Appearance of nuclear protease activity after embryonal carcinoma cells undergo differentiation

B. Scholtz, Kimberly Lamb, Edward Rosfjord, Michelle Kingsley, Angie Rizzino

Research output: Contribution to journalArticle

33 Citations (Scopus)

Abstract

Proteolytic systems are involved via multiple mechanisms in the regulation of gene expression, including tightly controlled metabolism of transcription factors. In this study, we demonstrate that differentiation of mouse embryonal carcinoma cells to parietal endoderm-like cells is accompanied by the appearance of nuclear protease activity. Interestingly, this nuclear-associated protease activity is not observed in the visceral endoderm-like cell line, PSA-5E, or in the differentiated cells derived from both mouse embryonic stem cells and the human embryonal carcinoma cell line NT2/D1. We also determined that this differentiation-associated nuclear protease activity causes proteolysis of a wide range of different transcription factors, including ATF-1, Sp1, NF-YA and B, and octamer-binding proteins Oct-1 and Oct-3. Based on the effects of specific inhibitors, the nuclear protease(s) can be classified as a cysteine protease; however, lack of inhibition by calpastatin and EGTA distinguishes this protease activity from the calpain family of proteases. Given the properties of the differentiation-associated nuclear protease(s), we discuss the possibility that this protease(s) plays a role in the metabolism of transcription factors during the differentiation of specific embryonic cells.

Original languageEnglish
Pages (from-to)420-427
Number of pages8
JournalDevelopmental Biology
Volume173
Issue number2
DOIs
Publication statusPublished - Feb 1 1996

Fingerprint

Embryonal Carcinoma Stem Cells
Cell Differentiation
Peptide Hydrolases
Endoderm
Transcription Factors
Activating Transcription Factors
Cell Line
Calpain
Cysteine Proteases
Egtazic Acid
Gene Expression Regulation
Protease Inhibitors
Proteolysis
Carrier Proteins

ASJC Scopus subject areas

  • Developmental Biology

Cite this

Appearance of nuclear protease activity after embryonal carcinoma cells undergo differentiation. / Scholtz, B.; Lamb, Kimberly; Rosfjord, Edward; Kingsley, Michelle; Rizzino, Angie.

In: Developmental Biology, Vol. 173, No. 2, 01.02.1996, p. 420-427.

Research output: Contribution to journalArticle

Scholtz, B. ; Lamb, Kimberly ; Rosfjord, Edward ; Kingsley, Michelle ; Rizzino, Angie. / Appearance of nuclear protease activity after embryonal carcinoma cells undergo differentiation. In: Developmental Biology. 1996 ; Vol. 173, No. 2. pp. 420-427.
@article{6cbf183bea004975a8c91220c46ce488,
title = "Appearance of nuclear protease activity after embryonal carcinoma cells undergo differentiation",
abstract = "Proteolytic systems are involved via multiple mechanisms in the regulation of gene expression, including tightly controlled metabolism of transcription factors. In this study, we demonstrate that differentiation of mouse embryonal carcinoma cells to parietal endoderm-like cells is accompanied by the appearance of nuclear protease activity. Interestingly, this nuclear-associated protease activity is not observed in the visceral endoderm-like cell line, PSA-5E, or in the differentiated cells derived from both mouse embryonic stem cells and the human embryonal carcinoma cell line NT2/D1. We also determined that this differentiation-associated nuclear protease activity causes proteolysis of a wide range of different transcription factors, including ATF-1, Sp1, NF-YA and B, and octamer-binding proteins Oct-1 and Oct-3. Based on the effects of specific inhibitors, the nuclear protease(s) can be classified as a cysteine protease; however, lack of inhibition by calpastatin and EGTA distinguishes this protease activity from the calpain family of proteases. Given the properties of the differentiation-associated nuclear protease(s), we discuss the possibility that this protease(s) plays a role in the metabolism of transcription factors during the differentiation of specific embryonic cells.",
author = "B. Scholtz and Kimberly Lamb and Edward Rosfjord and Michelle Kingsley and Angie Rizzino",
year = "1996",
month = "2",
day = "1",
doi = "10.1006/dbio.1996.0037",
language = "English",
volume = "173",
pages = "420--427",
journal = "Developmental Biology",
issn = "0012-1606",
publisher = "Academic Press Inc.",
number = "2",

}

TY - JOUR

T1 - Appearance of nuclear protease activity after embryonal carcinoma cells undergo differentiation

AU - Scholtz, B.

AU - Lamb, Kimberly

AU - Rosfjord, Edward

AU - Kingsley, Michelle

AU - Rizzino, Angie

PY - 1996/2/1

Y1 - 1996/2/1

N2 - Proteolytic systems are involved via multiple mechanisms in the regulation of gene expression, including tightly controlled metabolism of transcription factors. In this study, we demonstrate that differentiation of mouse embryonal carcinoma cells to parietal endoderm-like cells is accompanied by the appearance of nuclear protease activity. Interestingly, this nuclear-associated protease activity is not observed in the visceral endoderm-like cell line, PSA-5E, or in the differentiated cells derived from both mouse embryonic stem cells and the human embryonal carcinoma cell line NT2/D1. We also determined that this differentiation-associated nuclear protease activity causes proteolysis of a wide range of different transcription factors, including ATF-1, Sp1, NF-YA and B, and octamer-binding proteins Oct-1 and Oct-3. Based on the effects of specific inhibitors, the nuclear protease(s) can be classified as a cysteine protease; however, lack of inhibition by calpastatin and EGTA distinguishes this protease activity from the calpain family of proteases. Given the properties of the differentiation-associated nuclear protease(s), we discuss the possibility that this protease(s) plays a role in the metabolism of transcription factors during the differentiation of specific embryonic cells.

AB - Proteolytic systems are involved via multiple mechanisms in the regulation of gene expression, including tightly controlled metabolism of transcription factors. In this study, we demonstrate that differentiation of mouse embryonal carcinoma cells to parietal endoderm-like cells is accompanied by the appearance of nuclear protease activity. Interestingly, this nuclear-associated protease activity is not observed in the visceral endoderm-like cell line, PSA-5E, or in the differentiated cells derived from both mouse embryonic stem cells and the human embryonal carcinoma cell line NT2/D1. We also determined that this differentiation-associated nuclear protease activity causes proteolysis of a wide range of different transcription factors, including ATF-1, Sp1, NF-YA and B, and octamer-binding proteins Oct-1 and Oct-3. Based on the effects of specific inhibitors, the nuclear protease(s) can be classified as a cysteine protease; however, lack of inhibition by calpastatin and EGTA distinguishes this protease activity from the calpain family of proteases. Given the properties of the differentiation-associated nuclear protease(s), we discuss the possibility that this protease(s) plays a role in the metabolism of transcription factors during the differentiation of specific embryonic cells.

UR - http://www.scopus.com/inward/record.url?scp=0030039974&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0030039974&partnerID=8YFLogxK

U2 - 10.1006/dbio.1996.0037

DO - 10.1006/dbio.1996.0037

M3 - Article

VL - 173

SP - 420

EP - 427

JO - Developmental Biology

JF - Developmental Biology

SN - 0012-1606

IS - 2

ER -