Identification of testis specific calcineurin β subunit isoform by a monoclonal antibody and detection of a specific six amino acid sequence

Nishio, Hisahide; Matsui, Hideki; Etoh, S; Moia, Lizomar J.M.P.; Tokuda, Masaaki; Itano, Toshifumi; Hatase, Osamu

doi:10.1016/s0006-291x(05)80108-1

Cited by 15 publications

(9 citation statements)

References 10 publications

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“…The expression of unique isoforms of PP1, 2A and 2B in mammalian testis has also been reported [25][26][27]. In the present study the specific expression of PP2C for the first time.…”

Section: Substrate Specificity Of Pp2c~ Isoformssupporting

confidence: 76%

Differentiation‐dependent enhanced expression of protein phosphatase 2Cβ in germ cells of mouse seminiferous tubules

et al. 1996

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“…The expression of unique isoforms of PP1, 2A and 2B in mammalian testis has also been reported [25][26][27]. In the present study the specific expression of PP2C for the first time.…”

Section: Substrate Specificity Of Pp2c~ Isoformssupporting

confidence: 76%

Differentiation‐dependent enhanced expression of protein phosphatase 2Cβ in germ cells of mouse seminiferous tubules

et al. 1996

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“…Isoform diversity exists for both subunits. A second isoform of the B subunit (B2) has been isolated from testis, which also contains the other (B1) isoform (Nishio et al, 1992). Three different isoforms of the A subunit (α, β, γ) have been recognized (Guerini and Klee, 1989;Ito et al, 1989;Kuno et al, 1989;Kincaid et al, 1990;Muramatsu et al, 1992).…”

Section: Ca 2+ -Regulated Protein Dephosphorylationmentioning

confidence: 99%

Generation, Control, and Processing of Cellular Calcium Signals

Carafoli

Santella

Branca

et al. 2001

Critical Reviews in Biochemistry and Molecular Biology

482

321

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In the course of evolution, Ca2+ has emerged as the most versatile intracellular messenger. Its concentration within cells is controlled by reversible binding to specific classes of proteins that act as Ca2+ sensors to decode its information before passing it on to targets. The decoding operation is based on specific conformational changes in the sensor proteins. Other proteins intrinsic to membranes simply control Ca2+ concentration without processing its message, by transporting it across membrane boundaries. They are located in the plasma membrane and in the membranes of the organelles (the endo(sarco)plasmic reticulum, the mitochondria, the nuclear envelope), which play distinctive roles in the cellular homeostasis of Ca2+. Ca2+ is an ambivalent signaling agent. It carries information to virtually all processes important to cell life (e.g., it couples excitation to contraction, secretion, gene transcription, and controls enzyme activity through protein phosphorylation-dephosphorylation), but also transmits signals that promote the programmed demise of cells. When escaping control, Ca2+ also precipitates toxic cell death.

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“…The reason that changes in the electrophoretic mobility of most Ca 2+ -binding proteins on SDS-PAGE differ in the presence and absence of Ca 2+ remains unanswered, but it was reported that EF-hand calcium-binding proteins show calcium shift on SDS-PAGE [11]. In CBPs such as calmodulin, major conformational changes result after the filling of Ca 2+ -binding sites [15].…”

Section: Discussionmentioning

confidence: 99%

“…In mice, varying stages of germ cells exist in pubertal seminiferous tubule [2]. The expression of high Mr CBPs such as molecular chaperone involved in spermatogenesis [4], protein phosphatase [11] calmodulin [9], Ca 2+ sequestering molecule [10], antigen involved in membrane fusion of spermatozoa [13], and acrosomal component [12] have been reported in testis. Therefore, this result coincided with the structural and functional differentiation of cellular components of seminiferous epithelia at puberty.…”

Section: Discussionmentioning

confidence: 99%

Postnatal Changes in the Calcium Binding Proteins of Mouse Testis

Gye

Kim²,

Ahn³

et al. 2001

Archives of Andrology

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To define the changes in calcium-binding proteins (CBPs) of mouse testis during postnatal development, testicular protein extracts were analyzed by mobility shift after Ca2+ binding (MSACB) in the 2-dimensional SDS-PAGE. In the adult testis extracts, 29 kinds of protein spots showed mobility shift in the gel containing Ca2+. Among them, 2 spots showed nonspecific mobility shift and 4 spots showed Zn2+ shift. Drastic changes in expression of high-Mr CBPs (Mr > 25 kDa) were observed in testis 3 weeks after birth, suggesting that their expressions were developmentally changed. There was no obvious difference in the qualitative patterns of CBP between 4-week-old testis and adult testis. There was a large mass of CBPs (Mr = 20-25 kDa) expressed constitutively in testis throughout the postnatal development. Degree of MSACB (Mr on the diagonal line/Mr of shifted point in Ca2+ gel) of each spot was in the range of 1.1-1.7 in 12% acrylamide gel. These results suggest that changes in CBPs of testis are closely related with progression of spermatogenesis in mouse testis.

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Identification of testis specific calcineurin β subunit isoform by a monoclonal antibody and detection of a specific six amino acid sequence

Cited by 15 publications

References 10 publications

Differentiation‐dependent enhanced expression of protein phosphatase 2Cβ in germ cells of mouse seminiferous tubules

Differentiation‐dependent enhanced expression of protein phosphatase 2Cβ in germ cells of mouse seminiferous tubules

Generation, Control, and Processing of Cellular Calcium Signals

Postnatal Changes in the Calcium Binding Proteins of Mouse Testis

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