Pertussis toxin catalyzes the ADP-ribosylation of two distinct peptides, 40 and 41 kDa, in rat fat cell membranes

Craig C. Malbon; Peter J. Rapiejko; J. Adolfo Garciá-Sáinz

doi:10.1016/0014-5793(84)81184-9

Pertussis toxin catalyzes the ADP-ribosylation of two distinct peptides, 40 and 41 kDa, in rat fat cell membranes

Craig C. Malbon
, Peter J. Rapiejko
, J. Adolfo Garciá-Sáinz

Pharmacological Sciences

Stony Brook University

Stony Brook University
Universidad Nacional Autónoma de México

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

22 Scopus citations

Abstract

Pertussis toxin catalyzes the ADP-ribosylation of a single 41-kDa peptide of membranes prepared from rat hepatocytes, S49 mouse lymphoma wild-type and cyc-mutant cells. This 41-kDa peptide has been shown to be the α-subunit of the inhibitory, guanine nucleotide binding regulatory component of adenylate cyclase (N_i). Incubating membranes of rat fat cells with pertussis toxin and [³²P]NAD⁺ radiolabels a 41- and a 40-kDa peptide. Possible homologies between these peptides were investigated by comparing the electrophoretic patterns of proteolytic fragments derived from each of them that are radiolabeled by [³²P]NAD⁺ and pertussis toxin. The 40-kDa substrate for pertussis toxin-catalyzed ADP-ribosylation and the α-subunit of N_i in rat fat cells appear to be homologous, but non-identical peptides.

Original language	English
Pages (from-to)	301-306
Number of pages	6
Journal	FEBS Letters
Volume	176
Issue number	2
DOIs	https://doi.org/10.1016/0014-5793(84)81184-9
State	Published - Oct 29 1984

Keywords

ADP-ribosylation
Inhibitory guanine nucleotide-binding regulatory component
Pertussis toxin
Rat fat cell

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10.1016/0014-5793(84)81184-9

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title = "Pertussis toxin catalyzes the ADP-ribosylation of two distinct peptides, 40 and 41 kDa, in rat fat cell membranes",

abstract = "Pertussis toxin catalyzes the ADP-ribosylation of a single 41-kDa peptide of membranes prepared from rat hepatocytes, S49 mouse lymphoma wild-type and cyc-mutant cells. This 41-kDa peptide has been shown to be the α-subunit of the inhibitory, guanine nucleotide binding regulatory component of adenylate cyclase (Ni). Incubating membranes of rat fat cells with pertussis toxin and [32P]NAD+ radiolabels a 41- and a 40-kDa peptide. Possible homologies between these peptides were investigated by comparing the electrophoretic patterns of proteolytic fragments derived from each of them that are radiolabeled by [32P]NAD+ and pertussis toxin. The 40-kDa substrate for pertussis toxin-catalyzed ADP-ribosylation and the α-subunit of Ni in rat fat cells appear to be homologous, but non-identical peptides.",

keywords = "ADP-ribosylation, Inhibitory guanine nucleotide-binding regulatory component, Pertussis toxin, Rat fat cell",

author = "Malbon, \{Craig C.\} and Rapiejko, \{Peter J.\} and Garci{\'a}-S{\'a}inz, \{J. Adolfo\}",

year = "1984",

month = oct,

day = "29",

doi = "10.1016/0014-5793(84)81184-9",

language = "English",

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journal = "FEBS Letters",

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T1 - Pertussis toxin catalyzes the ADP-ribosylation of two distinct peptides, 40 and 41 kDa, in rat fat cell membranes

AU - Malbon, Craig C.

AU - Rapiejko, Peter J.

AU - Garciá-Sáinz, J. Adolfo

PY - 1984/10/29

Y1 - 1984/10/29

N2 - Pertussis toxin catalyzes the ADP-ribosylation of a single 41-kDa peptide of membranes prepared from rat hepatocytes, S49 mouse lymphoma wild-type and cyc-mutant cells. This 41-kDa peptide has been shown to be the α-subunit of the inhibitory, guanine nucleotide binding regulatory component of adenylate cyclase (Ni). Incubating membranes of rat fat cells with pertussis toxin and [32P]NAD+ radiolabels a 41- and a 40-kDa peptide. Possible homologies between these peptides were investigated by comparing the electrophoretic patterns of proteolytic fragments derived from each of them that are radiolabeled by [32P]NAD+ and pertussis toxin. The 40-kDa substrate for pertussis toxin-catalyzed ADP-ribosylation and the α-subunit of Ni in rat fat cells appear to be homologous, but non-identical peptides.

AB - Pertussis toxin catalyzes the ADP-ribosylation of a single 41-kDa peptide of membranes prepared from rat hepatocytes, S49 mouse lymphoma wild-type and cyc-mutant cells. This 41-kDa peptide has been shown to be the α-subunit of the inhibitory, guanine nucleotide binding regulatory component of adenylate cyclase (Ni). Incubating membranes of rat fat cells with pertussis toxin and [32P]NAD+ radiolabels a 41- and a 40-kDa peptide. Possible homologies between these peptides were investigated by comparing the electrophoretic patterns of proteolytic fragments derived from each of them that are radiolabeled by [32P]NAD+ and pertussis toxin. The 40-kDa substrate for pertussis toxin-catalyzed ADP-ribosylation and the α-subunit of Ni in rat fat cells appear to be homologous, but non-identical peptides.

KW - ADP-ribosylation

KW - Inhibitory guanine nucleotide-binding regulatory component

KW - Pertussis toxin

KW - Rat fat cell

UR - https://www.scopus.com/pages/publications/0021682447

U2 - 10.1016/0014-5793(84)81184-9

DO - 10.1016/0014-5793(84)81184-9

M3 - Article

C2 - 6386524

SN - 0014-5793

VL - 176

SP - 301

EP - 306

JO - FEBS Letters

JF - FEBS Letters

IS - 2

ER -

Pertussis toxin catalyzes the ADP-ribosylation of two distinct peptides, 40 and 41 kDa, in rat fat cell membranes

Abstract

Keywords

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