Purification of novel calcium binding proteins from Trypanosoma brucei: properties of 22-, 24- and 38-kilodalton proteins

Haghighat, Nasser; Ruben, Larry

doi:10.1016/0166-6851(92)90205-x

Cited by 48 publications

(32 citation statements)

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“…Its wide occurrence in many different tissues, and even in plants [6], makes it likely that it interferes indirectly with the signal-transduction cascade that leads to histamine release. In this connection, its high calcium affinity is noteworthy, suggesting that it has a role in calcium metabolism [5,9]. Although it is known that TCTP is certainly not a tumor-specific protein [7], we preferred to stay with this terminology because it is that most used in the literature and in databases.…”

Section: Discussionmentioning

confidence: 99%

“…This situation is further complicated by experiments showing that TCTP can act on basophils of atopic patients in an IgE-dependent way as a histamine releasing factor [8]. Furthermore TCTP has been described as a protein which binds calcium with high affinity, but does not belong to any known family of calcium-binding proteins [5,9].Despite the fact that its physiological role is currently not clearly defined, the regulation of expression of TCTP demands Correspondence to B.-J. Thiele,…”

mentioning

confidence: 99%

“…The mouse protein was also designated as p21 [2] and the human homologue as p23 [3]. TCTP is a highly conserved fairly abundant protein which is found not only in mammals but also in many other species, including nematodes [4], trypanosomes [5], and plants [6]. Recent studies have shown that the term 'TCTP' is somewhat misleading because it is definitely not a protein restricted to tumor cells [7].…”

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confidence: 99%

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Structure of the promoter and complete sequence of the gene coding for the rabbit translationally controlled tumor protein (TCTP) P23

Thiele

Berger

Lenzner

et al. 1998

European Journal of Biochemistry

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We have isolated genomic recombinants containing the complete gene coding for the rabbit translationally controlled tumor protein (TCTP), also known as histamine-releasing factor (HRF) P23. The gene is organized into five introns and six exons and its total length amounts to 3819 nucleotides. All intron/ exon boundaries are in accordance with the GT/AG rule. Transcription of the gene generates two mRNAs of 843 and 1163 nucleotides differing in the length of their 3′-untranslated regions. They are formed by alternative polyadenylation. The transcription initiation site has been determined by comparison of sequences of the gene and several processed TCTP pseudogenes. The full-length 5′-untranslated region comprises 116 nucleotides and starts with an oligopyrimidine tract important for translational regulation. Additionally 1.2 kb of the 5′-flanking promoter region has been sequenced. The promoter contains a TATA box at Ϫ30 and potential binding sites for transcription factors such as stimulating protein 1 (Sp1), nuclear factor 1 (NF1), activator protein 1 (AP1), c-Ets1, cAMP-response element (CP2), myeloid-specific zinc finger protein 1 (MZF1) and others. For functional analysis 5′-flanking sequences up to Ϫ918 were fused to the chloramphenicol acetyltransferase (CAT) gene and tested using a rabbit aortic smoothmuscle cell line by cell transfection and CAT assays. The results confirm that the analyzed gene is the actively transcribed TCTP gene.Keywords : translationally controlled tumor protein; histamine-releasing factor; gene organization ; promoter; pseudogenes.The translationally controlled tumor protein (TCTP) was described initially by Brawerman's group [1] as a growth-related protein in mouse ascites and erythroleukemic cells whose mRNA is stored as translationally inactive mRNP complexes. The mouse protein was also designated as p21 [2] and the human homologue as p23 [3]. TCTP is a highly conserved fairly abundant protein which is found not only in mammals but also in many other species, including nematodes [4], trypanosomes [5], and plants [6]. Recent studies have shown that the term 'TCTP' is somewhat misleading because it is definitely not a protein restricted to tumor cells [7]. This situation is further complicated by experiments showing that TCTP can act on basophils of atopic patients in an IgE-dependent way as a histamine releasing factor [8]. Furthermore TCTP has been described as a protein which binds calcium with high affinity, but does not belong to any known family of calcium-binding proteins [5,9].Despite the fact that its physiological role is currently not clearly defined, the regulation of expression of TCTP demands Correspondence to B.-J. Thiele,

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Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

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Structure of the promoter and complete sequence of the gene coding for the rabbit translationally controlled tumor protein (TCTP) P23

Thiele

Berger

Lenzner

et al. 1998

European Journal of Biochemistry

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“…The first studies on intracellular functions of TCTP reported its Ca 2+ -binding activity (Haghighat and Ruben 1992) and its microtubule association. Our study revealed that TCTP/P23 is bound to microtubules, inclusive of the mitotic spindle, in a cell-cycle-dependent manner, and that it has microtubule-stabilising activity (Gachet et al 1999).…”

Section: The 'Translationally Controlled Tumour Protein Tctp': Names mentioning

confidence: 99%

“…Ca 2+ -stress and maintenance of ion homeostasis. Possibly the earliest functional association of the TCTP protein to be discovered was the Ca 2+ -binding activity of a protein from Trypanosomes (Haghighat and Ruben 1992). Later, it was shown that TCTP levels are regulated in response to perturbations of intracellular Ca 2+ -homeostasis (Xu et al 1999).…”

