with the exceptions of the arginyl and histidyl derivatives which were identified by colorimetric spot tests (Hermodson et al, 1972).…”

Section: Methodsmentioning

confidence: 99%

Neisseria pili proteins: amino-terminal amino acid sequences and identification of an unusual amino acid

Hermodson¹,

Chen²,

Buchanan³

1978

Biochemistry

189

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“…The monomer of human PF4 consists of 70 amino acids with a molecular mass of 7766 daltons and is identical in sequence to recombinant human PF4 reported previously and used in these studies (Hermodson et al, 1977;Morgan et al, 1977;Walz et al, 1987). Under physiological conditions, four identical polypeptide chains assemble in a defined manner, and it is assumed that the tetramer is the active form of PF4 in biological systems.…”

mentioning

confidence: 91%

Crystal Structure of Recombinant Human Platelet Factor 4

Zhang¹,

Chen²,

Bancroft³

et al. 1994

Biochemistry

185

192

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The crystal structure of human platelet factor 4 (PF4) has been solved to a resolution of 2.4 A by molecular replacement and refined to an R-factor of 24.1%. The structure consists of four polypeptide chains which form a tetrameric unit. N-terminal residues, previously defined as a random coil or extended loop region, form antiparallel beta-sheet-like structures that form noncovalent associations between dimers. These antiparallel beta-sheet-like structures are positioned lateral to the beta-bilayer motif and stabilize the tetrameric unit. A positively charged ring of lysine and arginine side chains encircles the PF4 tetramer sphere, presenting multiple potential sites and orientations for heparin binding. The electrostatic interactions of multiply charged amino acid side chains and hydrogen bonding interactions at the AB/CD dimer interface serve to stabilize the tetrameric structure further.

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Isolation, crystallization, and primary amino acid sequence of human platelet factor 4.

Cited by 159 publications

References 17 publications

Platelet proteins, including platelet-derived growth factor, specifically depress a subset of the multiple components of the response elicited by glutathione in Hydra.

Platelet proteins, including platelet-derived growth factor, specifically depress a subset of the multiple components of the response elicited by glutathione in Hydra.

Neisseria pili proteins: amino-terminal amino acid sequences and identification of an unusual amino acid

Crystal Structure of Recombinant Human Platelet Factor 4

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