Phosphorylation of Soluble Pig Epidermal Proteins by Endogenous Calcium-activated, Phospholipid-dependent Protein Kinase

Overview

Journal Arch Dermatol Res

Specialty Dermatology

Date 1986 Jan 1

PMID 3566339

Citations 2

Authors

H Koizumi

T Aoyagi

A Ohkawara

Affiliations

Soon will be listed here.

Abstract

Endogenous calcium-activated, phospholipid-dependent protein kinase phosphorylates pig epidermal protein. Pig epidermis was homogenized and centrifuged at 30,000 X g for 30 min. The supernatant was incubated with or without calcium and phospholipid. A 97 kD soluble protein from pig epidermis was phosphorylated in the presence of calcium and phosphatidylserine. The phosphorylation reaction occurred immediately. With the use of two-dimensional polyacrylamide gel electrophoresis, it was shown that the 97 kD fragment was a basic protein, and that several small proteins were also phosphorylated. The characterization of these proteins is yet to be undertaken.

Citing Articles

Effect of hexadecane on protein kinase C of pig epidermis.

Koizumi H, Yamanaka K, Ohkawara A Arch Dermatol Res. 1987; 279(6):402-5.

PMID: 3674964 DOI: 10.1007/BF00412627.

Adenylate cyclase induces intracellular Ca2+ increase in single human epidermal keratinocytes of the epidermal sheet as measured by digital imaging microscopy using Fura 2-AM.

Osawa Y, Koizumi H, Fukaya T, Yasui C, Ohkawara A, Ueda T Arch Dermatol Res. 1991; 283(2):91-5.

PMID: 2069417 DOI: 10.1007/BF00371615.

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