Identification and partial characterization of phospholipases in isolated adrenocortical cells. The effects of synacthen [corticotropin-(1-24)-tetracosapeptide] and calcium ions

S. G. Laychock; R. C. Franson; W. B. Weglicki; R. P. Rubin

doi:10.1042/bj1640753

Identification and partial characterization of phospholipases in isolated adrenocortical cells. The effects of synacthen [corticotropin-(1-24)-tetracosapeptide] and calcium ions

S. G. Laychock
, R. C. Franson
, W. B. Weglicki
, R. P. Rubin

Pharmacology and Toxicology

Virginia Commonwealth University

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

15 Scopus citations

Abstract

Phospholipase A activity was determined in homogenates and subcellular fractions of trypsin-dispersed cat adrenocortical cells. At pH 7.4 homogenate phospholipid hydrolysis was activated by added Ca²⁺ and inhibited by EGTA. Phospholipid degradation in the presence and absence of Synacthen was completely blocked by EGTA. Ca²⁺-dependent activation of a membrane-bound phospholipase may be a critical control mechanism for regulating the molecular changes taking place during stimulation by Synacthen.

Original language	English
Pages (from-to)	753-756
Number of pages	4
Journal	Biochemical Journal
Volume	164
Issue number	3
DOIs	https://doi.org/10.1042/bj1640753
State	Published - 1977

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10.1042/bj1640753

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title = "Identification and partial characterization of phospholipases in isolated adrenocortical cells. The effects of synacthen [corticotropin-(1-24)-tetracosapeptide] and calcium ions",

abstract = "Phospholipase A activity was determined in homogenates and subcellular fractions of trypsin-dispersed cat adrenocortical cells. At pH 7.4 homogenate phospholipid hydrolysis was activated by added Ca2+ and inhibited by EGTA. Phospholipid degradation in the presence and absence of Synacthen was completely blocked by EGTA. Ca2+-dependent activation of a membrane-bound phospholipase may be a critical control mechanism for regulating the molecular changes taking place during stimulation by Synacthen.",

author = "Laychock, \{S. G.\} and Franson, \{R. C.\} and Weglicki, \{W. B.\} and Rubin, \{R. P.\}",

year = "1977",

doi = "10.1042/bj1640753",

language = "English",

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journal = "Biochemical Journal",

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T1 - Identification and partial characterization of phospholipases in isolated adrenocortical cells. The effects of synacthen [corticotropin-(1-24)-tetracosapeptide] and calcium ions

AU - Laychock, S. G.

AU - Franson, R. C.

AU - Weglicki, W. B.

AU - Rubin, R. P.

PY - 1977

Y1 - 1977

N2 - Phospholipase A activity was determined in homogenates and subcellular fractions of trypsin-dispersed cat adrenocortical cells. At pH 7.4 homogenate phospholipid hydrolysis was activated by added Ca2+ and inhibited by EGTA. Phospholipid degradation in the presence and absence of Synacthen was completely blocked by EGTA. Ca2+-dependent activation of a membrane-bound phospholipase may be a critical control mechanism for regulating the molecular changes taking place during stimulation by Synacthen.

AB - Phospholipase A activity was determined in homogenates and subcellular fractions of trypsin-dispersed cat adrenocortical cells. At pH 7.4 homogenate phospholipid hydrolysis was activated by added Ca2+ and inhibited by EGTA. Phospholipid degradation in the presence and absence of Synacthen was completely blocked by EGTA. Ca2+-dependent activation of a membrane-bound phospholipase may be a critical control mechanism for regulating the molecular changes taking place during stimulation by Synacthen.

UR - https://www.scopus.com/pages/publications/0017702242

U2 - 10.1042/bj1640753

DO - 10.1042/bj1640753

M3 - Article

C2 - 19012

AN - SCOPUS:0017702242

SN - 0264-6021

VL - 164

SP - 753

EP - 756

JO - Biochemical Journal

JF - Biochemical Journal

IS - 3

ER -

Identification and partial characterization of phospholipases in isolated adrenocortical cells. The effects of synacthen [corticotropin-(1-24)-tetracosapeptide] and calcium ions

Abstract

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