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Functional characterization of the ‘PBX interacting protein’ (HPIP) in normal and malignant human haematopoiesis.

von Dr. Pak

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[1.] Pak/Fragment 028 07 - Diskussion
Zuletzt bearbeitet: 2014-04-06 20:55:21 Hindemith
Abramovich et al 2000, BauernOpfer, Fragment, Gesichtet, Pak, SMWFragment, Schutzlevel sysop

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Untersuchte Arbeit:
Seite: 28, Zeilen: 7-12, 14-20
Quelle: Abramovich et al 2000
Seite(n): 26172, 26174, 26176, Zeilen: 26172: l.col: 4-8: 26174: l.col: 34-39 - r.col: 1-2 ; 26176: r.col: 13-15, 19-20
The new haematopoietic PBX-interacting protein (HPIP) was identified by a yeast two-hybrid screen of a fetal-liver haematopoietic cDNA library using PBX1 as bait. HPIP cDNA encodes a novel protein of 731 amino acid residues containing no homology to any known protein and has a calculated molecular mass of 80 kDa. HPIP is predicted to have a coiled-coil domain, suggesting that it interacts with other proteins. [...] The expression of PBX1 and HPIP was characterized observed by reverse transcription-PCR analysis of RNA obtained from bone marrow: HPIP expression was detected in the CD34+ fraction containing the haematopoietic progenitors and at lower levels in the CD34- matures cell population.

The same pattern was found for PBX1, indicating that HPIP and PBX1 are coexpressed in the same haematopoietic compartment.

A yeast two-hybrid screen of a fetal liver-hematopoietic cDNA library using PBX1a as bait led to the discovery of a novel non-homeodomaincontaining protein that interacts with PBX1 as well as PBX2 and PBX3.

[page 26174]

HPIP expression in primitive human hematopoietic cells was also demonstrated by reverse transcription-PCR analysis of RNA obtained from human bone marrow. Fig. 2B shows that HPIP is strongly expressed in the CD34+ fraction containing the hematopoietic progenitors and at lower levels in the CD34- mature cell population. The same pattern of expression was found for PBX1, indicating that HPIP and PBX1 are co-expressed in the same hematopoietic compartment.

[page 26176]

HPIP cDNA encodes a novel protein of 731 amino acid residues containing no homology to any known protein. The predicted HPIP protein has a calculated molecular mass of 80 kDa [...]. HPIP is predicted to have a coil-coil domain, suggesting that it interacts with other proteins.

Anmerkungen

The source is given just before the documented passage and it can be understood from the text that what follows is describing the work of the authors of the source. It is not clear, however, that the text is taken from the source.

Note: the sentence not taken from this source (line 13), can be found here: Pak/Fragment 028 12

Sichter
(Hindemith) Schumann

[2.] Pak/Fragment 028 12 - Diskussion
Zuletzt bearbeitet: 2014-04-06 21:12:43 Hindemith
Abramovich et al 2002, Fragment, Gesichtet, KomplettPlagiat, Pak, SMWFragment, Schutzlevel sysop

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Untersuchte Arbeit:
Seite: 28, Zeilen: 12-14
Quelle: Abramovich et al 2002
Seite(n): 6766, Zeilen: r.col: 22-26
HPIP can bind to different members of the mammalian PBX family, inhibit the binding of PBX1/Hox complex to DNA and block the transcriptional activity of E2A-PBX1. HPIP can bind to the different members of the mammalian Pbx family, inhibit the binding of Pbx1/Hox complex to DNA and block the transcriptional activity of E2A-Pbx (Abramovich et al., 2000).
Anmerkungen

There is a reference to the source further down the page in the following paragraph for another sentence that is also taken from it.

Sichter
(Hindemith) Schumann


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