Complete amino acid sequence of a histidine-rich proteolytic fragment of human ceruloplasmin.

Kingston, I B; Kingston, B L; Putnam, Frank W.

doi:10.1073/pnas.76.4.1668

Cited by 30 publications

(25 citation statements)

References 19 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Because crystallographic structures and amino acid sequences are established for some of the small blue proteins and some of the large multicopper oxidases, we have searched our sequence data for ceruloplasmin for segments homologous to the known copper-binding sites in these proteins. We have shown (7)(8)(9)14) that the carboxy-terminal sequence of the 19-kDal fragment…”

Section: Resultsmentioning

confidence: 99%

“…Histidines at the copper-binding site of bovine superoxide dismutase (23,24) are enclosed in circles. Sources ofsequence data: cytochrome oxidase polypeptide 1(CCO), human (25), bovine (26); human ceruloplasmin (Cp) 19-kDal fragment (7); superoxide dismutase, human (27), bovine (24), yeast (28). For each sequence the position number is given for the first amino acid shown.…”

Section: Resultsmentioning

confidence: 99%

“…With the recent completion of the primary structures of the 50,000-dalton (50-kDal) (6) and 19,000-dalton (7)(8)(9) fragments ofhuman ceruloplasmin [ferroxidase; iron(II):oxygen oxidoreductase, EC 1.16.3.1], 564 residues of the amino acid sequence of the single polypeptide chain of this protein are known. These fragments are from the carboxyl terminus of the molecule and account for more than halfofthe primary structure of this blue copper oxidase.…”

mentioning

confidence: 99%

See 2 more Smart Citations

Internal duplication and evolution of human ceruloplasmin.

Dwulet¹,

Putnam²

1981

Proc. Natl. Acad. Sci. U.S.A.

Self Cite

View full text Add to dashboard Cite

With ihe completion of the primary structure of the 50,000-and 19,000-dalton fragments of human ceruloplasmin [ferroxidase; iron(il):oxygen oxidoreductase, EC 1.16.3.11], over halfofthe covalent structure ofthe single polypeptide chain ofthis protein is known. Visual and computer analysis of the sequence of the 564 amino acid residues in the two fragments gives clear evidence of statistically significant internal homology suggestive of evolutionary replication of two smaller units. Two homology regions, each composed of 224 residues, were defined by an intrasequence alignment that required only three gaps in each 224-residue segment. The two homology regions exhibited 43% identity in sequence, and 13% of the remaining positions had similar residues. The sequence ofa 160-residue segment in ceruloplasmin exhibits significant homology to the active (copper-binding) sites of blue electron-transfer proteins such as azurins and plastocyanins and multicopper oxidases such as cytochrome oxidase and superoxide dismutase. It is proposed that a primitive ceruloplasmin gene was formed by the fusion of two genes coding, respectively, for proteins about 160 and 190 amino acid residues in length and that this precursor gene coding for about 350 amino acids was later triplicated to form the gene for the present-day ceruloplasmin molecule of about 1050 amino acids.Analytical and statistical comparison of amino acid sequences has been a powerful method for detection and estimation of structural similarities among and within proteins, for evaluation of structure-function relationships in a family of proteins, and for study of genetic change in the course of evolutionary development of a class of proteins (1-3). The comparison may be done by visual alignment oftwo sequences for best fit as judged both by identity and similarity of paired amino acids at corresponding positions; gaps in the sequences are sometimes inserted to maximize the fit. Statistical methods for assessing relatedness of proteins are based on computer programs that accumulate pair scores for two amino acids, using a mutation data matrix based on physical and structural parametersg and codon differences for all possible pairs ofamino acids (4) or from actual accepted point mutations accumulated from related sequences (5). By such means the degree of intersequence or intrasequence homology may be assessed; here "homologous" is used to mean matching (identical or similar) in structure, position, physical characteristics, and codons.With the recent completion of the primary structures of the 50,000-dalton (50-kDal) (6) and 19,000-dalton (19-kDal) (7-9) fragments ofhuman ceruloplasmin [ferroxidase; iron(II):oxygen oxidoreductase, EC 1.16.3.1], 564 residues of the amino acid sequence of the single polypeptide chain of this protein are known. These fragments are from the carboxyl terminus of the molecule and account for more than halfofthe primary structure of this blue copper oxidase. During our study we identified a remarkable degree of internal homology in c...

show abstract

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

mentioning

confidence: 99%

See 1 more Smart Citation

Internal duplication and evolution of human ceruloplasmin.

Dwulet¹,

Putnam²

1981

Proc. Natl. Acad. Sci. U.S.A.

