Possible involvement of protein kinase C in parathyroid hormone degradation by osteoblast-like rat osteosarcoma cell line UMR106

Yuko Katakami; Yoshinobu Nakao; Toshimitsu Matsui; Tamio Koizumi; Kozo Kaibuchi; Yoshimi Takai; Takuo Fujita

doi:10.1016/0006-291X(86)90002-1

Possible involvement of protein kinase C in parathyroid hormone degradation by osteoblast-like rat osteosarcoma cell line UMR106

Yuko Katakami, Yoshinobu Nakao, Toshimitsu Matsui, Tamio Koizumi, Kozo Kaibuchi, Yoshimi Takai, Takuo Fujita

Research output: Contribution to journal › Article › peer-review

Abstract

The effects of 12-O-tetraadecanoyl phorbol-13-acetate (TPA), 1-oleoyl-2-acetyl-glycerol (OAG), and 1-(5-isoquinolinesulfonyl)-2-methylpiperazine (H-7) on the parathyroid hormone (PTH) degrading activity in a PTH-responsive osteoblast-like rat osteosarcoma cell line UMR106 were investigated to assess the role of Ca²⁺-activated, phospholipid dependent protein kinase (protein kinase C) on the degradation of hormones. TPA and OAG, activators of protein kinase C, enhanced the PTH degrading activity dose-dependently, whereas H-7, an inhibitor of protein kinase C, exhibited a dose-dependent inhibition on this activity. These data suggest that protein kinase C activation may enhance PTH degrading activity by UMR106 cells as a possible regulator of PTH degradation.

Original language	English
Pages (from-to)	539-544
Number of pages	6
Journal	Biochemical and Biophysical Research Communications
Volume	143
Issue number	2
DOIs	https://doi.org/10.1016/0006-291X(86)90002-1
State	Published - 1987
Externally published	Yes

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title = "Possible involvement of protein kinase C in parathyroid hormone degradation by osteoblast-like rat osteosarcoma cell line UMR106",

abstract = "The effects of 12-O-tetraadecanoyl phorbol-13-acetate (TPA), 1-oleoyl-2-acetyl-glycerol (OAG), and 1-(5-isoquinolinesulfonyl)-2-methylpiperazine (H-7) on the parathyroid hormone (PTH) degrading activity in a PTH-responsive osteoblast-like rat osteosarcoma cell line UMR106 were investigated to assess the role of Ca2+-activated, phospholipid dependent protein kinase (protein kinase C) on the degradation of hormones. TPA and OAG, activators of protein kinase C, enhanced the PTH degrading activity dose-dependently, whereas H-7, an inhibitor of protein kinase C, exhibited a dose-dependent inhibition on this activity. These data suggest that protein kinase C activation may enhance PTH degrading activity by UMR106 cells as a possible regulator of PTH degradation.",

author = "Yuko Katakami and Yoshinobu Nakao and Toshimitsu Matsui and Tamio Koizumi and Kozo Kaibuchi and Yoshimi Takai and Takuo Fujita",

year = "1987",

doi = "10.1016/0006-291X(86)90002-1",

language = "English",

volume = "143",

pages = "539--544",

journal = "Biochemical and Biophysical Research Communications",

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publisher = "Elsevier B.V.",

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T1 - Possible involvement of protein kinase C in parathyroid hormone degradation by osteoblast-like rat osteosarcoma cell line UMR106

AU - Katakami, Yuko

AU - Nakao, Yoshinobu

AU - Matsui, Toshimitsu

AU - Koizumi, Tamio

AU - Kaibuchi, Kozo

AU - Takai, Yoshimi

AU - Fujita, Takuo

PY - 1987

Y1 - 1987

N2 - The effects of 12-O-tetraadecanoyl phorbol-13-acetate (TPA), 1-oleoyl-2-acetyl-glycerol (OAG), and 1-(5-isoquinolinesulfonyl)-2-methylpiperazine (H-7) on the parathyroid hormone (PTH) degrading activity in a PTH-responsive osteoblast-like rat osteosarcoma cell line UMR106 were investigated to assess the role of Ca2+-activated, phospholipid dependent protein kinase (protein kinase C) on the degradation of hormones. TPA and OAG, activators of protein kinase C, enhanced the PTH degrading activity dose-dependently, whereas H-7, an inhibitor of protein kinase C, exhibited a dose-dependent inhibition on this activity. These data suggest that protein kinase C activation may enhance PTH degrading activity by UMR106 cells as a possible regulator of PTH degradation.

AB - The effects of 12-O-tetraadecanoyl phorbol-13-acetate (TPA), 1-oleoyl-2-acetyl-glycerol (OAG), and 1-(5-isoquinolinesulfonyl)-2-methylpiperazine (H-7) on the parathyroid hormone (PTH) degrading activity in a PTH-responsive osteoblast-like rat osteosarcoma cell line UMR106 were investigated to assess the role of Ca2+-activated, phospholipid dependent protein kinase (protein kinase C) on the degradation of hormones. TPA and OAG, activators of protein kinase C, enhanced the PTH degrading activity dose-dependently, whereas H-7, an inhibitor of protein kinase C, exhibited a dose-dependent inhibition on this activity. These data suggest that protein kinase C activation may enhance PTH degrading activity by UMR106 cells as a possible regulator of PTH degradation.

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DO - 10.1016/0006-291X(86)90002-1

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JO - Biochemical and Biophysical Research Communications

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IS - 2

ER -

Possible involvement of protein kinase C in parathyroid hormone degradation by osteoblast-like rat osteosarcoma cell line UMR106

Abstract

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