Complete covalent structure of human .beta.-thromboglobulin

Begg, Geoffrey S.; Pepper, Duncan S.; Chesterman, Colin N.; Morgan, Francis J.

doi:10.1021/bi00602a024

Cited by 210 publications

(85 citation statements)

References 24 publications

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“…The C termini of pCEF-4 and CTAP-III are 56% homologous when conserved residues are taken into account. Other related proteins such as ,B-thromboglobulin (19), platelet basic protein (a probable precursor of both CTAP-III and ,B-thromboglobulin, ref. 20), platelet factor 4 (16), and 'yIP-10, an interferon-inducible gene (21), also have homology with pCEF-4.…”

Section: Resultsmentioning

confidence: 99%

“…The sequence of the pCEF-4 insert predicts a protein sequence homologous to CTAP-III and other biologically active peptides found in human platelets (16,(18)(19)(20). Although pleiotropic effects on cellular metabolism have been ascribed to this family of related polypeptides, including the stimulation of synthesis of DNA, glycosaminoglycan, hyaluronic acid as well as glycolysis, the significance of constitutive expression of pCEF4 in fibroblasts remains to be determined.…”

Section: Discussionmentioning

confidence: 99%

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Constitutive expression of a gene encoding a polypeptide homologous to biologically active human platelet protein in Rous sarcoma virus-transformed fibroblasts.

Bédard

Alcorta

Simmons

et al. 1987

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

121

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A molecular clone corresponding to a 1.2-kilobase mRNA enriched in Rous sarcoma virus-transformed chicken embryo fibroblasts (CEF) was identified by differential screening of a cDNA library. The induction of the cloned sequence (denoted pCEF-4) in CEF infected by the temperature-sensitive mutant NY72-4 Rous sarcoma virus is rapid and independent of protein synthesis. DNA sequencing of the 1.2-kilobase insert of CEF4 revealed an open reading frame that predicts an 11-kDa protein. The predicted pCEF-4 gene product is homologous to human connective tissue-activating peptide III (CTAP-Il) and platelet factor 4 (PF-4). Serum stimulation of quiescent normal CEF results in a rapid but transient expression ofpCEF-4 mRNA. Hence, pCEF-4 mRNA is expressed at the G.-G1 transition and during the first G, phase of normal CEF reentering the cell cycle. The expression of pCEF-4 mRNA in Rous sarcoma virus-transformed CEF appears to be the result of transcriptional activation and stabilization of the transcript.Much of our knowledge of the gene products responsible for cell transformation is derived from investigations of the virally encoded oncogenes and of the protooncogenes, their cellular ancestors. Functional and structural similarities often exist between oncogene products and growth factors, growth factor receptors, or the products of other genes expressed during the normal mitogenic response (1). In several instances, the alteration in cellular protooncogenes resulting in their oncogenic activation is understood (1-4). Hence, considerable progress has been accomplished regarding the biochemical characterization of some of the agents that cause cell transformation. In contrast, little is known about the biochemical pathways and cellular activities critically modified during the transformation process. The absence of functional assays and the lack of an appropriate model system amenable to genetic manipulation have clearly limited our progress in this respect. Various approaches have been utilized to circumvent these limitations. One involves the study of protein phosphorylation in normal and transformed cells, because a class of transforming proteins exhibits tyrosine-specific kinase activity. Some investigators have also compared the role of protooncogenes in normal and malignant growth because of the obvious links between this class of genes and the mitogenic response. We have followed a third approach by searching for genes repressed or expressed in response to transforming proteins or growth factors without regard to their possible relationship to known oncogenes.In this report, we describe a cDNA clone (denoted pCEF-4) corresponding to a 1.2-kilobase (kb) mRNA species that is expressed transiently in response to serum and constitutively in Rous sarcoma virus (RSV)-transformed chicken embryo fibroblasts (CEF) in the presence or absence of serum. Increased transcription and stabilization result in the accumulation of the pCEF-4 mRNA in RSV-transformed cells. A polypeptide of Mr 11,000 is predicted by the nucleic...

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Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Constitutive expression of a gene encoding a polypeptide homologous to biologically active human platelet protein in Rous sarcoma virus-transformed fibroblasts.

Bédard

Alcorta

Simmons

et al. 1987

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

121

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“…21,22 Although many activities have been ascribed to PF-4, 1,4,23 a G protein-coupled receptor for this oldest CXC chemokine has still to be identified. In view of its high affinity for heparin, PF-4 was shown to activate neutrophils through binding to chondroitin sulfate-type glycosaminoglycans.…”

Section: Discussionmentioning

confidence: 99%

Identification of a blood-derived chemoattractant for neutrophils and lymphocytes as a novel CC chemokine, Regakine-1