Section: Involvement In Cellular Stress Responsesmentioning

confidence: 99%

The Translational Controlled Tumour Protein TCTP: Biological Functions and Regulation

Bommer

2017

Results and Problems in Cell Differentiation

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The Translational Controlled Tumour Protein TCTP (gene symbol TPT1, also called P21, P23, Q23, fortilin or histamine-releasing factor, HRF) is a highly conserved protein present in essentially all eukaryotic organisms and involved in many fundamental cell biological and disease processes. It was first discovered about 35 years ago, and it took an extended period of time for its multiple functions to be revealed, and even today we do not yet fully understand all the details. Having witnessed most of this history, in this chapter, I give a brief overview and review the current knowledge on the structure, biological functions, disease involvements and cellular regulation of this protein. TCTP is able to interact with a large number of other proteins and is therefore involved in many core cell biological processes, predominantly in the response to cellular stresses, such as oxidative stress, heat shock, genotoxic stress, imbalance of ion metabolism as well as other conditions. Mechanistically, TCTP acts as an anti-apoptotic protein, and it is involved in DNA-damage repair and in cellular autophagy. Thus, broadly speaking, TCTP can be considered a cytoprotective protein. In addition, TCTP facilitates cell division through stabilising the mitotic spindle and cell growth through modulating growth signalling pathways and through its interaction with the proteosynthetic machinery of the cell. Due to its activities, both as an anti-apoptotic protein and in promoting cell growth and division, TCTP is also essential in the early development of both animals and plants. Apart from its involvement in various biological processes at the cellular level, TCTP can also act as an extracellular protein and as such has been involved in modulating whole-body defence processes, namely in the mammalian immune system. Extracellular TCTP, typically in its dimerised form, is able to induce the release of cytokines and other signalling molecules from various types of immune cells. There are also several examples, where TCTP was shown to be involved in antiviral/antibacterial defence in lower animals. In plants, the protein appears to have a protective effect against phytotoxic stresses, such as flooding, draught, too high or low temperature, salt stress or exposure to heavy metals. The finding for the latter stress condition is corroborated by earlier reports that TCTP levels are considerably up-regulated upon exposure of earthworms to high levels of heavy metals. Given the involvement of TCTP in many biological processes aimed at maintaining cellular or whole-body homeostasis, it is not surprising that dysregulation of TCTP levels may promote a range of disease processes, foremost cancer. Indeed a large body of evidence now supports a role of TCTP in at least the most predominant types of human cancers. Typically, this can be ascribed to both the anti-apoptotic activity of the protein and to its function in promoting cell growth and division. However, TCTP also appears to be involved in the later stages of cancer progression, such ...

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Cellular distribution of translationally controlled tumor protein in rat and human testes

et al. 2001

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In a recent proteomic study we identified 53 spermatogonial proteins among which was the translationally controlled tumor protein (TCTP). This is a protein previously reported as being implicated in proliferation events in normal and tumoral tissues that had never previously been seen in the testis. The present study was aimed at establishing the complete cellular distribution of TCTP and its transcript and the ontogenetic expression of this gene within the testis. Using an immunohistochemistry technique, an intense TCTP signal was detected in gonocytes (the prespermatogonia) in the fetal rat testis and in spermatogonia within adult human and neonatal and adult rat testes. Meiotic spermatocytes and postmeiotic haploid spermatids were also strongly immunostained in a stage-dependent manner in human and rat testes. In addition, different levels of TCTP expression were also observed in the testicular somatic cells, with strong expression in Leydig cells and peritubular cells, and weak expression in Sertoli cells. Western and Northern blot analyses confirmed the presence of TCTP at all ages studied, with higher levels of RNA expression at 9 and 20 d postpartum, when spermatogonia and primary spermatocytes represent the highest proportion of germ cells: it was also confirmed that TCTP is present in all populations of isolated testicular cells. A transcript of 0.85 kb corresponding to TCTP, was expressed at all ages studied. This transcript was found to be expressed strongly in spermatogonia, somewhat less in isolated Leydig, resident macrophage, peritubular and Sertoli cells, weakly in the primary spermatocytes but not at all in spermatids. Interestingly, in the latter, a different transcript of 1.1 kb was present. The same 1.1 kb transcript appeared in testis extracts from 35 days postpartum onwards, corresponding to an age when spermatids accumulate within the tubules. Of note is that resident macrophages were found to express both the 0.85 and the 1.1 kb transcripts. We conclude that the strong expression of TCTP in spermatogonia makes it highly likely that the protein plays a significant role in spermatogenesis.

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Purification of novel calcium binding proteins from Trypanosoma brucei: properties of 22-, 24- and 38-kilodalton proteins

Cited by 48 publications

References 28 publications

Structure of the promoter and complete sequence of the gene coding for the rabbit translationally controlled tumor protein (TCTP) P23

Structure of the promoter and complete sequence of the gene coding for the rabbit translationally controlled tumor protein (TCTP) P23

The Translational Controlled Tumour Protein TCTP: Biological Functions and Regulation

Cellular distribution of translationally controlled tumor protein in rat and human testes

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