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Calreticulins: Calcium-binding prot...

Persson, Staffan Hans.

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Calreticulins: Calcium-binding proteins with functional diversity and evolutionary duality.

紀錄類型:	書目-電子資源 : Monograph/item
正題名/作者:	Calreticulins: Calcium-binding proteins with functional diversity and evolutionary duality./
作者:	Persson, Staffan Hans.
面頁冊數:	228 p.
附註:	Source: Dissertation Abstracts International, Volume: 64-07, Section: B, page: 3036.
Contained By:	Dissertation Abstracts International64-07B.
標題:	Biology, Botany. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3099007
ISBN:	0496466119

Calreticulins: Calcium-binding proteins with functional diversity and evolutionary duality.
Persson, Staffan Hans.

Calreticulins: Calcium-binding proteins with functional diversity and evolutionary duality. - 228 p.

Source: Dissertation Abstracts International, Volume: 64-07, Section: B, page: 3036.

Thesis (Ph.D.)--North Carolina State University, 2003.

Calreticulin is a multifunctional protein mainly localized in the endoplasmic reticulum in eukaryotic organisms. The protein comprises three distinct regions: the N-terminal N domain, the C-terminal C domain, and the central P domain, reflecting the functional diversity of calreticulin. In animal cells the protein can bind approximately 25 mol Ca2+ per mol protein. Although a similar Ca2+ binding capacity is evident for plant calreticulins, the physiological relevance of the protein in endoplasmic reticulum Ca2+ regulation has been elusive. Nicotiana tabacum suspension cells were therefore transformed with a maize crt cDNA, under the control of a heat-shock promoter. Induction of the calreticulin transgene enhanced the endoplasmic reticulum Ca2+ content in vitro. Furthermore, heat shock-induced Arabidopsis plants, transformed with the same construct, grew better on medium containing low levels of Ca2+ compared with control plants.

ISBN: 0496466119Subjects--Topical Terms:

1017825
Biology, Botany.

Calreticulins: Calcium-binding proteins with functional diversity and evolutionary duality.
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520 $a Calreticulin is a multifunctional protein mainly localized in the endoplasmic reticulum in eukaryotic organisms. The protein comprises three distinct regions: the N-terminal N domain, the C-terminal C domain, and the central P domain, reflecting the functional diversity of calreticulin. In animal cells the protein can bind approximately 25 mol Ca2+ per mol protein. Although a similar Ca2+ binding capacity is evident for plant calreticulins, the physiological relevance of the protein in endoplasmic reticulum Ca2+ regulation has been elusive. Nicotiana tabacum suspension cells were therefore transformed with a maize crt cDNA, under the control of a heat-shock promoter. Induction of the calreticulin transgene enhanced the endoplasmic reticulum Ca2+ content in vitro. Furthermore, heat shock-induced Arabidopsis plants, transformed with the same construct, grew better on medium containing low levels of Ca2+ compared with control plants.
520 $a The multifunctional properties assigned to calreticulins have triggered a search for additional isoforms and for two or more copies of calreticulin genes in mammals. By performing BLASTP searches we found a calreticulin isoform (Crt2) in human, which differed significantly from the previously established isoform. In addition, a homolog to the Crt2 protein was obtained from mouse, and suggested an orthologous Crt2 isoform present in several mammalian species. Similar to the calnexin homolog calmegin, the crt2 gene was exclusively expressed in testis of the tissues investigated.
520 $a Arabidopsis contains three calreticulin isoforms. Phylogenetic analyses and expression profiling revealed that both monocotyledons and eudicotyledons contain two distinct calreticulin isoform groups: a Crt1/Crt2 and a Crt3 group. Whereas the crt1/crt2 genes were active in all tissue types investigated, peaking in flowers, the crt3 gene was mainly expressed in root and leaf tissues. Furthermore, members from the different isoform groups were induced differently in response to tunicamycin, an inhibitor of N-linked glycosylation. To provide a common research basis for plant calreticulins, a new nomenclature for the proteins was suggested. The discovery of two orthologous calreticulin isoform groups in both animals and plants support an evolutionary duality, and suggest functional diversity for calreticulins.
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