Struyf

Proost

Lenaerts

et al. 2001

Blood

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Chemokines constitute a large family of chemotactic cytokines that selectively attract different blood cell types. Although most inflammatory chemoattractants are only induced and released in the circulation during acute infection, a restricted number of CXC and CC chemokines are constitutively present in normal plasma at high concentrations. Here, such a chemotactic protein was purified to homogeneity from serum and fully identified as a novel CC chemokine by mass spectrometry and amino acid sequence analysis. The protein, tentatively designated Regakine-1, shows less than 50% sequence identity with any known chemokine. This novel CC chemokine chemoattracts both neutrophils and lymphocytes but not monocytes or eosinophils. Its modest chemotactic potency but high blood concentration is similar to that of other chemokines present in the circulation, such as hemofiltrate CC chemokine-1, platelet factor-4, and ␤-thromboglobulin. Regakine-1 did not induce neutrophil chemokinesis. However, it synergized with the CXC chemokines interleukin-8 and granulocyte chemotactic protein-2, and the CC chemokine monocyte chemotactic protein-3, resulting in an at least a 2-fold increase of the neutrophil and lymphocyte chemotactic response, respectively. The biologic effects of homogeneous natural Regakine-1 were confirmed with chemically synthesized chemokine. Like other plasma chemokines, it is expected that Regakine-1 plays a unique role in the circulation during normal or pathologic conditions. IntroductionSerum is a rich source of leukocyte chemotactic factors that influence the migration of different leukocytic cell types to and from the blood circulation. For example, anaphylatoxin, or C5a, a cleavage product formed during complement activation, chemoattracts both polymorphonuclear and mononuclear blood cells. Other serum proteins such as platelet factor-4 and neutrophil-activating protein-2 are thrombocytederived chemotactic cytokines belonging to the chemokine family. [1][2][3][4] In contrast to C5a, these and other chemokines are each selectively attracting a defined set of leukocytic cell types. The chemokine family is subdivided into 2 major classes, ie, CXC and CC chemokines depending on the positioning of conserved cysteine residues. 1-5 The spectrum of target cells for each chemokine depends on the expression of one or more specific receptors on the different leukocyte subtypes. The receptors of all chemokines as well as those of C5a and other chemoattractants such as leukotriene B 4 and bacterial N-formylmethionyl-containing peptides belong to the family of G protein-coupled 7-transmembrane domain receptors. 6 Addition of bovine or human serum is often essential for the growth or maintenance of continuous and primary cell cultures. For example, we and others have used in the past low serum concentrations to preserve high viability of freshly isolated human leukocytes or to support the growth of hematopoietic progenitor cells in well-defined media. 7 Conflicting or variable experimental results have often been rela...

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“…All inductions were done in the regular cell growth media. The IFN--y was always diluted into medium containing either 1 Positive phage were plaque purified, and DNA isolated from these phage was used for restriction analysis against human DNA. Northern (RNA blot) and Southern blot (hybridization) analyses.…”

Section: *Corresponding Authormentioning

confidence: 99%

“…The deduced amino acid sequence of the IP-10 protein reveals that it is a member of a newly emerging family of cytokines having chemotactic, mitogenic, and immunomodulatory activities. This family includes the platelet basic proteins (PBP) (e.g., ,B-thromboglobulin [1] and connective tissue-activating peptide III [7]), platelet factor 4 (PF4) (9), and two recently isolated cDNA clones designated 9E3 (36) and 310c (J. Schmid and C. Weissman, J. Immunol., in press).…”

mentioning

confidence: 99%

Genomic characterization of a gamma-interferon-inducible gene (IP-10) and identification of an interferon-inducible hypersensitive site.

Luster¹,

Ravetch²

1987

Mol. Cell. Biol.

139

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The genomic organization of a gamma-interferon-inducible gene, IP-1O, reveals three introns that interrupt the transcribed sequence into four functional domains. Comparison of the intron-exon structure of this gene to the gene for an homologous chemotactic platelet protein, platelet factor 4, establishes that both genes are interrupted in precisely the same positions within homologous codons; this demonstrates that they belong to a gene family that evolved from a common ancestor. IP-IO and PF4 are two members of a newly described gene family that is likely to include the homologous chemotactic and mitogenic platelet basic proteins (connective tissue-activating protein Ill and P-thromboglobulin), the transformation-related protein 9E3, and 310c, a mitogen-stimulated leukocyte protein. A DNase I-hypersensitive site has been found in responsive cells in a region upstream of the RNA initiation site. This hypersensitive site is induced by gamma interferon and thus provides a structural basis for the transcriptional activation seen for this gene by gamma interferon.

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Complete covalent structure of human .beta.-thromboglobulin

Cited by 210 publications

References 24 publications

Constitutive expression of a gene encoding a polypeptide homologous to biologically active human platelet protein in Rous sarcoma virus-transformed fibroblasts.

Constitutive expression of a gene encoding a polypeptide homologous to biologically active human platelet protein in Rous sarcoma virus-transformed fibroblasts.

Identification of a blood-derived chemoattractant for neutrophils and lymphocytes as a novel CC chemokine, Regakine-1

Genomic characterization of a gamma-interferon-inducible gene (IP-10) and identification of an interferon-inducible hypersensitive site.

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