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1

Multilevel regulation of the tyrosine hydroxylase. I.Posttranscriptional levels

100%
Lenartowski R., Goc A.
Postępy Higieny i Medycyny Doświadczalnej
|
2002
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vol. 56
|
issue 4
555-565
EN
The tyrosine hydroxylase plays a key role in the catecholamine synthesis responding to many stimuli disturbing homeostasis. In this part we described the posttranscriptional levels of the gene and the protein regulation including: alternative splicing, isoform specificity, feedback inhibition, protein phosphorylation and dephosphorylation, protein stability, translational regulation.
2

Multilevel regulation of the tyrosine hydroxylase. II. Transcriptional regulation

100%
Lenartowski R., Goc A.
Postępy Higieny i Medycyny Doświadczalnej
|
2002
|
vol. 56
|
issue 5
671-686
EN
The tyrosine hydroxylase gene is subject to very precise regulation which aim is to adjust the level of the catecholamines to current stimuli disturbing the homeostasis . The fine tuning of the TH gene activity is realized by the ?cross-talk? between the complexes of transcriptional factors with their appropriate regulatory sequences. The transcriptional aspect of that regulation has been reviewed emphasizing the rule of the regulatory sequences in determining cell, tissue and developmental specificity of the TH gene activity.
3

Localization of the calreticulin gene mRNA in unpollinated and pollinated styles of Petunia hybrida

81%
Lenartowska M., Lenartowski R., Bednarska E.
Journal of Applied Genetics
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2001
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vol. 42
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issue 1
15-20
EN
The objective of our research on Petunia hybrida is to understand the role of calreticulin in the growth of pollen tubes in the pistil. The aim of this study was the first step: finding out whether CRT gene expression takes place in unpollinated and pollinated styles. It was revealed by in situ hybridization that the transcription of the calreticulin gene takes place in the transmitting cells of unpollinated and pollinated styles and in pollen tubes growing in vivo. The mRNA transcripts of the CRT gene were localized mainly on the surface of endoplasmic reticulum (ER) membranes, both in transmitting cells and in the tip cytoplasm of pollen tubes. The results of this study show that calreticulin can be involved in pollen ? pistil interaction in vivo.
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