Self Cite

View full text Add to dashboard Cite

show abstract

“…Since S100A13 (Landriscina et al, 2001a) and FGF1 (Engleka and Maciag, 1992) have been characterized as Cu 2+ -binding proteins, and there is a high degree of crystallographic structural conservation between the FGF and IL-1 prototypes (Graves et al, 1990;Zhang et al, 1991) including the presence of three solvent accessible histidine residues (Graves et al, 1990) that are conventionally regarded as being important for the binding of proteins to copper (Kingston et al, 1979;Kwiatkowski et al, 1977), it was perhaps not surprising that IL-1α is a Cu 2+ -binding protein and the precursor and mature forms of IL-1α can readily be purified from media conditioned by heat shock. However, our data demonstrate for the first time that human U937 cells use intracellular Cu 2+ for the export of the signal sequence-less polypeptides, IL-1α and FGF1, into the extracellular compartment in response to temperature stress.…”

Section: Discussionmentioning

confidence: 99%

S100A13 mediates the copper-dependent stress-induced release of IL-1α from both human U937 and murine NIH 3T3 cells

Mandinova

Soldi

Graziani

et al. 2003

Journal of Cell Science

View full text Add to dashboard Cite

Copper is involved in the promotion of angiogenic and inflammatory events in vivo and, although recent clinical data has demonstrated the potential of Cu2+ chelators for the treatment of cancer in man, the mechanism for this activity remains unknown. We have previously demonstrated that the signal peptide-less angiogenic polypeptide, FGF1, uses intracellular Cu2+ to facilitate the formation of a multiprotein aggregate that enables the release of FGF1 in response to stress and that the expression of the precursor form but not the mature form of IL-1α represses the stress-induced export of FGF1 from NIH 3T3 cells. We report here that IL-1α is a Cu2+-binding protein and human U937 cells, like NIH 3T3 cells, release IL-1α in response to temperature stress in a Cu2+-dependent manner. We also report that the stress-induced export of IL-1α involves the intracellular association with the Cu2+-binding protein, S100A13. In addition, the expression of a S100A13 mutant lacking a sequence novel to this gene product functions as a dominant-negative repressor of IL-1α release, whereas the expression of wild-type S100A13 functions to eliminate the requirement for stress-induced transcription. Lastly, we present biophysical evidence that IL-1α may be endowed with molten globule character, which may facilitate its release through the plasma membrane. Because Cu2+ chelation also represses the release of FGF1, the ability of Cu2+ chelators to potentially serve as effective clinical anti-cancer agents may be related to their ability to limit the export of these proinflammatory and angiogenic signal peptide-less polypeptides into the extracellular compartment.

show abstract

“…The confusion originated from the extreme susceptibility of the ceruloplasmin molecule to limited proteolysis. The analysis was complicated further by the following factors: (i) difficulty in preventing autolytic degradation during purification, (ii) strong interaction among the degraded fragments, which could be dissociated only by use of strong denaturing agents, (iii) technical difficulties in se-quence determination of such a large protein, and (iv) the extraordinary degree of internal duplication in the sequence of the polypeptide chain later recognized by us (8)(9)(10)(11).…”

mentioning

confidence: 99%

Single-chain structure of human ceruloplasmin: the complete amino acid sequence of the whole molecule.

Takahashi¹,

Ortel²,

Putnam³

1984

Proc. Natl. Acad. Sci. U.S.A.

Self Cite

200

108

View full text Add to dashboard Cite

We have determined the amino acid sequence of the amino-terminal 67,000-dalton (67-kDa) fragment of human ceruloplasmin and have established overlapping sequences between the 67-kDa and 50-kDa fragments and between the 50-kDa and 19-kDa fragments. The 67-kDa fragment contains 480 amino acid residues and three glucosamine oligosaccharides. These results together with our previous sequence data for the 50-kDa and 19-kDa fragments complete the amino acid sequence of human ceruloplasmin. The polypeptide chain has a total of 1,046 amino acid residues (Mr 120,085) and has attachment sites for four glucosamine oligosaccharides; together these account for the total molecular mass of human ceruloplasmin (132 kDa). The sequence analysis of the peptides overlapping the fragments showed that one additional amino acid, arginine, is present between the 67-kDa and 50-kDa fragments, and another, lysine, is between the 50-kDa and 19-kDa fragments. Only two apparent sites of amino acid interchange have been identified in the polypeptide chain. Both involve a single-point interchange of glycine and lysine that would result in a difference in charge. The results of the complete sequence analysis verified that human ceruloplasmin is composed of a single polypeptide chain and that the subunitlike fragments are produced by proteolytic cleavage during purification (and possibly also in vivo

show abstract

Complete amino acid sequence of a histidine-rich proteolytic fragment of human ceruloplasmin.

Cited by 30 publications

References 19 publications

Internal duplication and evolution of human ceruloplasmin.

Internal duplication and evolution of human ceruloplasmin.

S100A13 mediates the copper-dependent stress-induced release of IL-1α from both human U937 and murine NIH 3T3 cells

Single-chain structure of human ceruloplasmin: the complete amino acid sequence of the whole molecule.

Contact Info

Product

Resources

About